Thermal Interference Configure Thermal Interference Activate/Deactivate Thermal Interference Exit Thermal Interference Active Wireless Unit Density Configure Active Wireless Unit Density Activate/Deactivate Active Wireless Unit Density Exit Active Wireless Unit Density Terrain Interference Configure Terrain interference Activate/Deactivate Terrain Interference Exit Terrain Interference Network Equipment Performance Configure Network Equipment Performance Activate/Deactivate Network Equipment Performance Exit Network Equipment Performance Exit Pro-Active Menu In the manual verification mode any changes will not occur until a network engineer verifies the change. A list of suggested changes and the case file that is created will be sent to engineers as the changes are created. In auto correction mode all changes will be made immediately. To reduce any system catastrophes network wide changes are limited to certain tolerances in the diagnostic protocols to eliminate network instability issues. Correlating Mapping Software (2828) No modification to the correlated mapping software 2828 or similar software/hardware is necessary because it is not specifically needed for the proactive software to operate. Correlating Data For Lat/Long Information (2830) No modification to the correlated data for Iat'long information 2830 or similar software/database entry(s) is necessary because its uses are the same in the new configuration that includes the pro-active software 4200. Display Software (2832) The display software 2832 does not need modified because it is used in the same way when the pro-active software is integrated. Primary Analytic Software (2814) The primary analytic software 2814 is the controlling software of the NTS and integrates all the elements into a single software package for a user. From the software, a user may access all features of the system and run either active, passive, or inactive modes. The pro-active system 4200 can integrate in the primary analytic software 2814 in the active and passive modes. However, many features can only be available in the active mode due to the real-time requirements for some pro-active tuning features. Passive mode will always prompt the network engineer before making changes and therefore is unrealistic for most pro-active features. All features are available in the active mode while only the terrain and network features are available in the passive mode. The specific reason is listed below for each feature. Thermal Interference—The ability for the system to react to thermal interference requires a CASE file to be generated frequently to record network performance factors that indicate thermal interference. A typical interval will be at 10-30 minute intervals. The primary analytic software 2814 then submits the changes to the fault diagnosis and correction software 2806 where modifications for pro-active diagnostics are implemented. The frequency in manual mode is to frequent for network engineers to manually approve each time. Active mode allows case files to be sent automatically and modifications to be made also. Active Wireless Unit Density—Active mobile unit density is a rapidly changing factor that changes every second or faster. The processing ability and excess overhead internal trunking affect the time necessary to calculate density. CASE files are generated as fast as possible without affecting other vital processes. The system could not send network engineer approval requests before making changes. Specific changes to accommodate the inclusion of the pro-active features are very specific. First, all CASE files created that are for pro-active features must have a flag set that indicates that fact. The flag allows fast routing of the diagnostics to be considered by new pro-active decision algorithms. Second, the system must first allocate additional processing power and other resources for pro-active features as the active wireless unit density specifically requires additional processing power that can take away from other processes. User Interaction with the Pro-active System The user's primary interaction will be through the display software 2832 and will interact will the additional menu items. As described in the display software section, the user may access these menus to control the new features. Specific interaction and the results are listed below for all the new menu items. Also to be noted, the user may access this system using the existing tuning system's architecture that allows for remote access via intranet, Internet, and other devices. Main Menu Item: Pro-Active Features 5205: The additional menu item appears at the main menu, which is presented to a user after logging on to the system and being authenticated. Thermal Interference 5210: Selecting this feature enables the system to monitor and adapt to thermal interference. Configure Thermal Tuning 5211: The selection allows the user to edit the thermal tuning configuration file. Enable/Disable Thermal Tuning 5212: The selection toggles enable or disable thermal tuning. Exit 5213: Exits the thermal tuning menu. Active Wireless Unit Density 5215: Selecting this feature enables the system to monitor and adapt to active wireless unit density. Configure Active Wireless Unit Density Tuning 5216: The selection allows the user to edit the active wireless unit density tuning configuration file. Enable/Disable Active Wireless Unit Density Tuning 5217: The selection toggles enable or disable active wireless unit density tuning. Exit 5218: Exits the active wireless unit density tuning menu. Terrain Interference 5220: Selecting this feature enables the system to monitor and adapt to terrain interference. Configure Terrain Tuning 5221: The selection allows the user to edit the terrain tuning configuration file. Enable/Disable Terrain Tuning 5222: The selection toggles enable or disable terrain tuning. Exit 5223: Exits the terrain tuning menu. Network Equipment Performance 5225: Selecting this feature enables the system to monitor and adapt to network equipment performance. Configure Network Equipment Tuning 5226: The selection allows the user to edit the network equipment tuning configuration file. Enable/Disable Network Equipment Tuning 5227: The selection toggles enable or disable network equipment tuning. Exit 5228: Exits the network equipment tuning menu. Exit 5230: Exits the pro-active tuning menu. Location Tracking System Detailed Description of the Operations Drawings FIG. 53 FIG. 53 is a flowchart illustrating the process of a user logging into the location tracking system (LTS) 5300. The LTS 5300 may be provided by a wireless service provider, an internet website provider, an asset tracking service, an employee tracking service, a personal tracking service or other types of service providers. The user accesses the LTS 5300 thru an internet 3202 website, a wireless interface, a wireless service provider, publicly switched telephone network 138, a fax on demand service, an automated telephone system, a laptop/desktop computer 2910, a PDA, a wireless device 104, or other types of devices. To begin the login process, the LTS 5300 prompts the user to enter a username and password 5302. The LTS 5300 then waits for the user to respond with a username and password 5304. If the user responds 5304, the LTS's 5300 internal CPU and computer 2816 logs the entered username and password 5304 into its internal storage memory 5306. The LTS 5300 checks the LTS's 5300 membership database for the username and password 5304. If the LTS 5300 finds the user's record 5312, the user then enters the desired telephone number, FIG. 53, BOX 5314. FIG. 54 displays the complete entry process. If the user's records cannot be found 5312, the LTS 5300 informs the user that there is a problem with the username or password 5302, and the user is returned to FIG. 53, BOX 5302, as shown in FIG. 53, BOX 5316. The LTS 5300 then prompts the user to enter username and password 5302. If the user does not enter a username and/or password 5304, the LTS 5300 prompts the user to become a user of record 5312 by entering personal information and billing information into the LTS 5318. The LTS 5300 then waits for the user to enter personal and billing information 5320. If the user does not enter personal and billing information within a specified period of time 5320, the user is logged off 5322 the LTS 5300, sent to help menu or forwarded to a service agent or operator 5322, depending on the configuration of the LTS 5300 settings and the users choice. If the user enters personal and billing information 5320, the LTS's 5300 internal CPU and computer 2816 logs the personal information and billing information into its internal storage memory 5306. The LTS 5300 then attempts to verify the user's personal information and billing information 5326 by placing a call through a modem to the LTS's 5300 merchant credit card services account and charges to the users credit card 5326. If the user's personal and billing information can be verified 5328, and the users credit card is billed, the LTS 5300 establishes a user record 5312 by transferring the logging the personal and billing information from the internal storage memory 5306 to the LTS's membership database 5308. The user is then enters the desired telephone number, FIG. 53, BOX 5332. FIG. 54 displays the complete entry process. If the user's personal information and billing information cannot be verified 5328, the user is notified is a problem with their personal information and billing information and returned to FIG. 53, BOX 5318, as shown in FIG. 53, BOX 5330. The user login, personal information and billing information are optional features of this embodiment. The LTS 5300 may be provided at no charge, or offered as a value added feature in conjunction with other services. Whoever, if the user wishes to utilize all the features of the LTS 5300, a login is required to enable the LTS 5300 to retrieve and access the user's settings and user's entries from the LTS's 5300 memory. FIG. 54 FIG. 54 illustrates the initial entry of a phone number that the user wishes to track. Once the user has logged onto the LTS 5300, the internal computer and CPU 2816 checks the users records 5312 if the user has a phonebook saved in the membership database 5400. If the user has phonebook entries saved as part of the user's records, the LTS 5300 gives the user menu choices, 5404. This process is illustrated in FIG. 55. If the user has not previously saved an entry into the phonebook 5400, the LTS 5300 then prompts the user to enter the telephone number or identification information of the wireless device 104 the user wishes to locate and/or track 5402. The LTS 5300 then waits a specified period for the user to enter a telephone number 5406. If the user enters a telephone number for a wireless device 104 that they wish to track, the LTS 5300 logs the user's entry into the internal storage memory 5306. The LTS 5300 then queries a user location database(ULD) 900, user location database coordinator(ULDC) 908, access users case files 2820, queries the base station controller (BSC) 206 of a wireless network 100 with the LTS's device location software 2808 for the lat/long coordinates of the wireless device 104 being tracked, Global Positioning System (GPS) Information, or other means of obtaining locations of wireless devices 5406. The use of ULD 900, ULDC 908, and other location means is disclosed (offered only as an example of location means) in a Provisional Patent Application Ser. No. 60/327,327; and was files on Oct. 4, 2001. If the wireless device 104 is not located, the user is informed of the problem, and returned to FIG. 54, BOX 5402, as illustrated in FIG. 54, BOX 5416. If the wireless device 104 is located 5414, the LTS 5300 receives the lat/long coordinates and displays the lat/long coordinates to the user in their choice of formats. For example, the location may by overlaid on a display screen 2836 along with a street map overlay 5418, a map of the overlaid screens may be faxed to a user via a fax on demand service, the location may be converted to a postal address 5422 or cross-street using the LTS's postal address conversion software 5422 and displayed on a screen 2836, faxed to a user, or read to a user over the phone using the LTS's 5300 automated answering system and voice text read-up software 5426. Once the wireless device 104 has been located and displayed 5418, the LTS 5300 prompts the user to enter the specific wireless device 104 into a user phonebook by selecting “phonebook” 5428. If the user selects “phonebook” 5428 to save the entry to their Phonebook 5430, the user is forwarded to the phonebook menu section, FIG. 56, BOX 5600, as illustrated in FIG. 54, BOX 5432. If the user does not select to save the current entry to their phone book 5330, the user is forwarded to the phonebook section of the user's choice menu FIG. 55, BOX 5500, as illustrated is FIG. 54, BOX 5434. When prompted by the LTS 5406, if the user does not enter a phone number of the wireless device 104 they wish to locate and/or track, the LTS 5300 prompts the user to enter other identification information such as a persons name, company name, or other identifying information 5438. If the user does not enter identification information within a specified period of time 5438, the LTS 5300 logs off the user 5440. If the user enters identification information 5438, the LTS 5300 logs the user's entry, and the identification information is then cross referenced against the LTS's Cuss-Cross Phonebook database 2812 or other supplies sources to obtain the phone number for the desired wireless device 5442. If the LTS 5300 finds the phone number 5410, the LTS 5300 logs the phone number 5406, and the location process continues as described as if the user entered the number described above 5408. If the phone number of the wireless device 104 cannot be located in the Criss-Cross Phonebook database 2812, the LTS 5300 informs the user the number could not be found and prompts the user to enter a phone number 5412. FIG. 55 FIG. 55 illustrated the processing of the user's choice menu 5502. The user's choice menu's 5502 physical realization may be in the form of a display screen 2836 navigated by a mouse, keyboard/keypad, interactive display screen, voice recognition or other forms of selection. The user's choice menu 5502 also may be an automated answering system and could be navigated by voice recognition, a keyboard/keypad or other forms of selection. Initially, the LTS 5300 prompts the user to enter a phone number of a wireless device 104 that the user wants to locate or track by selecting ‘locate” 5500. The LTS 5300 waits a specified period for the user to select ‘locate” 5504. If the user responds by selecting ‘locate” 5504, the LTS 5300 asks the user to enter a phone number by the process described in FIG. 54, FIG. 55, BOX 5506. If the user does not respond within the specified period of time 5504, the LTS 5300 prompts the user to select a phonebook entry he wishes to locate 5508. The LTS 5300 then waits a specified period for the user to select “phonebook” 5530. If the user responds by selecting “phonebook” 5330, the user selects the building he wants to display 5510. FIG. 56 describes the process. If the user does not respond within the specified period of time 5530, the LTS 5300 prompts the user to add, delete or edit a phonebook entry(ies) to a wireless device(s)1 04 that the user wants to locate/track by selecting ‘Add, Delete or Edit” 5512. The LTS 5300 then waits a specified period for the user to select “Add, Delete, or Edit” 5514. If the user responds by selecting “Add, Delete or Edit” 5514, the LTS 5300 prompts the user to add, delete, or edit phonebook entries 5516. FIG. 57 describes the process. If the user does not respond within the specified period 5514, the LTS 5300 prompts the user to view selected businesses, government buildings, and/or homes on the display screen by selecting “buildings” 5518. The LTS 5300 then waits a specified period for the user to select “buildings” 5520. If the user responds by selecting “buildings” 5520, the LTS 5300 prompts the user to select buildings to display 5522. FIG. 58 describes the process to select buildings for display. If the user does not respond within the specified period 5520, the LTS 5300 prompts the user to view a history of call/location/tracking history of phonebook entry(ies) to a wireless device(s) 104 that the user wants to locate/track by selection “view history” 5524. The LTS 5300 then waits a specified period for the user to select “view history” 5526. If the user responds by selecting “view history” 5526, the LTS 5300 forwards the user to the view history process 5528. FIG. 67 illustrates the view history process. If the user does not respond within the specified period of time 5526, the LTS 5300 prompts the user to print a history of call/location history of phonebook entry(ies) to a wireless device(s)104 by selecting “print history” 5530. The LTS 5300 then waits a specified period for the user to select “print history” 5532. If the user responds by selecting “print history” 5532, the LTS 5300 forwards the user to the print history process 5534. FIG. 68 illustrates the print history process. If the user does not respond within the specified period of time 5530, the LTS 5300 prompts the user to add a history of call/location/tracking history to the wireless service bill by selecting “add to bill” 5536. The LTS 5300 then waits a specified period for the user to select ‘add to bill” 5538. If the user responds by selecting ‘add to bill” 5539, the LTS 5300 executes the process to add the call/location report to the wireless service bill 5540. FIG. 69 illustrates the process to add the call/location report to the wireless service bill. If the user does not respond within the specified period 5538, the LTS 5300 logs the user off 5542. FIG. 56 FIG. 56, illustrates the process of entering and selecting phonebook entries. When the user is transferred to the “phonebook” section, the LTS 5300 first queries the user records 5312 to determine if the user is currently locating/tracking the location of a wireless device 5600. If the LTS 5300 is currently locating/tracking a wireless device 5600, the LTS 5300 logs the current entry into the phonebook 5602. The LTS 5300 then displays the user's phonebook including the new entry 5604. Once the LTS 5300 displays the phonebook 5604, the LTS 5300 prompts the user to select phonebook entries that they would like to locate/track 5606. The LTS 5300 then waits a specified period for the user to respond 5608. If the user selects phonebook entries to be located/tracked 5608, the LTS 5300 logs the selected phonebook entries and retrieves the location of the wireless devices 104 requested by the user 5610. The LTS 5300 retrieves the lat/long locations of the wireless devices 104 by querying a ULD 900, a ULDC 908, by querying case files 2820 containing lat/long of wireless devices 104, by querying the wireless network's BSC 206 or by other location means. The LTS 5300 then plots the lat/long of the located wireless devices 104 and overlays the locations onto a street/topographic map 5612. If the LTS 5300 is not able to locate a selected entry, the LTS 5300 notifies the user that the entry(ies) could not be located 5614. The LTS 5300 then prompts the user to select businesses, government buildings and/or private homes to be added to the display screen by selecting “buildings” 5518. The LTS 5300 then waits a specified period for the user to select “buildings” 5520. If the user selects “buildings” 5520, the LTS 5300 prompts the user to select buildings for display 5522. FIG. 58 illustrates the process. If the user does not select “buildings” 5520, the user is forwarded to the user choice menu 5502. If the LTS 5300 is not currently locating/tracking a wireless device 104 when the user logs into the “phonebook” menu 5600, the LTS 5300 determines if the user has previously established a phonebook containing stored entries, within the user's record 5312. If the user does have a phonebook within the user's record 5312, the LTS 5300 displays the user's phonebook 5616, and the LTS 5300 permits the user to select and locate wireless devices 104 from their phonebook 5606. If the user does not have a phonebook as part of the user's records 5312, the user is informed that no phonebook records are contained in the user's record 5618, and the LTS 5300 forwards the user to the user's choice menu 5502. FIG. 57 FIG. 57 illustrates the “add, delete, and editing phonebook entries menu”. The diagram illustrates the process, which allows users to add, delete, and edit phonebook entries. The LTS 5300 prompts the user to add a new entry to the phonebook by selecting “add” 5700. The LTS 5300 then waits a specified period for the user to respond by selecting “add” 5702. If the user responds by selecting “add” 5702 a new entry, the LTS 5300 prompts the user to enter a telephone number or identification information 5704, described in FIG. 54. If the user does not respond 5702, the LTS 5300 then prompts the user to delete an existing entry in the phonebook by selecting “delete” 5706. The LTS 5300 then waits a specified period for the user to respond selecting “delete” 5708. If the user responds by selecting “delete” 5708, the LTS 5300 allows the user to delete a selected phonebook entry and the LTS 5300 logs the change 5710 to the user's record 5312. The LTS 5300 then forwards the user to the user's choice menu 5502. If the user does not respond within the specified period of time 5708, the LTS 5300 then prompts the user to edit an existing entry in the phonebook by selecting “edit” 5712. The LTS 5300 then waits a specified period for the user to respond selecting ‘edit” 5712. If the user responds by selecting ‘edit” 5714, the LTS 5300 allows the user to edit a selected phonebook entry and the LTS 5300 logs the change 5716 to the user's record 5312. The LTS 5300 forwards the user to the user's choice menu 5502. If the user does not respond within the specified period of time 5714, the LTS 5300 forwards the user to the user's choice menu 5502. FIG. 58 FIG. 58 illustrates the process of selection “buildings” that will be displayed on the display screen 2836. The LTS 5300 determines the user's current location 5800. The LTS 5300 prompts the user to enter or select a city by city name or zip code if the default city is not desired 5802. The LTS 5300 waits for the user to select a city 5804. If the user selects a different city 5804, the LTS 5300 logs the user's choice and makes it the default city 5806. After the user selects a city, the LTS 5300 checks if the user has entries in the building memory 5808. If the user does not have entries in the building memory 5808, the LTS 5300 sends the user to the building memory choice menu 5810, described in FIG. 59. If the user has entries in the building memory 5808, the LTS 5300 asks the user if he wants to select “building memory” 5812. The LTS 5300 waits for user response 5814. If the user does not select “building memory” 5814, the LTS 5300 sends the user to the building memory choice menu 5814 described in FIG. 59. If the user selects “building memory” 5814, the LTS 5300 displays the user's building memory and prompts the user to select entries 5816. The LTS 5300 waits for a user response 5818. If the user selects entries, the selected entries are display on the display screen 5820. Then the LTS 5300 sends the user to the building memory choice menu 5810 described in FIG. 59. If the user does not select any entries 5818, the LTS 5300 sends the user to the building memory choice menu 5810 described in FIG. 59. FIG. 59 The building memory user's choice menu 5902 allows the user to add, select, and delete entries to their building memory. The LTS 5300 prompts the user to select a business, government office or home by selection “Display Building” 5900. If the user selects “display building” 5902, the LTS 5300 prompts the user to enter the listing they want to display 5904. If the user does not select “display building” 5902, the LTS 5300 prompts the user to add an entry to the building memory by selecting “add” 5906. If the user selects “add” 5908, the LTS 5300 forwards the user to the add building process 5910. FIG. 60 illustrates the add building process. If the user does not select add 5914, the LTS 5300 prompts the user to delete an entry in the building memory by selecting “delete” 5912. If the user selects “delete” 5914 , the LTS 5300 logs the user's choice and displays the user's building memory 5916. The LTS 5300 prompts the user to select the entry he wants to delete 5918. If the user selects an entry 5920, the LTS 5300 logs the user's choice and deletes the entry from the building memory 5922. The LTS 5300 then prompts the user to either go to the user's choice menu or log off 5924. If the user selects to go to the user's choice menu 5926, the LTS 5300 returns the user to the user's choice menu 5502. If the user chooses to logoff 5926, the LTS 5300 logs the user off the system 5930. If the user does not select an entry to delete 5930, the LTS 5300 then prompts the user to either go to the user's choice menu or log off 5924. If the user selects to go to the user's choice menu 5926, the LTS 5300 returns the user to the user's choice menu 5502. If the user chooses to logoff 5926, the LTS 5300 logs the user off the system 5930. If the user does not select the “delete” option 5912, the LTS 5300 then prompts the user to either go to the user's choice menu or log off 5924. If the user selects to go to the user's choice menu 5926, the LTS 5300 returns the user to the user's choice menu 5502. If the user chooses to logoff 5926, the LTS 5300 logs the user off the system 5930. FIG. 60 FIG. 60 continues the building memory process and illustrates the process to add an entry to the building memory. The LTS 5300 prompts the user to add a new building by selecting “name”, “category”, ‘address“, or “phone number” 6000. If the user selects “name” 6002, the LTS 5300 adds the entry by name 6004. FIG. 63 illustrates the process to add an entry by name. If the user selects “category” 6006, the LTS 5300 adds the entry by category 6008. FIG. 64 illustrates the process to add an entry by category. If the user selects “address” 6010, the LTS 5300 adds the entry by address 6012. FIG. 65 illustrates the process to add an entry by address. If the user selects “phone number” 6014, the LTS 5300 adds the entry by phone number 6016. FIG. 66 illustrates the process to add an entry by phone number. If the user does not select any menu option 6014, the LTS 5300 returns the user to the user's choice menu 5502. FIG. 61 FIG. 61 illustrates the process for categorizing the building memory. The LTS 5300 logs the user's choice and prompts the user to enter the desired listing by name, category, address or phone number 6100. If the user enters a listing 6102, the LTS 5300 adds a “listing” 6104. FIG. 62 illustrates the add “listing” process. If the user does not enter a “listing” 6102, the LTS 5300 prompts the user to enter the name of the desired entry 6106. If the user enters a name 6108, the LTS 5300 adds the entry by name 6110. FIG. 63 illustrates the process to add an entry by name. If the user does not enter name 6108, the LTS 5300 prompts the user to enter a category 6112. If the user enters a category 6114, the LTS 5300 adds the entry by category 6116. FIG. 64 illustrates the process to add an entry by category. If the user does not enter a category 6114, the LTS 5300 prompts the user to enter an address 6118. If the user enters an address 6120, the LTS 5300 adds the entry by address 6122. FIG. 65 illustrates the process to add an entry by address. If the user does not enter an address 6120, the LTS 5300 prompts the user to enter a phone number 6124. If the user enters a phone number 6126, the LTS 5300 adds the entry by phone number 6128. FIG. 66 illustrates the process to add an entry by address. If the user does not enter a phone number 6126, the LTS 5300 returns the user to the user’ choice menu 5502. FIG. 62 FIG. 62 displays the process to enter a “listing” to the building memory. The LTS 5300 logs the user's entered listing and searches the criss-cross phonebook with the lat/long correlation 2810 or address coordinates for all matching entries 6200. If the listing is not found 1005, the LTS notifies the user the listing is not found 6202 and the user is sent to the user choices menu 5502. If the listing is found 6202, the LTS 5300 displays all the entries that contain the entered “listing” and the LTS 5300 prompts the user to select the desired entry 6206. If the user does not select a listing 6208, the user is sent to the user choices menu 5502. If the user selects an entry 6208, the LTS 5300 displays the selected listing on the display screen 2836 with the following information: name, category of listing, address, and phone number. The LTS 5300 plots and labels the listing location on a street map with the location of the wireless devices 6210. The LTS 5300 prompts the user if he wants to save the listing in the building memory 6212. If the user does not save the listing 6214, he is sent to the user choices menu 5502. If the user saves the listing, the LTS 5300 saves the listing in the building memory 6216, and the LTS 5300 returns the user to the building memory user's choice menu 6218. FIG. 63 FIG. 63 displays the process to enter a “name” to the building memory. The LTS 5300 logs the user's entered name and searches the criss-cross phonebook with the lat/long correlation 2812 or address correlation's for all matching entries 6300. If the name is not found 6302, the LTS 5300 notifies the user the listing is not found 6304 and the user is sent to the user choices menu 5502. If the listing is found 6302, the LTS 5300 displays all the entries that contain the entered “name” and the LTS 5300 prompts the user to select the desired entry 6306. If the user does not select a listing 6308, the user is sent to the user choices menu 5502. If the user selects an entry 6308, the LTS 5300 displays the selected listing on the display screen 2836 with the following information: name, category of listing, address, and phone number. The LTS 5300 plots and labels the listing location on a street map with the location of the wireless devices 6310. The LTS 5300 prompts the user if he wants to save the listing in the building memory 6212. If the user does not save the listing 6214, he is sent to the user choices menu 5502. If the user saves the listing, the LTS 5300 saves the listing in the building memory 6316, and the LTS 5300 and the LTS 5300 returns the user to the building memory user's choice menu 6218. FIG. 64 FIG. 64 displays the process to enter a “category” to the building memory. The LTS 5300 logs the user's entered listing and searches the criss-cross phonebook with the 1st/long correlations 2812 or address coordinates for all matching entries 6400. If the listing is not found 6402, the LTS 5300 notifies the user the listing is not found 6404 and the user is sent to the user choices menu 5502. If the listing is found 6204, the LTS 5300 displays all the entries that contain the entered “category” and the LTS 5300 prompts the user to select the desired entry 6406. If the user does not select a listing 6408, the user is sent to the user choices menu 5502. If the user selects an entry 6408, the LTS 5300 displays the selected listing on the display screen 2836 with the following information: name, category of listing, address, and phone number. The LTS 5300 plots and labels the listing location on a street map with the location of the wireless devices 6410. The LTS 5300 prompts the user if he wants to save the listing in the building memory 6212. If the user does not save the listing 6214, he is sent to the user choices menu 5502. If the user saves the listing, the LTS 5300 saves the listing in the building memory 6216, and the LTS 5300 and the LTS 5300 returns the user to the building memory user's choice menu 6218. FIG. 65 FIG. 65 displays the process to enter a “address” to the building memory. The LTS 5300 logs the user's entered listing and searches the criss-cross phonebook with the latllong correlations 2812 or address coordinates for all matching entries 6500. If the listing is not found 6502, the LTS 5300 notifies the user the listing is not found 6504 and the user is sent to the user choices menu 5502. If the listing is found 6502, the LTS 5300 displays all the entries that contain the entered “address” and the LTS 5300 prompts the user to select the desired entry 6506. If the user does not select a listing 6508, the user is sent to the user choices menu 5502. If the user selects an entry 6508, the LTS 5300 displays the selected listing on the display screen 2836 with the following information: name, category of listing, address, and phone number. The LTS 5300 plots and labels the listing location on a street map with the location of the wireless devices 6510. The LTS 5300 prompts the user if he wants to save the listing in the building memory 6212. If the user does not save the listing 6214, he is sent to the user choices menu 5502. If the user saves the listing, the LTS 5300 saves the listing in the building memory 6216, and the LTS 5300 and the LTS 5300 returns the user to the building memory users choice menu 6218. FIG. 66 FIG. 66 displays the process to enter a “phone number” to the building memory. The LTS 5300 logs the user's entered listing and searches the crisscross phonebook with the lat/long correlations 2812 or address coordinates for all matching entries 6600. If the listing is not found 6602, the LTS 5300 notifies the user the listing is not found 6604 and the user is sent to the user choices menu 5502. If the listing is found 6602, the LTS 5300 displays all the entries that contain the entered “phone number” and the LTS 5300 prompts the user to select the desired entry 6606. If the user does not select a listing 6608, the user is sent to the user choices menu 5502. If the user selects an entry 6608, the LTS 5300 displays the selected listing on the display screen 2836 with the following information: name, category of listing, address, and phone number. The LTS 5300 plots and labels the listing location on a street map with the location of the wireless devices 6610. The LTS 5300 prompts the user if he wants to save the listing in the building memory 6212. If the user does not save the listing 6214, he is sent to the user choices menu 5502. If the user saves the listing, the LTS 5300 saves the listing in the building memory 6216, and the LTS 5300 and the LTS 5300 returns the user to the building memory user's choice menu 6218. FIG. 67 The user's history report may be generated by building and/or retrieving case files that are generated at the time that communications are sent/received by the wireless device 104, and which contain the location of the wireless device 104 at the time of the communication. This tracking method is best for tracking wireless devices 104, which are used, on a frequent basis during the day. Alternatively, the user's history report may be generated by building and/or retrieving case files by periodically (every hour, twice a day etc.) querying a user location database 900, user location database coordinator 908, or querying the wireless networks base station controller 118-A or other network components, for the location of the wireless device 104. This alternative method of generating a user's history report would be preferred for locating/tracking wireless devices 104 that are not used frequently. If a wireless device 104 only receives one or two communications a day, a periodic report (every hour, etc.) would give a more complete report of the location of the wireless device 104 through the day. A third method of generating a user's history report is to combine the two methods mentioned above. This involves reporting case files with call/location generated when the wireless device 104 sends/receives a communication, combined with the periodic case file, which is generated periodically (every hour, etc., depending on the selected monitoring period set by the owner of the wireless device 104, the user of the LTS 5300, or the wireless service provider). FIG. 67 shows the process to display call history report. The LTS 5300 prompts the user to select a range of time the report will cover 6700. If the user does not select a time range 6702, the LTS 5300 will send the user to the user choice menu 5502. If the user selects a time range 6702, the LTS 5300 logs the time range 6704 and the LTS 5300 queries the ULD 900 or case file database that correspond with the selected phonebook entries and time range 6706. The ULD 900, GPS, or the BSC 118-A determine the lat/long of the case files 6708. The LTS 5300 correlation software converts the latitude and longitude of the case files to a postal address, cross street, business, government, house name 6710. The LTS 5300 prompts the user to select how he wants to sort the call history 6712. The user can sort the call history by: time of call, location of call, calling party, or wireless phone number 6712. If the user does not select a sort type 6714, the default sort type is used 6716. Otherwise, the LTS 5300 logs the users choice and displays the transcribed postal address in the selected order with the corresponding phone number, length of call, time of call, and calling party 6718. The LTS 5300 then prompts the user to select an individual call record that the user desires to plot on a map 6720. If the user does not select a call record 6722, the LTS 5300 asks the user if he wants to print the call history 6724. If the user selects a call record 6722, the LTS 5300 logs the choice and overlays the calls latitude and longitude location on a topographic street map 6726. The LTS 5300 then prompts the user if he wants to return to the call/location display screen 6728. If the user selects to return to the call/location display screen 6730, the LTS 5300 prompts the user to select a time range for the call history report 6732. Otherwise, the LTS 5300 returns the user to the users choice menu 5502. FIG. 68 FIG. 68 shows the process to print call history report. The LTS 5300 prompts the user to select a range of time the report will cover 6800. If the user does not select a time range 6802, the LTS 5300 will send the user to the user choice menu 5502. If the user selects a time range 6802, the LTS 5300 logs the time range 6804 and the LTS 5300 queries the ULD 900 or case file database that correspond with the selected phonebook entries and time range 6806. The ULD 900, GPS, or the BSC 206 determine the latllong of the case files 6808. The LTS 5300 correlation software converts the latitude and longitude of the case files to a postal address, cross street, business, government, house name 6810. The LTS 5300 prompts the user to select how he wants to sort the call history 6812. The user can sort the call history by: time of call, location of call, calling party, or wireless phone number. If the user does not select a sort type 6814, the default sort type is used 6816. Otherwise, the LTS 5300 logs the user's choice and displays the transcribed postal address in the selected order with the corresponding phone number, length of call, time of call, and calling party 6818. The LTS 5300 then prompts the user if he wants to print the history report 6820. If the user does not print the history report 6822, the LTS 5300 prompts the user if he wants to include the call history report on the user's phone bill 6826. If the user prints the call history report 6822, the LTS 5300 sends the report to the desired printer 6824. The LTS 5300 then prompts the user if he wants to include the call history report on the user's phone bill 6826. If the user selects to include the report with the user's phone bill 6828, the LTS 5300 includes the call history report in the user's phone bill 6832. Otherwise, the LTS 5300 returns the user to the users choice menu 5502. FIG. 69 FIG. 69 displays the process to include the call history report in the user's phone bill. The LTS asks the user if he wants the call history report included in the billing statement. If the user chooses not to add the call history report 6902, the LTS 5300 returns the user to the user's choice menu 5502. If the user chooses to add the call history 6902, the LTS 5300 logs the user's choice 6904, and prompts the user to enter authorization information to verify he is the owner of the wireless device 6906. If the user does not enter authorization information 6908, the LTS 5300 returns the user to the user's choice menu 5502. If the user enters authorization information 6908, the LTS 5300 logs the authorization information and matches the information with wireless providers records 6910. If the authorization information does not match the records 6914, the LTS 5300 notifies the user of the mismatch 6916, and returns the user to the user's choice menu 5502. If the information matches 6914, the LTS 5300 prompts the user to approve the charges added to the bill for the call history report 6918. If the user does not approve the charges 6920, the LTS 5300 returns the user to user's choice menu 5502. If the user approves the charges 6920, the LTS 5300 logs the user's choice and instructs the wireless service to include the call location history report to the bill 6922. The LTS 5300 prompts the user if he wants to return the user's choice menu 6924. If the user selects to returns to the user's choice menu 6926, the LTS 5300 returns the user to the user's choice menu 5502. Otherwise the user is logged off the LTS 6930. Location Tracking System; Summary The location tracking system 5300 is a method of determining the location and then tracking a single or plurality of wireless devices 104 on a given wireless device network(s) 100 based on a criterion provided by a user. Based on this criterion a log is created that record the location and network status of any wireless device 104 fitting the criterion. These logs are recorded to a database and then later transferred to a user database for storage on a local server database. Accessing the database can be accomplished remotely or locally. Local access is from local service terminals on the network or mainframe. Remote access can be from a TCP/IP, IPX, Dial-up, remote server SQL Queries, and other listed methods. This allows for third party vendors to have access to the said primary embodiment 2800 features and use the technology to create product support and technological spin-offs. Examples of technological spin-offs would be; a cellular phone bill that gives the user's geographic location at the time of each logged call, an internet 3202 website that would allow business owners to track the location of employees or equipment comprising a wireless device 104, or a geographical advertising system (GAS) that would allow targeted advertising based on the location of the user of a wireless device 104. Many other technological spin-offs are also possible. Tracking the wireless devices 104 can be done by utilizing a user location database (ULD) 900, GPS data from the phone, direct analysis of the network communication parameters, or by other third party methods. When a wireless device 104 is not located on a local server a user location database coordinator (ULDC) 908 or other system can be used to discover the location of a device to allow a log to be created. Logs can be created and appended as a wireless device 104 roams a local wireless device network 100 or a remote wireless device 1900 network. Using TCP/IP and ATM connections, servers for discreet wireless device networks 100 can communicate together and allow seamless network interoperability. This allows the tracking logs to record the location of wireless devices 104 on a plurality of wireless device networks 100 having had a request generated from any network connected to the deemed wide-area network. Internet 3202 Protocol 6 and 7 should allow this to become even more practical. Notification from the server to external programs, users, wireless devices 104 is a native capability of the said primary embodiment 2800. The messages can be sent alerting the said wireless device 104 of a system event. A user sets up this event when the log setup process begins by the user. The user can have the system send an alert based on a criterion such as the completion of a log. The advantage is that an alert can be sent to external programs triggering an external event. This allows third party software to use this to create a new technology and create a new product for their consumers. An example is for a wireless device user 102 to be tracked and logged. A message could be sent via SMS (simple message system) to a prescribed wireless device 104 when that wireless device 104 being tracked leaves a certain geographic region. The system would for example allow a parent to be alerted when their child is going somewhere they shouldn't. The primary embodiment 2800 also describes a method for allowing a large volume of users to access the logging and tracking database. The primary embodiment 2800 describes the method that allows a large volume of tracking to be done and logged simultaneously. By making separate database structures on separate hardware entities the load is divided into active database buffers were logs being created are stored, to a separate structure where inactive logs are saved for users. A graphical interface and display protocol database 3004 is described that allows users to interact with the system and remotely retrieve meaningful representations of the data from the logs. Tracking logs simply contain data that describes network parameters as well as geographic and timing information. Alone this data is simply text. The said graphical display allows a useful extraction of the data to be represented. Multiple logs can be shown with data overlays including maps, topological information 4160, and other network parameters. The physical structure for the wireless device network 100 is described in including the database hardware implementation, the networking implementation and the processing implementation. Examples of appropriate hardware and peripherals are given. Amounts of storage and hardware configurations are described. RAID architecture is listed and the preferred level of RAID deployment is also suggested for various deployments of the primary embodiment 2800 based on budget and performance. A major user interaction of the primary embodiment 2800 is envisioned, but not excluded to, the ability to track and record wireless devices 104 that users have administrative control over. This would allow them to monitor, record, and review were and how their wireless devices 104 are used. Uses could be to monitor the location of workers, children, demographically defined users, and other types. Monitoring wireless devices 104 by demographics has the unique ability to allow business to discover the location and moving habits of its customers. An example of this would be for a company to track all wireless devices 104 based on a set of demographic criterion that matches its target audience. The system would then track all wireless devices 104 matching those criterion and record the locations to a server database log, allowing the company to find a location to possibly build a new store that would maximize it exposure to its target customers. Another us would be for a company to search for customers (based on a local mailing list of customers phone numbers) and when the customer enters a region (geographic distance) from the store location, a log would be created. A page or message could be sent to an external program indicating the event. A subsequent push' message technology such as SMS could be used to deliver content to the wireless device 104 in the form of an advertisement. This technology would allow the company to restrict its advertising to valid customers of interest and reduce the costs of advertising. Description Of Embodiments Device Tracking and Logging The wireless device 104 tracking and logging option of the location tracking system 5300 is used to monitor and record the location (latitude/longitude/altitude) of a wireless device 104 over a period of time. The feature requires the use of the device location software 2808, location database manager904, as their associated components. For a wireless device 104 to be tracked it must be able to be recognized by the system. The device location software 2808 allows for a wireless device 104 (wireless device 104, 2 way pager, satellite phone, GPS enabled device, wireless LAN device, other) to be tracked as long as the system can access the control hardware/software for the appropriate wireless device network 100. For GPS satellite network 114 enabled devices, certain considerations must be taken into account due to the nature of multi-path in cellular environments. Multi-path is the error caused by reflected signals entering the front end of the receiver and masking the real correlation peak. In this case, signal from the GPS satellite network 114 to the wireless device 104. The effects tend to be more pronounced in a static receiver near large reflecting surfaces, where 15 m in or more in ranging error can be found in extreme cases. In this case, a wireless device 104 slightly indoor or in a city between buildings would be relevant. Monitor or reference stations (in this case the BTS 118-A of the wireless device network 100) require special care in placing (the BTS's 118-A) to avoid unacceptable errors. The first line of defense is to use the combination of antenna 2430 cut-off angle and antenna 2430 location that minimizes this problem. It however is not always possible in a wireless device network 100 and can cause undue or uneven accuracy in location ability over a wireless device network 100. A second approach is to use so-called “narrow correlatoe” receivers that tend to minimize the impact of multi-path on range tracking accuracy's. The approach does not apply to wireless device networks 100 and should not be used. Overall the effects of GPS satellite network 114 error still allow the most accurate location results. But consideration for its inaccuracies should be noted. The wireless devices 104 that can be tracked are limited to the wireless device networks 100 the device location software 2808 is attached to. A noted exception is when a ULD 900 or ULDC network 1600 (or similar) is available for the system to query. In this case the wireless device 104 will be able to retrieve the location of any wireless device 104 that exists in the database regardless of the type of network it is operating on. The design would be preferred because it creates a type of universal standard that would allow a plurality of wireless devices 100 to be tracked over a variety of networks. A further requirement for the wireless device 104 to be tracked is that the attached network or ULD 900/ULDC 908 to the location tracking system 5300 is capable of being polled (by software means) for locations of wireless devices 104 at regular intervals as short as less than one second or as long as many hours. The necessary hardware must exist on the wireless device network 100 to accommodate the required bandwidth and pipe-lining of multiple simultaneous requests for the location of a wireless device 104. When no database such as an ULD 900 or ULDC network 1600 is available, the attached networks are required to provide the following elements from internal registers pertaining to an attached wireless device 104 on the wireless device network 100, as to allow the location tracking system 5300 software to calculate a location for the wireless device 104: Base station(s) 118-A or antenna(s) 2430 location for all network equipment communicating with the wireless device 104 and; The round trip delay time for communications between the network antenna(s) 2430 and the wireless device 104 and/or; The signal receive strength from the wireless device 104 to the network antenna(s) 2430 and/or; Other location assisting information When these design requirements on the network side are available then the location tracking system 5300 is capable of tracking a plurality of wireless devices 104 and recording user records 5312 to an internal/external database that includes the location referenced to time for the said wireless devices 104. The location tracking system 5300 software first utilizes the display screen 2836 to display a menu to the user on their display screen 2836 of the wireless device 104 they are accessing the system from. The menu asks for the user to enter a single or list of wireless devices 104 to be logged. It also asks for a time frame to track these wireless devices 104 for. The time frame can be from the current system time to any given time. It can also begin at a future time and then end at any arbitrary time. Additionally, it can offer a log to be generated that includes only the location and basic other information (1 second duration or other short time). The location tracking system 5300 software would allow subsequent database queries to retrieve call location for all calls to a wireless device 104. Hence, an additional option that allows a log to be generated for all calls by a wireless device 104 for an indefinite time period is also required. The user then can specify the log entry filenames for the database entries. When the user enters this information they are prompted with alerting options. These options include the user to be sent a message in the case of a set criterion is met. The user can then enter a list of criteria. These include: Geographic boundary that wireless devices 104 cannot exceed/enter Distance wireless devices 104 may travel from any user defined location If a wireless device 104 comes with in some distance of a user defines location When these criteria are entered the user enters their contact information. The location tracking system 5300 will alert the user if any criterion are met and include a message that indicates the wireless device 104 name and database entry that may be viewed to retrieve the results. The alerting options may take any of the following forms but are not limited to: Email SMS messaging Website posting Online messaging Page Text messaging Automated voice call (synthesized voice) to a voice line Fax Other messaging protocols that can send to wireless devices 104 Once the user selects this option the system can ask the user to review the choices. The user approves them, then the system sends the criteria to the location database manager 904. The users selected wireless devices 104 will be tracked for the remainder of the selected times. The user connects and they also review a list of active logs and cancel the logging or change the parameters and resubmit them to the location database manager 904. The system will overwrite the old tracking options for any modified wireless device 104. The location database manager 904 now adds the wireless device 104 names (and corresponding wireless device identification 3724 information) into its location queue. The location queue contains the wireless device identifiers 3724 of all wireless devices 104 being logged. The location database manager 904 cycles through the list and determines the location of each wireless device 104 at the said time, and stores that information to a database record as named by the user in the setup. When a new entry is added to the queue a database entry is established and necessary disk space is allotted for the duration specified by the user. The process assures that the system will not have to slow down to a lot more space later. The database disk space reserved is equal to the data storage rate times the file size per location query times the tracking time plus overhead for the database file entry. The queue is automatically cycled though. Its size is dynamic because entries to it are constantly being made. Additionally, entries are always being removed from it. As the time(s) for entries to stop recording, as entered by a user, are met, and entry is removed from the queue. The database entry is then moved to a storage database on a different physical medium. The disk space on the primary databases physical drive is then free to be recorded to by a new record. Users may now access any records on the second database. They may also access records for location tracking(s) in progress. When this occurs the location database manager 904 overwrites the end time to the current time. The location database manager 904 then creates a new entry that starts at the current time and ends at the original end time. The result is that on the next cycle through the queue the record would be stored (up to the current time) to the secondary database so that the user could access the tracking information up to the current time. When a user retrieves the user record(s) 5312 the display software 2832 generates a map that covers the geographic boundaries of the users record(s) 5312 being opened. To display the user records 5312 the following information is needed: Geographic database 4160 Metropolitan road database Building location database Topographic information 2810 Other The information is then correlated to the user records 5312 based on the location in terms of latitude and longitude (and possible altitude). At this point the display software 2832 overlays this onto the user records 5312 and displays this information to the user. The user may zoom in and move the geographic boundaries. The resolution of the record will be limited to the time between updates and the distance traveled between those times by the wireless device 104. Mathematical extrapolations for missing data can be made by commonly known techniques to approximate the location between samples. Location Database Logs Logs created by the location tracking system 5300 software and database management software must have a consistent format that will allow universal parsing of the formatted data. The content listed in the logs must allow for a complete list of descriptive data to be saved and stored in an efficient manner. When the data is stored to the logs key elements. are required to identify the logs owner and relevant network identifiers. The requirements to establish this are the following categories: User identifier Home network for user Current network log is being generated on User's permanent storage location The next elements listed in the database log are the elements that will be tracked. These elements will be listed under categories in the log to allow rapid parsing of the log by software after it has been created and stored to a user's local directory of sectionalized portion of a home database structure. The categories are: Device ID numbers 3724 Network hardware ID numbers Event ID numbers The device ID numbers 3724 correspond to a unique identifier that is assigned to every wireless device 104 on a plurality of wireless device networks 100 that identifies itself and the wireless device network 100 it is on (ESN number, HEX ID code, wireless device 104 number, etc). The network hardware ID numbers are the identifiers of specific radio tower with BTS 110 or radio tower network 105 side equipment that communicates with users. Listed hardware elements here allow all wireless devices 104 communicating with these network components to be logged. Event ID numbers correspond to system events that would allow subsequent tracking of wireless devices 104. An example is when a wireless device network 100 fault occurs the system will monitor the wireless device 104 that the fault occurred on. The log has a start and stop time stamp field additionally that allows the date and time of the logs creation and completion to be noted and parsed quickly. Additionally there are time stamps for all recorded data. The next fields are data log fields. In this section there exists only wireless device ID numbers 3726 because only wireless devices 104 are ever tracked. The structure of this field is: Wireless device number 3726 Tracking reference ID a plurality of data measurements (taken at sequential times) Location of device (GPS data or latitude/longitude) Time of measurement Date of measurement Other Network parameters Wireless device 104 statistics Etc There can be many wireless device numbers 3726 in the log as well as many data measurements for each wireless device 104. The structure allows a plurality of wireless devices 104 to be listed and for each wireless device 104 to have independent amounts of data written to it. The tracking reference ID number allows for a link to the initial reason the wireless device 104 was tracked. An external query can just look for wireless devices 104 with respect to initial tracking criteria. For example, if a criterion was to monitor all wireless devices 104 on 2 physical radio tower network 105, then a tracking reference ID would be associated with that and affixed to every wireless device 104 log that was created for that reason. The tracking elements each have pre assigned ID numbers that are given by the database manager software and the software then also puts the same ID on each relevant wireless device 104 tracked corresponding to the tracking requirement. Cumulative Reports for Devices The idea of a cumulative report would be to allow a user to retrieve information on a plurality of database log entries made on a specific or plurality of wireless devices 104. The reports could be extended to include details on all call activity on a wireless device 104 by allowing that wireless device 104 to have a log generated each time an active call is made. The location tracking system 5300 software is designed to allow this to happen. A short duration track occurs for every call that is made from a wireless device 104 and stored a personal storage space on the secondary database used for user long-term storage. The qualifications placed on all tracking a wireless device 104 are that the wireless device 104 must verify a location and all call activity must be valid on the traffic channel. The qualification would exclude certain types of calls from being recorded. In general these calls would not show up as billable calls and would result in a user not being able to even initiate a voice channel on the phone. Their duration are typically less than one second. Examples of situations that would not record data including location of a wireless device 104 are: Network Access Failures Drop Calls before call is established on Network Poor Physical channel properties resulting in a call/network time out Hard Block Soft Block Capacity Block All calls that are successfully initiated on the wireless device network 100 will have a location database log created by the location tracking system 5300 software, and subsequently user location database manager 904. All the logs are then stored into the user directory. A possible use of this data is for it to be included in billing data. The user would receive a bill from the wireless device 104 carrier they use that could include call location information on where every call was initiated 6904. The caller ID features could allow the system to retrieve the number of the phone that was incoming or the outgoing phone dialed. This would also allow the location of that wireless device 104 to be noted. The location of the user's wireless device 104 when the call was made would be accomplished by parsing the user's database 3216 by means of SQL techniques or by other database query tools commonly known. Each call logged would be referenced to other call information including time and date. They can then be referenced to calls listed on the billable statement sent to the user. The location would be recorded as a latitude and longitude location. If a user elects the system could convert this to a landmark location or address by referring to a criss-cross latitude longitude map/database. The nearest address could be listed. An additional option would be to list a general area as opposed to an address which could often be incorrect due to location accuracy. The dialed number (for outgoing calls) or incoming caller's Id (for received calls) could also have a location listed. To accomplish this, the remote wireless device 1900 would be determined if it is a land line 142 device or a wireless device 104. If the device is a land locked device than an address for the phone number will be available through a database from the phone service provider of the number. If, however, the device is a wireless device 104 unit then this will not work. The wireless device 104 will have to be queried remotely. In this case the system can use an ATM, I based, or other method to query the main service provider of the wireless device 104 for the user location database 900 entry for that user. If authentication is allowed, and a log was made for a call at that time then a location would be available. The location could then be added to a billing cycle. If as in many cases, the remote wireless device 1900 had no call log made, then the wireless device 104 location can only be guessed upon. The system would have to resort to the users “home” NID and then supply that to the querying system. The NID could be resolved into a city, state, geographic region. The information would be included in the billing cycle as an approximation of the user's location. An appropriate consideration would be to inform on the billing cycle that is location is inaccurate and only an approximation and could be incorrect. An additional use of a cumulative report would be for an external query to be made on a plurality of logs. The logging criteria could list any data field include wireless device identifiers 3724 (ex: phone #'s), logs from geographic regions, etc. The query could be remote or from an internal memory storage 2818 system. To make this possible, the external query would have to be IP base, ATM, or another universal standard that would allow a plurality of users access to the system and provide a secure data transmission. The filter can then derive only the logs for a given user, or group of users, personal database folders. The results would then be returned and could be listed either textually or graphically to the user. A text representation would be for a list of database entries that met the specifications to be listed on the screen. A graphical representation could be to plot a map and indicate log locations on it. These options are described in the data log graphical display section. Data Log Graphical Display The user may parse a tracking log in their personal database. These logs will contain the location tracking system 5300 information for anything the user requested from the location tracking system 5300 software. The user can read this information after it is parsed in text form however a series of latitudes and longitudes will simply be repeated at the update intervals for each time a location was determined. The series of latitudes and longitudes is not very valuable to a user in general. An easy way for the user to gain valuable insight is to display this information on a graphical display unit. This could be a monitor or other display hardware attached to the querying device. It could also be a hard copy reproduced and printed on a printing device. The log can be parsed and converted to a graphical display for the user by the following method. First, the database entry must be scanned and read all the correlated data for latitude and longitude information 2830 for the tracked wireless device 104. The most extreme dimensions in for example, east, west, north and south (using Cartesian coordinates) will be noted. In this case you could also use any other dimensionally system convenient (radial, spherical). The extreme locations will be the boundaries of the displayed map. The data points will be plotted on that map, correlating data for latitude and longitude information 2832 to the correlated pixel separation as correlated to the scale of the map. The minimum resolution is the pixel separation at the monitors screen resolution. The distance will be used to disregard location points at distances less than a given amount. The plotting system can then plot the remaining points to the display screen 2836. The system will then have a map with the data points plotted to it. To increase accuracy the system may also be able to provide the described functionality that is not common knowledge. All roadways and transportation ways will be illustrated and correlating data for latitude and longitude information 2830 on the map. If a wireless device 104 is traveling in a direction for a given distance and follows a road way but is not on it exactly the software could assume the wireless device 104 is on the roadway and re-center the data points on the roadway to increase accuracy. The plotting system would allow the system to more accurately display a tracked wireless device 104 to a user. When the location of this wireless device 104 is plotted it would not show the device passing though buildings or other objects and allow the location of the data point to be shifted to the adjacent roadway or habitable area. Definable parameters would be the distance traveled along a roadway and the distance away from the road way that the software could use as criteria to assume the wireless device 104 is on the road. The distance should be conservative as to prevent obscuring real locations. An appropriate distance could be from 5 meters to 100 meters depending on the tuning of a network engineer for a particular situation. Displaying the wireless device 104 travel vector may also be useful. This Would allow the user to see the relative travel direction and speed of the wireless device 104. To accomplish this, the system would sample a defined parameter that represents how many data points to average. If the software averages 20 data points then the average direction and velocity would be represented by a vector on the display. The foot of the vector would be at the mean location of the sample range, and the vector length from foot to tip would be proportional to the average velocity over that sample time. The vectors would be plotted for every group of data points. The group size could be adjustable by the user and is accomplishable through any data interface. Another display option would be for the user to have a real-time replay of the user's location. The display could be accomplished by plotting points to the screen at the minimum pixel separation over the time interval shown. The plotting is easily done and would give the user a perspective of where the user was at various points in time. A text information box can then additionally show the time during the call while points are being plotted. The display software 2832 that gives the GUI and mapping ability can also show a plurality of log locations for a plurality of log database entries. The mapping can be accomplished by, as before, scanning logs for extreme distances. In this case though, all logs that are selected would have to be scanned for their maximum geographic dimensions. Once this is done, a map could be generated based on the dimensions. The overlay for the logs would be definable by programming, but a convenient method is to determine the initial starting location of each call and then to plot these points for each call on the map. The user may select points and then the entire route can be plotted on the map. The user who wants more detail may zoom in. The new dimensionally of the map would require the minimum pixel separation to be re-computed and would then allow more detail or less depending on if the user zoomed in or out. Alternate method that could be used if more detailed location information is available in future network configurations would be: Plotting altitude Inside building location Plotting call detail (logged speech) Inter Network Communication To make the location tracking system 5300 available to other networks outside any single entity, a database sharing system must be established. A most likely case would be for a system such as an ATM routing center or an IP (con nectionless) based system to be used. The first system is beneficial in cases where a large number of database queries may be made. ATM switching allows for a dedicated path to be established between host and user sites and allow a rapid connection once the line is established. Basic benefits to consider when choosing ATM switching are: High performance via hardware switching Dynamic bandwidth for busy traffic Class-of-service support for various traffic type Scalability in speed and network size Common LAN/WAN architecture Opportunities for simplification via VC architecture International standards compliance The benefits of IP switching as opposed to direct ATM connections between wireless device networks 100 are that the complexity is reduced. You only route packets to the next routing point and can take advantage of preexisting hardware on other networks to get your data to the destination, in our case the other wireless device 104 network. The ability to handle security on a traditional router basis is very complex and the speed at which a router switches or routs a packet is very slow and cumbersome because every packet has to be looked at as it goes through the wireless device network 100. This can reduce security and is a consideration for any wireless provider when implementing IP switching. With an IF switch (MTX or other) 130-based network, what happens is the first packet is looked at and the supplementary packets do a quick forward look-up and then everything else goes through the network very, quickly, so it's less costly and it's easier to administer. ATM systems require new and expensive hardware to be added but are often faster and more reliable. The system is also a far more secure method because all information is on a protected network at all times. IF based system here could use the internet 3202 to send requests between wireless device network 100 locations and allow for rapid development and low cost of implementation. The inter-network structure would allow wireless device networks 100 to query each other for information. Security and fire-wall precautions aside, this allows one wireless device network 100 to retrieve the location of a wireless device 104 on any other wireless device network 100. The inter-network structure would allow the tracking of the two, or more, wireless devices 104 on a call or other communication. It would also allow tracking wireless devices 104 as they moved off of a network providers system and on to a remote system. IF version 6 provides for the internet 3202 solutions to inter-network wireless device 104 movement and would allow tracking to occur over multiple wireless device networks 100. The data logs could then be generated at the remote wireless device network 100 and retrieved by the user's home wireless device network 100. This would allow tracking beyond the users own network boundaries. Security The security of this wireless device network 100 can be viewed in two subsystems. First the network must secure access to the system at a user level access, or group access scheme. Second, the system must secure user system rights. In this regard, it must secure that any user may not gain access to sensitive information of another user it does not have rights to. The access of a user to the system will be defined and can be implemented by various methods. Secure Socket Layer (SSL) can be used to guarantee that and external wireless device user 102 has a secure connection. Modern internet 3202 browsers use a SSL to encrypt the information that flows between the browser and the web server. A browser using SSL has established a secure encrypted connection with the server, meaning it is safe to send sensitive data. In the case of a local connection less line security is necessary. 128 bit or higher encryption of data across a wireless device network 100 will allow data to remain private in transit. To allow for a secure connection various protocols can be used. FTP, and telnet offer some protection, but secure connections such as used by verisign and other companies to establish “user identity” are recommended. The connection types should be connectionless service types. The secure connection ensures that packet never follow the same path across a network such as the internet 3202. The secure connection allows for less possibility of snooping and more security. On secure connections (point-to-point), connection oriented ATM links can suffice because the line is secure in a physical sense. Wireless device users 102 will be placed in categories based on access rights. All three categories are defined by a administrator and are adjustable, but generally accepted standards are: User Super user Administrator A user level access will give the entity connecting to the system the ability to access only files created and stored in it user directory. The user may only request logs be created for wireless devices 104 that have been added to its authorized list by an administrative account. A super user has access to all the user rights for itself, but may also have rights to the files and permissions of a group of wireless device users 102. This would allow the user to track wireless devices 104 listed on other wireless device users 102 accounts. An administrator has all the access of the super user but also has the ability to create and delete accounts, as well as file management. This allows the administrator unrestricted access to all files on a server. It can also alter and change system parameters that affect any or all wireless device users 102. Physical Hardware to Realize Embodiment To implement the primary embodiment 2800 there must be a hardware platform for the software to function from. The term function refers to the normal operation of the software that includes the primary embodiment 2800 as well as any other secondary software packages that would run to assist the primary embodiment 2800. The secondary processes are commonly known and would not be covered by this patent. An example would be dynamic link libraries that are commonly known and used to linking various software elements. The hardware required to implement the user location database manager 904 is inclusive of but not limited to, based on any unique hardware setup: Data storage medium Data storage controller (RAID, etc) Computer 2910 (includes motherboard, CPU, RAM, etc) Network interface card The data storage medium should consist of a hard disk or other nonvolatile storage medium that is can be accessed by a computer 2910. It can conform to either, IDE or SCSI standards. Extended standards could include ultra wide SCSI and EIDE as well as other derivations. The claimed scope is that a communications protocol database 3004 and physical layer would provide high bandwidth capacity and high efficiency. Examples of this hardware may be a western digital 10,000 RPM 80 GB deskstar hard disk drive. The data storage controller consists of one of the following generic classes: IDE/EIDE/etc SCSI/U W-SCSI/etc RAID type 1, 2, etc The controllers are required for the computer 2910 to be allowed to access the hard disk drive. To allow for this to work the computer 2910 must be compatible with the controller. The RAID controller allows a unique benefit to the database and storage architecture. Having many configurations, very high bandwidth and redundancy of data is possible. The accurate usage of RAID architecture is critical for these databases as VERY high bandwidth is required on large wireless device networks 100. Explained as follows are the recommended RAID types and the considerations in choosing each. In RAID 0, the controller will store the data across two or more disks, writing the data in blocks across the disks. For example, if you have two disks, block one will be written to disk one, block two to disk two, block three to disk one, and so on. The data will increase performance since the controller can read/write in parallel, but there is no redundancy, if one disk fails, the whole array fails, since the data is spread across the array. RAID 0 is the most efficient level in terms of cost/space/performance, as you will increase performance without sacrificing any disk space, though access times suffer slightly. RAID 0 is best used where cost/performance is critical, but data integrity is not. For this reason the type of RAID would be the least recommended for the primary embodiment 2800 and its databases. A RAID 1 array consists of two or more disks and acts as one logical disk while mirrored data 1532 is passed between the disks. If you have an array consisting of two 36 GB disks, you will end up with a logical disk of 36 GB, with data being stored on both the physical disks. Hence one of the physical disks can fail, and the array will keep working, and if the disks are hot-swappable, which is the case with most SCSI RAID setups, the failed disk can be swapped for a new disk, and the controller will synch the data between the disks, restoring the array to full functionality, with no downtime. RAID 1 also increases the read performance since both disks can be read at once, while write performance will be more or less identical to that of one single disk. RAID 1 is a way to achieve good read performance, as well as redundancy. For this reason it is recommended over RAID 0 and will allow higher bandwidth and therefore more throughput from the database to the computer 2910 Striping with parity increases performance while maintaining a handle on redundancy. RAID 3 does this by implementing a RAID 0 and then creating a separate disk to write parity information. RAID 3 helps, if you lose a disk, that disk's information can be recreated. RAID 3 works on a binary system. (i.e. 11=Oparity, 000parity, 01=1parity, 10=11parity) You can take any two bits, and recreate the lost one. The benefits of this are performance and safety, although with RAID 3 you put a large strain on the odd disk that contains parity as everything has to be calculated and written to it. For ever bit written to any other disk, one gets written there, both bottlenecking performance, and creating more strain on this disk. 50 is considered to be a much better option. A required minimum of 3 disks, and an odd number of disks. RAID 3 is very expensive in terms of CPU power when implemented in software. For this reason this configuration is recommended over RAID 0 but less than RAID 1 for the primary embodiment 2800. RAID 5 is a quite common type of RAID but it doesn't offer the performance of RAID 1+0, but is much cheaper. Three or more disks a required for a RAID 5 array. RAID 5 stores parity information (unlike RAID 1 which stores data redundantly) across the disks in the array, this information can then be used to rebuild lost data in case of disk failure. Raid 5 is not recommended at all but is explained such that RAID 50 can next be fully understood. Raid 50 is the combo of RAID 5 and RAID 0. The major benefit is speed. RAID 50s take the data to write, say 256 k, then split that among the RAID 0, so 128 k+128 k, then split that among the RAID 5s, so you could be writing 32 k+32 k+32 k+32 k+32 k+32 k+32 k+32 k all to separate disks at the same time. The same is true in reverse as well for reading. You could also lose I disk out of each array and the controller would keep running. You can stream high amounts of data to several machines at once over the network. To do it right it really should be done on two controllers, or one multi-channel controller to give the arrays as much bandwidth as possible. RAID 50 requires a minimum of 6 disks, and an even number of disks. The setup is recommended for the database controller. The system will be able to keep up with network connection bandwidth (T-1, T-3, OC-3, etc). The primary embodiment 2800 will operate at maximum efficiency using this setup. The physical hardware should consist of a processor capable of computing the necessary work load. A dual processor system would reduce the load further. An intel XEON system (dual processor) at 1 GHz or above would suffice. Additional RAM in excess of 1 G would be beneficial and allow fast access to cached data. Similar systems to this are produced by AMD and other chip manufacturers. The location tracking software 5300 may exist on any of the above said hardware but should have its own reserved storage medium. A low bandwidth connection to the computer 2910 is OK because the software will run from cache memory as it is a static program that is accessed frequently. The display software 2832 does not require a specific set of hardware, more of a class of hardware. The display hardware 2832 required is a display driver or graphics hardware controller, commonly called a graphics card. Performance of the card need not be high but should allow for an adequate resolution display for the minimum programming of the display software 2832. Display hardware 2832 that could be used as the physical display device can be CRT computer 2910 monitor displays, LCD displays of various sizes including palm-top sized displays. Example of this is a Viewsonic 19″ CRT G790, this monitor would support up to 1 600×1 200 at 80 Hz refresh which would allow proper viewing of all visual data from the preferred embodiment 2800 The network interface cards required would be a 121100 base-T or higher connection. Hardware such as a 3COM Etherfast NIC would function properly. External connectivity to the internet 3202 or other high speed data access points is also required which often requires a ATM connection or other gateway routing wireless device 104. Directional Assistance Network (DAN) The Dan Comprises: A COMPUTER SYSTEM HARDWARE/SOFTWARE AN OPERATING SYSTEM A DIRECTIONAL ASSISTANCE OPERATING PROGRAM AN AUTOMATED TELEPHONE HARDWARE/SOFTWARE A VOICE RECOGNITION HARDWARE/SORTWARE TRAFFIC MONITORING AND ROUTE PLANNING HARDWARE /SOFTWARE AND MAPPING HARDWARE/SOFTWARE A WIRELESS DEVICE USER LOCATION DATABASE AND DATABASE LOGIC CENTER HARDWARE/SOFTWARE (OPTIONAL IF LOCATION DATA IS OBTAINED FROM AN OUTSIDE DATABASE, E-MOBILITY, ETC.) A PSTN USER LOCATION DATABASE AND DATABASE LOGIC CENTER HARDWARE/SOFTWARE (OPTIONAL IF LOCATION DATA IS OBTAINED FROM AN OUTSIDE DATABASE, E-MOBILITY, ETC.) LOCATION CONVERSION HARDWARE/SOFTWARE AND DATABASE TO CONVERT STREET ADDRESSES TO LONGITUDE AND LATITUDE DATA, AND TO CONVERT LONGITUED AND LATITUDE DATA TO STREET ADDRESS DATA. A VOICE MAIL SYSTEM INTERNET ACCES SABLE INTERNET ADDRESS AND WEB SITE. ABILITY TO MAKE AND SENT MAPS TO WCD, NAVIGATIONAL SYSTEMS, FAXES, E-MAILS, ETC. A LIVE OPERATOR WHO CAN ACCESS, PROGRAM AND SERVICE ALL PARTS OF THE DAN. CONVERSION/STANDERDIZATION HARDWARE/SOFTWARE FOR INTER-FACING WITH WIRELESS NETWORKS, WIRELESS DEVICES AND PUBLICLY SWITCHED TETEPHONE NETWORKS. CONVERSION/STANDERDIZATION HARDWARE/SOFTWARE FOR SENDING AND RECEIVING MAPS, F-MAILS AND FAXES. DETAILED DESCRIPTION OF THE EMBODIMENTS FIG. 70 is a flowchart of the Directional Assistance Network (DAN) query process. To begin the query process, a person seeking directional assistance or location information begins a query for directional assistance by dialing a specified phone number, such as, for example, 411, 511, an 800 number or a dedicated button on a wireless device, navigational system or a land-based communications device 7000. The user may also process a DAN query via the Internet. The user can enter his DAN query via a keypad or keyboard, through the use of voice recognition software, a live operator or by way of an interactive display screen, such as may be found on a wireless device or a navigational system. The process begins when the DAN 8100 receives the user's call 7002. The DAN 8100 then queries a user location database (ULD) to determine the user's location and logs to user's location within the DAN 8100, BOX 7003. Still referring to FIG. 70, BOX 7003, if the DAN 8100 determines that the user is calling from a wireless communication device (WCD) 8205, such as, for example, a cellular phone, an Personal Digital Assistant (FDA), wireless navigational system, etc, then DAN 8100 queries a wireless network's ULD 900 in order to determine the user's location within the wireless network. The wireless network's ULD 900 can exist internally to the DAN 8100 and constructed by the DAN 8100 with information obtained from the wireless network through querying the wireless network's e-mobility services, switch and/or base station controller. The DAN 8100 could also find the user's location without a wireless network's ULD 900, by retrieving the user's location data from the wireless network on an as needed basis. The DAN 8100 can generate the location on an as needed basis by accessing pertinent location data, which can be obtained from the switch (MTX or other) 130, and the base station controller (BSC) 206. The pertinent information would include the round trip delay (RTD), signal strength and other factors needed for determining location of wireless device, which are disclosed in an attached document. The ability to determine the user's geographic location in the form of longitude and latitude data, when calling from a wireless device, is disclosed in an attached document entitled, ‘A machine for providing a dynamic database of geographic location information for a plurality of wireless communications devices and process for making same”. This document referenced above, is a United States Provisional Patent, U.S. Ser. No. 60/327,327, which was filed on Oct. 4, 2001, is hereby incorporated into this disclosure. Also, the wireless network's ULD 900 may be comprised of only a single service provider's network, or in may comprise a plurality of service provider's networks data regarding wireless device user location data. The DAN 8100 may use its conversion/standardization hardware/software 8160 to interface with wireless networks and wireless devices. Still referring to FIG. 70, BOX 7003, if the user's call originates from a publicly switched telephone network (PSTN) 138, the user's location can be determined by querying a PSTN phone location database 8145 which consists of listings of the names of businesses and private residences, their respective street addresses, city, state and corresponding longitude and latitude coordinates, and their telephone numbers. The PSTN phone location database 8145 could be internal or external to the DAN 8100. The database could also be comprised of a street map location system instead of a longitude and latitude based system. The DAN 8100 could also find the user's location without a PSTN's phone location database 8145, by retrieving the user's location data from the PSTN 138 on an as needed basis. The location can be generated on an as needed basis within the DAN 8100 by accessing pertinent location data, which can be obtained from the switch (MTX or other) 130, and the base station controller (BSC) 206 of the PSTN 138. The DAN 8100 may use its conversion/standardization hardware/software 8160 to interface with the PSTN 138. Regardless of whether the user is calling form a wireless device or a landline, once the user's geographic location has been determined and logged into the DAN's voice mapping software 8110, The DAN's automated telephone system prompts the user with a menu of services 7004. Still referring to FIG. 70, the DAN 8100 first asks the user “If you know the phone number of your desired destination, and would like to receive directions to that destination, please press or say 1” 7006. The automated telephone system waits for the user's response 7008. If the user selects “1”, the user is forwarded to FIG. 71, BOX 7100, the portion of the query process that retrieves the geographic coordinates of the users destination, based on the destination's area code and telephone number 7010. Again referring to FIG. 70, BOX 7008, if the user does not select “1” within a specified period of time, the automated telephone system continues to instruct the user “For the telephone number and directions to a specific business or person by name, press or say “2” 7012. The automated telephone system waits for the user's response 7014. If the user selects “2”, the user is forwarded to FIG. 72, BOX 7200, the portion of the query process that retrieves the business or residential listing by the name of the listing 7016. Still referring to FIG. 70, BOX 7014, if the user does not select “2” within a specified period of time, the automated telephone system continues to instruct the user, “For a phone number and directions to the nearest business by category, such as for example, a gas station or restaurant, press or say “3” 7018. If the user selects “3”, the user is forwarded to FIG. 73, BOX 7300, the portion of the query process that retrieves the geographic coordinates of the users destination, based on the category of the business which the user wishes to find 7022. Again referring to FIG. 70, BOX 7020, if the user does not select “3” within a specified period of time, the automated telephone system continues to instruct the user, “For a phone number and directions to as specific address, press or say “4” 7024. If the user selects “4”, the user is forwarded to FIG. 74, BOX 7400, the portion of the query process that retrieves the geographic coordinates of the specific address the user is requesting directions and the phone number 7028. Still referring to FIG. 70, BOX 7026, if the user does not select “4” within a specified period of time, the automated telephone system continues to instruct the user, “To locate or track a wireless device, press or say “5” 7030. The DAN 8100 then waits a specified period of time for the user to respond by selecting “5” 7032. If the user selects “5”, the user is forwarded to FIG. 78, BOX 7800 and the DAN 8100 continues it's query process 7034. Again referring to FIG. 70, BOX 7032, if the user does not select ‘5” within a specified period of time, the automated telephone system continues to instruct the user, “To repeat these choices, press or say “6” 7036. The DAN 8100 then waits a specified period of time for the user to respond by selecting “6” 7038. If the user selects “6”, the user is returned to FIG. 70, BOX 7006, the portion of the query process which has been described above is repeated 7032. If the user does not select “6” within a specified period of time, the automated telephone system continues to instruct the user, “To end this call, press or say “9”, or hang up” 7040. The DAN 8100 then waits a specified period of time for the user to respond by selecting “9” 7042. If the user selects “9”, the call is terminated 7044. If the user does not select ‘9” within a specified period of time, the automated telephone system continues to instruct the user, “To be connected to a DAN Operator, press or say “0”, or say on the line” 7046. The automated telephone system then forwards the user's call, to a live operator for assistance 7048. The live operator has direct access to all components of the DAN 8100 and can assist the user's how are having trouble with the automated system. Now referring to FIG. 71, the automated telephone system instructs the user, “Please dial or speak the area code and phone number of your desired destination to receive directions to that location” 7100. The automated telephone system waits for the user to dial or speak the area code and telephone number to the desired destination 7102. The automated telephone system waits for the user to respond within a specified period of time by dialing the phone number 7104. If the user dials the phone number, the number is matched against numbers within the PSTN phone location database 7110 of business and residential listings, which may be internal or external to the DAN 8100. The automated telephone system then tells the user, “We have located “X” number possible match(s)” 7114. Still referring to FIG. 71, if the user does not dial a phone number within the specified period of time, the automated telephone system waits for the user to respond by speaking the phone number 7106. If the user does not respond within a specified period of time, the user's query is forwarded to FIG. 71 BOX 7126, for further processing. If the user responds by speaking the phone number, a voice recognition program within the DAN 8100 converts the user's words into texts 7108. The DAN 8100 matches the text against telephone numbers contained within the database of business and residential listings 7112. The automated telephone system tells the user, “We have located “X” number possible match(s)” 7114. Again referring to FIG. 71, the automated telephone system then instructs the user, “For directions to “listing 1” located at “address 1” with a phone number of “phone 1”, press or say “1” 7116. The automated telephone system then waits a specified period of time for the user to press or say “1” 7118. If the user selects “1”, the user's choice is logged within the DAN 8100, and the user's query is forwarded to FIG. 75, BOX 7500, for further processing 7120. If the user does not select “1”, the automated telephone system instructs the user, “To repeat listing(s), press or say “4” 7122. The automated telephone system then waits a specified period of time for the user to respond by pressing or saying “4” 7124. If the user does select “4”, the automated telephone system returns to FIG. 71, BOX 7116 and repeats the listing. If the user does not select “4” within the specified period of time, the automated telephone system instructs the user, “To request a new listing, press or say “5” 7126. If the user selects “5”, the DAN 8100 returns the user to FIG. 70, BOX 7006, where the user can begin to search for a new listing 7130. If the user does not select “5”, the automated telephone system instructs the user, “To be connected to a Directional Assistance Operator, press or say “0”, or stay online” 7132. The automated telephone system then forwards the user, to a live directional assistance operator for assistance 7134. Now referring to FIG. 72, the automated telephone system instructs the user, “Please speak the name of the business or residents you wish to find” 7200. The automated telephone system waits for the user to speak the name of the desired business or person 7202. The voice interface software 8105 and voice mapping software 8110 within the DAN 8100 converts the user's spoken words into text 7204. The DAN 8100 matches the text against names within the PSTN phone location database 8145, which may be internal or external to the DAN 8100, BOX 7206. The automated telephone system then informs the user, “We have located “X” number of possible match(s)” 7208. Still referring to FIG. 72, the automated telephone system then instructs that user, “For directions to “listing 1” located at “address 1”, with a phone number of “phone number 1”, press or say 1” 7210. The automated telephone system then waits a specified period of time for the user to respond by selecting “1” 7212. If the user selects “1”, the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7214. If the user does not respond by selecting “1”, the automated telephone system instructs the user, “For directions to “listing 2” located at “address 2”, with a phone number of “phone number 2”, press or say “2” 7216. The automated telephone system then waits a specified period of time for the user to respond by selecting “2” 7218. If the user selects “2”, the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7220. If the user does not respond by selecting “2”, the automated telephone system instructs the user, “For directions to “listing 3” located at “address 3”, with a phone number of “phone number 3”, press or say “3” 7222. The automated telephone system then waits a specified period of time for the user to respond by selecting “3” 7224. If the user selects “3”, the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7226. Again referring to FIG. 72, if the user does not respond by selecting “3”, the automated telephone system instructs the user, “To repeat the previous listing(s), press or say “4” 7228. The automated telephone system then waits a specified period of time for the user to respond by selecting “4” 7230. If the user selects “4”, the DAN 8100 returns the user to FIG. 72, BOX 7210, were listings are repeated by the DAN's automated telephone system. If the user does not select the automated telephone system instructs the user, “To request a new listing, press or say “5” 7232. The automated telephone system then waits a specified period of time for the user to respond by selecting “5” 7234. If the user selects “5”, the DAN 8100 returns the user's query to FIG. 70, BOX 7006, were a new query process can begin 7236. If the user does not select “5”, the automated telephone system instructs the user, “To be connected to a Directional Assistance Operator, Press “0”, or say on the line” 7238. The user's call is then forwarded to a live operator for assistance 7240. Now referring to FIG. 73, the automated telephone system instructs the user, “Please speak the category of business you wish to find” 7300. The automated telephone system waits for the user to speak the name of the desired business category 7302. The voice interface software 8105 and voice mapping software 8110 within the DAN 8100 converts the user's spoken words into text 7304. The DAN 8100 matches the text against categories within the PSTN phone location database 8145 that most closely correspond to the user's geographic location 7306. If the DAN 8100 does not find any listings within the user's selected category 7308, the automated telephone system informs the user, “No listings were found in this category” 7336. The automated telephone system then instructs the user, “To request a new listing, press or say 5” 7338. The DAN 8100 then waits a specified period of time for the user's response 7340. If the user selects “5”, the user is returned to FIG. 70, BOX 7006, for an opportunity to select a new listing 7342. If the user does not select “5”, the automated telephone system instructs the user, “To be connected to a Directional Assistance Operator, Press “0”, or say on the line” 7344. The user's call is then forwarded to a live operator for assistance 7346. Still referring to FIG. 73, if the DAN 8100 finds the requested category, the listings contained within that category are sorted according to distance from the user's geographic location 7310. The automated telephone system then informs the user, ‘We have located “X” number of possible match(s)” 7312. The number “found” listings that are actually available to the user can be set within the DAN 8100 so as only to provide, for example, only the three closest listings within the selected category. Still referring to FIG. 73, the automated telephone system then instructs that user, “For directions to “listing 1” located at “address 1”, with a phone number of ‘phone number 1”, press or say “1” 7314. The automated telephone system then waits a specified period of time for the user to respond 7316. If the user selects “1”, the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7318. If the user does not respond, the automated telephone system instructs the user, “For directions to ‘listing 2” located at “address 2”, with a phone number of “phone number 2”, press or say ‘2” 7320. The automated telephone system then waits a specified period of time for the user to respond 7322. If the user selects “2”, the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7324. If the user does not respond, the automated telephone system instructs the user, “For directions to “listing 3” located at “address 3”, with a phone number of “phone number 3”, press or say “3” 7326. The automated telephone system then waits a specified period of time for the user to respond 7328. If the user selects “3”, the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7330. Again referring to FIG. 73, if the user does not respond, the automated telephone system instructs the user, “To repeat the previous listing(s), press or say “4” 7332. The automated telephone system then waits a specified period of time for the user to respond 7334. If the user selects “4”, the user is returned to FIG. 73, BOX 7314, were listings are repeated through the DAN's automated telephone system. If the user does not select “4”, the automated telephone system instructs the user, “To request a new listing, press or say “5” 7338. If the user selects “5”, the user's query is returned to FIG. 70, BOX 7006, were a new query process can begin 7342. If the user does not select “5”, the automated telephone system instructs the user, “To be connected to a Directional Assistance Operator, Press “0”, or say on the line” 7344. The user's call is then forwarded to a live operator for assistance 7346. Now referring to FIG. 74, the automated telephone system instructs the user, “Please speak the complete Street address including city and state, to receive phone number and directions to that address” 7400. The automated telephone system waits for the user to speak the name of the desired business or person 7402. The voice interface software 8105 and voice mapping software 8110 within the DAN 8100 converts the user's spoken words into text 7404. The DAN 8100 matches the text against addresses within the PSTN phone location database 7406. The automated telephone system then informs the user, “We have located “X” number of possible match(s)” 7408. Still referring to FIG. 74, the automated telephone system then instructs the user, “For directions to “listing 1” located at “address 1”, with a phone number of “phone number 1”, press or say 1” 7410. The automated telephone system then waits a specified period of time for the user to respond 7412. If the user selects 1”, the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7414. If the user does not respond, the automated telephone system instructs the user, “For directions to “listing 2” located at “address 2”, with a phone number of “phone number 2”, press or say “2” 7416. The automated telephone system then waits a specified period of time for the user to respond 7418. If the user selects ‘2” the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7420. If the user does not respond, the automated telephone system instructs the user, “For directions to “listing 3” located at “address 3”, with a phone number of “phone number 3”, press or say “3” 7422. The automated telephone system then waits a specified period of time for the user to respond 7424. If the user selects “3”, the user's choice is logged into the DAN 8100, and the DAN 8100 forwards the user to FIG. 75, BOX 7500, for further processing 7426. Again referring to FIG. 74, if the user does not respond, the automated telephone system instructs the user, “To repeat the previous listing(s), press or say “4” 7428. The automated telephone system then waits a specified period of time for the user to respond 7430. If the user selects ‘4”, the DAN 8100 returns the user to FIG. 74, BOX 7410, where listings are repeated. If the user does not select “4”, the automated telephone system instructs the user, “To request a new listing, press or say “5” 7432. If the user selects “5”, the user's query is returned to FIG. 70, BOX 7006, were a new query process can begin 7436. If the user does not select “5”, the automated telephone system instructs the user, “To be connected to a Directional Assistance Operator, Press “0”, or say on the tine” 7438. The user's call is then forwarded to a live operator for assistance 7440. Now referring to FIG. 75, the automated telephone system instructs the user, “To receive directions based on fastest travel time with current traffic conditions, press or say 1” 7500. The automated telephone system waits a specified period of time for the user to respond 7502. If the user does not respond with a specified period of time, the query process is forwarded to FIG. 76, BOX 7600, for further processing 7506. If the user does select “1”, the traffic monitoring software 8125 and routing software 8120, within the DAN 8100, plots the user's location and location of the selected destination, and determines a selected number of possible logical routes. The routes are sent to the DAN's traffic monitoring software and routing software 7504. The traffic monitoring software 8125 and routing software 8120 queries the wireless network's ULD 900 to examine the flow of traffic based on the movement and density of wireless devices, and calculates the fastest route based on available information including traffic movement, speed limits (if available) and distance 7508. Still referring to FIG. 75, upon determining the fastest route, the traffic monitoring software 8125 and routing software 8120 then calculates direction, distance, and estimated travel time 7510. The automated telephone system then informs the user, “Your destination is “X’ miles “North/South” and “Y” miles “East/West”, with an estimated driving distance of “W” miles. Current travel time is estimated at ‘1’ minutes” 7512. The automated telephone system then instructs the user, “To continue with these directions and receive the travel plans, press or say “1” 7514. The automated telephone system then waits a specified period of time for the user to select 1” 7516. If that user does not respond with within a specified period of time, the automated telephone system then instruments the user, “To repeat the previous information, press or say “2” 7528. The automated telephone system then waits a specified period of time for the user to select ‘2” 7530. If the user responds by selecting ‘2″, the DAN 8100 returns the user to FIG. 75, BOX 7512. If the user does not select “2” within a specified period of time, the automated telephone system then instruments the user, To return to the main menu, or to enter a new destination, press or say “3” 7532. The automated telephone system then waits a specified period of time for the user to select “3” 7534. If the user responds by selecting “3”, the user is returned to FIG. 70, BOX 7006 to began a new query 7536. If the user does not select “3” within a specified period of time, the automated telephone system then informs the user, “Thanking you for using the Direction Assistance Service”, and the call is terminated 7526. Again referring to FIG. 75, BOX 7516, if the user selects “1”, the automated telephone system then instructs the user, “To repeat these directions at anytime, press or say “9”. The directions are as follows, “XXXXXX” 7518. The automated telephone system then instructs the user, “To be instructed when to turn, to receive a notice when the fastest route to changes due to traffic conditions, or to receive a map of the travel plan, press or say 1” 7520. The automated telephone system then waits a specified period of time for the user to select “1” 7522. If the user responds by selecting “1”, the user is forwarded to FIG. 79, BOX 7900 for further processing 7524. If the user does not select “1” within a specified period of time, the automated telephone system then informs the user, “Thanking you for using the Direction Assistance Services”, and the call is terminated 7526. Now referring to FIG. 76, the automated telephone system instructs the user, “To receive directions based shortest travel distance, press or say “2” 7600. The automated telephone system waits a specified period of time for the user to respond 7602. If the user does not respond with a specified period of time, the DAN 8100 forwards the query process to FIG. 77, BOX 7700, for further processing 7606. If the user does select “2”, the traffic monitoring software 8125 and routing software 8120 comprised within the DAN 8100, plots the user's location, and location of the selected destination, and determines the shortest possible logical route 7604. The traffic monitoring software 8125 and routing software 8120 then determines the direction, distance, and estimated travel time 7610. The automated telephone system then informs the user, “Your destination is “X” miles “North/South” and “Y” miles “East/West”, with an estimated driving distance of “W” miles. Driving time is estimated at “Z” minutes” 7612. The automated telephone system then instructs the user, “To continue with these directions and receive the travel plans, press or say “1” 7614. The automated telephone system then waits a specified period of time for the user to select “1” 7616. If that user does not respond with within a specified period of time, the automated telephone system then instructs the user, “To repeat the previous information, press or say “2” 7628. The automated telephone system then waits a specified period of time for the user to select “2” 7630. If the user responds by selecting “2”, the user is returned to FIG. 76, BOX 7612. If the user does not select “2” within a specified period of time, the automated telephone system then instructs the user, “To return to the main menu, or to enter a new destination, press or say “3” 7632. The automated telephone system then waits a specified period of time for the user to-select “3” 7634. If the user responds by selecting “3”, the DAN 8100 returns the user to FIG. 70, BOX 7006 to began a new query 7636. If the user does not select “3” within a specified period of time, the automated telephone system then informs the user, “Thanking you for using the Directional Assistance Services”, and the call is terminated 7626. Again referring to FIG. 76, BOX 7616, if the user selects “1”, the automated telephone system then instructs the user, “To repeat these directions at anytime, press or say “9”. The directions are as follows, “XXXXXX” 7618. The automated telephone system then instructs the user, “To be instructed when to turn, or to receive a map of the travel plan, press or say “1” 7620. The automated telephone system then waits a specified period of time for the user to select “1” 7622. If the user responds by selecting “1”, the DAN 8100 forwards the user to FIG. 79, BOX 7900 for further processing 7624. If the user does not select “1” within a specified period of time, the automated telephone system then informs the user, “Thanking you for using the Directional Assistance Services”, and the call is terminated 7626. Now referring to FIG. 77, the automated telephone system instructs the user, “To be connected to your selective listing, press or say “3” 7700. The automated telephone system waits a specified period of time for the user to respond 7702. If the user does select “3”, the automated telephone system connects the user to their selected listing 7704. If the user does not respond by selecting “3” within a specified period of time, the automated telephone system instructs to user, “To repeat these choices, press or say “4” 7706. If the user does select ‘4”, the automated telephone system returns the user to FIG. 75, BOX 7500, and the query process continues 7710. If the user does not respond by selecting “4” within a specified period of time, the automated telephone system instructs to user, “To return to the main menu or to enter a new destination, press or say “5” 7712. If the user does select “5”, the automated telephone system returns the user to FIG. 70, BOX 7006, and the query process starts over 7716. If the user does not respond by selecting “5” within a specified period of time, the automated telephone system returns the user to FIG. 70, BOX 7046 and the user is connected to a live Directional Assistance Operator 7718. Now referring to FIG. 78, the automated telephone system instructs the user, “Please dial the area code and phone number of the wireless communications device you want to locate 7800. The automated telephone system then waits a specified period for time for the user to respond by dialing the wireless communications device's phone number the user wishes to find 7802. If the user does not respond within the specified period of time, the automated telephone system instructs the user, “To request a new listing, press or say 4” 7832. If the user does respond within the specified period of time, the telephone phone number is logged into the DAN 8100 and the telephone number is matched against telephone numbers within the wireless communication network's ULD 900, BOX 7804. The DAN 8100 then determines if the requested telephone number is located 7806. Still referring to FIG. 78, BOX 7806, if the phone number is not found, the automated telephone system instructs the user, “The wireless communications device (WCD) you are trying to locate cannot be found at this time. Please record and message for the wireless communications device's user, or press “4” for more options.” If the user selects “4”, the query is forwarded to FIG. 78, BOX 7832, to begin a new query 7808. If the user does not selected “4”, the DAN's voice mail system records the caller's message. The DAN 8100 searches for the wireless communications device periodically. When the wireless communications device is located, the DAN 8100 calls the wireless communications device and plays the recorded message 7810. Again referring to FIG. 78, BOX 7806, if the phone number is found, the automated telephone system tells the user, “We have located the phone number “XXX-XXX-XXXX” 7812. The automated telephone system then tells the user, “For current location of the wireless communications device, press or say “1” 7814. The automated telephone system then waits a specified period of time, for the user to respond by pressing 1” 7816. If the user does not select “1”, the automated telephone system forwards the user to FIG. 78, BOX 7832, to request a new listing. If the user does select “1”, the DAN's geographic database mapping software 8155 criss-cross lat/long geographic database 8150 and then converts the longitude and latitude coordinates provided by the wireless communication network's ULD 900 to a street address format 7818. The automated telephone system then informs the user of the Street address by saying, “The wireless device is currently located at “XXXXXXXX” 7820. The automated telephone system then instructs the user, “To repeat this location, press or say “2” 7822. The automated telephone system then waits for the user to respond by selecting “2” 7824. If the user does select “2” within a specified period of time, the users query is returned to FIG. 78, BOX 7820, in order to repeat the location information. Still referring to FIG. 78, BOX 7824, if the user does not select “2” within the specified period of time, the automated telephone system then instructs the user, “To receive a map of the wireless device's location, or to track the wireless device, press or say “3” 7826. The automated telephone system then waits for the user to respond within a selected period of time by selecting “3” 7828. If that user does select “3” within the specified period of time, the DAN 8100 logs the user's choice and forwards the user's query to FIG. 79, BOX 7900, for further processing 7830. Again referring to FIG. 78, BOX 7828, if the user does not select “3” within the specified period of time, the automated telephone system instructs the user, “To request a new listing, press or say “4” 7832. The automated telephone system then waits for the user to respond by selecting “4” 7834. If the user selects “4” within the specified period of time, the user's query is forwarded to FIG. 70 BOX 7006 to begin a new query 7836. If that user does not select “4” with them the specified period of time, the automated telephone system instructs the user, “To be connected to the Directional Assistance Operator, press “0” or stay on the line” 7838. The user is then forwarded to a live Operator for assistance 7840. Now referring to FIG. 79, the automated telephone system instructs the user, “To have a map and travel plans sent to your wireless device via a page, press or say “1” 7900. The automated telephone system then waits for the user to respond by selecting “1” 7902. If the user selects “1”, the DAN 8100 sends a map and travel plans to the standardization/conversion hardware/software 8160 to convert the map and travel plan to a format which will interface with the protocol of the user's wireless device. The map and travel plans are sent to the user's wireless device via a page and are updated if the user requests an update as traffic conditions change to as to offer a faster route. The user can also be notified when to turn if the DAN 8100 monitors the user's location and pages the user when the user is approaching a turn 7904. Again referring to FIG. 79, BOX 7902, if the user does not select 1’, the automated telephone system instructs the user, “To have a map and travel plans sent to your e-mail address, press or say ‘2” 7906. The automated telephone system then waits for the user to respond by selecting “2” 7908. If the user selects “2”, the DAN 8100 instructs the user to enter their e-mail address via keypad/keyboard, voice recognition, interactive display screen or other. The DAN 8100 then sends a map and travel plans to the standardization/conversion hardware/software 8160 to convert the map and travel plan to a format which will interface with the protocol of the user's e-mail service and navigational program. The map and travel plans are sent to the user's e-mail address and are updated if the user requests an update as traffic conditions change to as to offer a faster route. The user can also be notified when to turn if the DAN 8100 monitors the user's location and e-mails the user when the user is approaching a turn 7910. Again referring to FIG. 79, BOX 7908, if the user does not select “2”, the automated telephone system instructs the user, “To have a map and travel plans sent to your fax machine, press or say ‘3” 7912. The automated telephone system then waits for the user to respond by selecting “3” 7914. If the user selects “3”, the DAN 8100 instructs the user to enter the area code and telephone number were the faxes are to be sent. The DAN 8100 then sends a map and travel plans to the standardization/conversion hardware/software 8160 to convert the map and travel plan to a format, which will interface with the protocol of the user's Fax machine/program. The map and travel plans are sent to the user's fax machine and are updated if the user requests an update as traffic conditions change to as to offer a faster route. The user can also be notified when to turn if the DAN 8100 monitors the user's location and fax the user when the user is approaching a turn 7816. Again referring to FIG. 79, BOX 7914, if the user does not select “3”, the automated telephone system instructs the user, ‘To track a wireless device and have a map of their location sent to your wireless device, e-mail or fax, press or say “4” 7918. The automated telephone system then waits for the user to respond by selecting “4” 7920. If the user selects “4”, the DAN 8100 instructs the user to enter whether the tracking and map information should be sent to their wireless communication device, e-mail, website, navigational system, computer or fax. The users choice can be entered via a keyboard/keypad, voice recognition, interactive display screen or other. The DAN 8100 then instructs the user to input the wireless device area code and phone number, e-mail address, website address, navigational system address, computer address and/or area code and telephone number were the map and location information is to be sent regarding the wireless device being monitored. The DAN 8100 then sends a map and travel plans to the standardization/conversion hardware/software to convert the map and travel plan to a format, which will interface with the protocol of the user's wireless device, e-mail, website, navigational system, computer system or Fax machine/program. The map and location information are sent to the user's wireless device, e-mail, website, navigational system, computer system or fax machine and are updated if the user requests an update, as monitored wireless device travels from one location to another, or from time to time 7922. Again referring to FIG. 79, BOX 7920, if the user does not select “4”, the automated telephone system instructs the user, “To repeat these choices, press or say “5” 7924. The automated telephone system then waits for the user to respond by selecting “5” 7926. If the user selects “5”, the users query is returned to FIG. 79, BOX 7900, to repeat the choices 7928. Again referring to FIG. 79, BOX 7926, if the user does not select “5”, the automated telephone system instructs the user, “To return to the main menu, press or say “6” 7930. The automated telephone system then waits for the user to respond by selecting ‘6” 7932. If the user selects “6”, the users query is returned to FIG. 70, BOX 7006, to restart the query process 7934. If the user does not select “6”, the automated telephone system returns the user to FIG. 70, BOX 7046, to be connected with a Directional Assistance Operator 7936. FIG. 80 is a flowchart describing the operation of the DAN's traffic monitoring software 8125 and routing software 8120. To begin the query process, the traffic monitoring software 8125 and routing software 8120 plots the user's location. If the user is calling from a wireless device, the DAN 8100 queries the wireless network's ULD 900 to retrieve the user's longitude and latitude coordinates. The DAN 8100 then converts the longitude and latitude coordinates to a street address or location. This location is plotted into the traffic monitoring software 8125 and routing software 8120. If the user is calling from a landline within a PSTN 8138, the DAN 8100 retrieves the users location from the PSTN phone location database 8145. Then the DAN 8100 plots the street address provided by the PSTN phone location database into the traffic monitoring software 8125 and routing software 8120 BOX 8000. Still referring to FIG. 80, the DAN 8100 then plots the user's desired destination by cross-referencing and retrieving the destination information from the PSTN phone location database 8145. If the user has entered more than one destination, the DAN 8100 can plot multiple destinations for route planning purposes 8002. The traffic monitoring software 8125 and routing software 8120 them determines a selected number of possible logical driving routes and the distance in miles or meters for each possible route 8004. The traffic monitoring software 8125 and routing software 8120 then examines the movement of wireless devices that are traveling the possible logical routes to determine average speed or number of wireless devices on the possible logical routes 8006. The traffic monitoring software 8125 and routing software 8120 then calculates the estimated travel time for each route in order to determine the shortest possible travel time. Routes are considered in order of miles/meters from shortest to longest. The basic formula to obtain the travel time for a possible route is as follows: Distance(miles/meters)×Average Speed (Miles/Meters Per Hour)=Route Travel Time This is the basic formula, but other formulas may be entered into the traffic monitoring software 8125 and routing software 8120 to include such things as number of wireless devices on a route, weather conditions, posted speed limits, train schedules, road work, road closures, historical average speeds based on time of day/year, etc. 8008. The traffic monitoring software 8125 and routing software 8120 informs the user of the shortest or fastest route (as per their request) and sends the travel plan and map to the user if requested, in the form the user requested (Page to wireless device, e-mail, fax, etc.). If the user has requested to receive updates, the traffic monitoring software 8125 and routing software 8120 monitors the users location and informs them of faster routes, when to turn, and other requested items 8010. Detailed Description of the Preferred Embodiment The directional assistance network (DAN) 8100 is a machine and process that provides a dynamic location routing system and directional assistance to an entity though a variety of remote methods. One objective of the DAN 8100 is to provide a means for an entity to request mapping, voice, or other methods of directions that would give the said entity directions from entity's current geographic location to entity's target location. The routing system allows a. plurality of devices to connect to the DAN 8100 and request directional assistance to a plurality of target locations. The claimed entities could exist as a: Wireless device user Land line phone user Internet (world-wide-web) user Intranet user Non-human element such a software package Voice-over IP network user Dial-up user Other user selected entities The geographic location based technology would allow the said users to be routed along a path that would take the most direct or most timely route to the user's selected destination. For example, a user of a wireless device could query the DAN 8100 for a display of the user's current location on a street map, and the fastest driving route to the user's place of employment, based on current traffic conditions, distance, and other user defined attributes from available sources. The routing software 8120 within the DAN 8100 facilitates this process. The routing software 8120 allows a discrete computational analysis of traffic conditions based on recorded data from a plurality of sources. Current day realizable sources of this information are: data sampling from a wireless network, live national traffic alert databases, local traffic database entries, traffic cams, traffic radar gun” database, direct user input, or other available sources. The DAN 8100 also comprises traffic monitoring software 8125 that monitors traffic conditions in real time by, for example, tracking the movement of a plurality of wireless devices to determine the location of slow moving traffic. The routing software 8120 uses the traffic monitoring software 8125 to determine routing information, in order to provide directional assistance. This directional assistance is deliverable to the above listed entities. The user can select routing information based on the following: Time to destination Distance to destination Alternate routes based on ‘way points’ set by user Scenic routes (pre-programmed scenic information comprised within a criss-cross lat/long geographic database 8150) Routes bases on probability of reaching a destination within time constraints Routes to alternate locations of similar interest (Hospitals, etc) Routes based on user preferences established in a local preferences database. The first step of the routing software's 8120 is to retrieve the current geographic location of the requesting entity. The DAN 8100 retrieves the users current geographic location using the device location software 8115. The device location software 8115 allows the location of a wireless device, (and-fixed, Internet, or other user defined entity to be obtained. The device location software 8115 has the ability to query external sources for information. In the case of a wireless network, the device location software 8115 would analyze wireless network parameters and data at the base station controller (BSC) 206 or the MTX 130 for call information to determine the location of a wireless device. An additional technology that would allow rapid access to this data would be a dynamic database or system designed to store and hold information including latitude and longitude of the said wireless devices. The supporting databases required for the above claimed software to function include a criss-cross lat/long geographic database 8150. The crisscross at/long geographic database 8150 contains latitude and longitude information correlating to actual street locators, such as a directory of listings of business and residential address locations and contact information. Scenic locations, hospitals, and other ‘categorized’ locations could be extrapolated from this database. The geographic database mapping software 8155 controls the criss-cross lat/long geographic database 8150. The geographic mapping software 8155 allows multiple simultaneous requests, and is responsible for both resolving addressing information to latitude/longitude coordinates and resolving latitude/longitude coordinates to addressing information. To effective processing, the external connections to the criss-cross lat/long geographic database 8150, and primary logic software 8101, can utilize an ATM type packet routing. The ATM type pocket routing will allow very fast switching times and transfer speeds. To allow the entities to access the claimed primary embodiment, the DAN 8100 contains two similar software packages. The first software package is the voice interface software 8105. The voice interface software 8105 allows the user to access the functionality of the DAN 8100 via the human voice, To interpret the voice signal of the user, the voice interface software 8105 works with the voice mapping software 8110. The voice mapping software 8110 interprets voice signals from the user (spoken words) and converts the voice signals into data inputs for the voice interface software 8105. The voice mapping software 8110 allows the user to walk through a series of menus and input information. Menus such as “press 1 to spell or say the name of your destination” will be synthesized and presented to the human user. The user can then respond using their voice, “Hospital”. The voice mapping software 8110 would then resolve the spoken work “Hospital” into a data representation of the term. In addition, the voice mapping software 8110 allows target location information to be resolved into a data-formatted address that can be used along with the routing software to route directions, The next software component utilized by the DAN 8100 is the data interface software 8130. The data interface software 8130 receives input data in a usable format. The data interface software 8130 simply parses the supplied data and passes it to the DAN's 8100 primary logic software 8101. The external DAN query interface software 8135 allows external connectivity to the DAN 8100. The external DAN query interface software 8135 adapts and standardizes the many different physical interfaces and protocols that connects with the DAN 8100. The package is very important because it needs to be able to support many sophisticated entities that connects to the DAN 8100. The entities supply data in many different ways. These external connections to query devices 8140 can be: Physical Data connections (Ti, DCI, etc) Telephony connections Wireless network connection Direct Dial-up connection Data Formats SQL database entries Scripting Unformatted raw ascii text Formatted text WAP text entries Data Interface Protocols ftp http telnet dial-up direct-connect SMS The external DAN query interface software 8135 takes these external sources and formats the data stream that both the data interface software 8130 and the voice mapping software 8110 use to retrieve information from external sources. The DAN 8100 also includes the standardization/conversion hardware/software 8160. The standardization/conversion hardware/software 8160 is listed under the previously referenced provisional patent. The standardization/conversion hardware/software 8160 functions under a singleinput/single-output (SISO) type control structure, where a single input results in a single output. The standardization/conversion hardware/software 8160 receives a command from one protocol, and outputs the correct protocol to the receiving machine. The standardization/conversion hardware/software 8160 receives a command from an external network connection 8165 or from the primary logic software 8101. The standardization/conversion hardware/software 8160 first checks the received protocol against a pre-configured protocol, and then checks known types of protocols by querying an internal protocol database. If there is a matching protocol found within the internal protocol database, then the standardization/conversion hardware/software 8160 the appropriate protocol by checking the receive protocol list. The standardization/conversion hardware/software 8160 then determines if a conversion can be made. If the standardization/conversion hardware/software 8160 can convert the protocol command, then the command is sent to the connected device. The standardization/conversion hardware/software 8160 waits for another command. If any of the decision boxes are “no” than an error is recorded and send back to the sending source. The standardization/conversion hardware/software 8160 differs from the external DAN query interface software 8135 in that the DAN 8100 utilizes the standardization/conversion hardware/software 8160 to connect to networks or other devices and retrieve information used by various subroutines. The general example would be for the DAN 8100 to query a wireless network's MTX 130 and then BSC 206 to retrieve user information. Controlling all the software and hardware of the DAN 8101 is the primary logic software 8101. The primary logic software 8101 generates and processes the usage and pure control commands. Data storage is also part of the primary logic software 8101. The primary logic software 8101 must be able to process a large volume of external requests and processes created by entities requesting geographic routing information. The recommended physical architecture that the DAN 8100 would reside in a hardware that could supply enough bandwidth, memory, physical storage and processing ability to respond to an entities geographic routing request in a reasonable amount of time determined by a customer. The location that the DAN 8100 could exist can be any of the following: At a wireless switching office At telephony switching center/PSTN Located on the interne (with some static/dynamic range of IF addresses) In alternate embodiments where the DAN 8100 is located at locations other than a wireless network, additional equipment will need to be located at a wireless switch. The DAN linking software 8300 allows remote queries of the wireless switch. The DAN linking software 8300 connects to the e-mobility services 144 that links to the MTX 130. The DAN linking software 8300 includes the interim linking software 8515. The interim linking software 8515 negotiates and retrieves data from the MTX 130 or the BSC 206 components of a wireless switch. In addition, the DAN linking software 8300 includes packet routing software/hardware 8520 that allows packets to be passed from wireless devices (the WAP/e-mobility connections) to the DAN 8100 that is remotely located. The DAN linking software 8300 also includes the DAN data query software 8525 to manage the methods used to query the local wireless networks hardware/software. Routing Methodology to Obtain Directions for Requesting Entity When an entity connected to the DAN 8100 requests directions to an address or location, the DAN 8100 must have access to data sources that gives the location of the wireless device and the target location. The following are examples of data sources for obtaining this information: User location database (ULD)—containing mobile device location information 900 User location database coordinator (ULDC)—Containing ability to query multiple ULD's 908 Direct query of MTX 130 or BSC 206 for location of wireless devices Location information calculated by GPS at/in the wireless device Public addressing database containing addressing for location queried by wireless device. PSTN Database with a correlated latllong information for a fixed device, 8145 Location information sent from the querying device to the DAN 8100 When a wireless device requests directions to a location the following steps to carry out this process: The DAN determines the wireless devices current location in terms of latitude/longitude and converting to postal addressing relative to roadways. The DAN then determines the location of the target The DAN then calculates the route to the target through current streets and roads The DAN 8100 determines the wireless devices' location with the use of the criss-cross lat/long geographic database 8150, latitude/longitude coordinates obtained by GPS systems on the wireless device, a location retrieved though a ULD 900 or ULDC 908, or similar device that calculates the current location. The criss-cross lat/long geographic database 8150 can convert either an address to a latitude/longitude coordinate or a latitude/longitude coordinate into an address. After obtaining the location of the device in latitude/longitude coordinate form the information is processed and converted to standard addressing. Next, the DAN 8100 determines the target's location. The target location address could be resolved by querying a public addressing database for known locations. If the target location is another wireless device, the location would be retrieved though a ULD 900, or ULDC 908, or by querying the MTX 130 and/or the BSC 206 controlling the target wireless device, then converted to a standard address by the criss-cross lat/long geographic database 8150. Next, the DAN 8100 determines the most efficient route to the target address. While current commonly known software can accomplish this task, it is limited to resolving routes based on: Shortest distance (miles/Kilometers) traveled Time to arrive at destination User sensitive settings such as scenic routes What the commonly used software lacks is the ability to compensate for current road conditions (traffic jams, weather, etc). The DAN 8100 has the ability to resolve routes using information obtained from a wireless network or from other traffic databases, to determine the fastest route in units of time or distance. The routing software 8125 initially determines the route using commonly known methods, but then uses a unique and new method to check the level of traffic congestion along the route. The level of traffic congestion can be determined from either gathering information from traffic databases or from obtaining the location of devices on a wireless network. To gather the location of devices on any given segment of a road or route, data can be gathered from a MTX 130, in combination with a ULD 900 or ULDC 908, or direct query of the MTX 130 or the BSC 206. The information obtained from the ULD/ULDC/Direct Query includes the following: Number of wireless devices on the route calculated to target location Location of wireless devices on the route calculated to target location Current state (active/standby) of wireless devices along calculated route The routing software 8120 uses the route wireless device information to determine the congestion of the route. The congestion is measured by the following calculations. First, the location of the wireless devices is correlated to locations on the route. Next, the velocities of the wireless devices are calculated. The velocity is calculated by sampling the location of a device at fixed time intervals. The routing software 8120 then compares the velocities of the devices to the posted speed limits along the different segments of the route. The comparison measures the traffic flow and validates the devices that are in the traffic route and not on a sidewalk or other close area. In addition, the routing software 8120 calculates the wireless device geographic density along the route. Average and normal density would be calibrated depending on the size and attributes of the road. For example, a larger road would have a different average density than a smaller road. A multilane highway would have a different average density than a two-lane highway. The average values for wireless device density on roads would have to be adjusted for various road attributes. The routing software 8120 evaluates the current levels and compares them to the average value. After the routing software 8120 calculates the traffic density measurement, the routing software 8120 evaluates the traffic conditions along any given route. The routing software 8120 compares the calculated traffic density to a predetermined normal level. The comparison is described by the following: Dr=Dc/Dn, where Dr=density ratio, Dc=current density, and Dn=normal density. Using this formula, the density ratio for any traffic condition is calculated. For example, if a current traffic density of a geographic region is 100 units/distance, and the normal density is 50 units/distance, then the density ratio would be 2. The density ratio corresponds to 2 times or 200% more traffic than the normal traffic density for that area. The equation that determines the time it would take to cross a geographic segment is defined by the following formula: Time=α×eDr*β where α is an experimentally determined scaling factor that a network engineer can tune, and β is the normal time to cross the geographic segment. From this formula it is apparent that when is adjusted the time can be linearly scaled by the traffic engineer. It is also apparent that when the value of D changes that the Time changes exponentially. This should make since b/c as traffic increases, the time does not increases linearly For example, when Dr is 2 (2 times more or 200% the normal traffic) the time to reach the destination is not double the time, but less than that amount of time. Using the formula you can see the affects of the values of Dr and in FIGS. 86 and 87 respectively. After the time calculation is computed an adjusted travel time for the segment is sent to the routing software. Alternate routes based on normal traffic travel times are then send and run through this algorithm. When the route with least time based on actual traffic conditions is found, the DAN 8100 locks the route as the best traffic route. Each segment of the route is completed in this method. The result is a complete route from the origin of the device to the destination that allows for the quickest travel based on time. The DAN 8100 then sends the resulting route to the wireless device and the wireless device displays the route to the user. The user can then travel to the location. If the user desires, the software can continually monitor the route and alert the user to changing road conditions and report route corrections to the previous calculated directions. The user can then take additional detours to further speed the time or distance to the route. If the user requests directions to a wireless device on the wireless network, the calculated route would obviously not be a static route. The DAN 8100 would continuously update the route as required. The route could be calculated based on the route taken by the wireless device being tracked, or by simply using the method above to determining the fastest route to the target. The current state of the tracked wireless device would be taken into account. If the tracked wireless device were in an active state, then the route would update continuously. However, if the tracked wireless device is not active or if current location information is not available, then the route would not update, and the DAN 8100 can calculate the route using the last known location of the wireless device. The DAN 8100 would relay the tracked wireless device state to the requesting wireless device. Alternate Embodiment to the Directional Assistance Network The primary embodiment refers to a system that users on a plurality of devices (wireless/fixed location) may obtain directional mapping from their current locations. The DAN 8100 can also be implemented by an alternate method. The alternate method would include directional mapping databases and software integrated into its system. The method would not take into consideration traffic density and other variables that would affect directional routing. For the alternative method to work the wireless device would need to contain a map and a latitude/longitude referenced database of target locations. The databases could be cities, metropolitan areas, states, countries, or other variable sized geographic areas. The map would need to contain information on the current location of the wireless device. The wireless device could obtain the current location information from the device itself using GPS or from the wireless network. The database would need a large storage medium that could be created on a plurality of mediums including but not limited to: Hard Disk Micro Drive Optical Storage Medium (CD/DVD/etc) Flash Memory Device Memory Card EPROM EEPROM Removable Storage Medium The alternate embodiment requires the wireless device to have the ability to locate a destination based on address, company name, landmark, etc. If the wireless device cannot find the destination in the internal database, the wireless device queries the wireless network for the destination information. The wireless network server resolves the request. When the network server finds the destination information, it sends back the latitude and longitude of the destination to the requesting wireless device. The wireless device stores and appends the destination information with the latitude/longitude in the local database for subsequent path resolution. If the wireless network server does not find the destination, then the wireless device alerts the user that the device could not find the destination. Advantages of the alternative embodiment are the user will be able to: Obtain faster routing information Not inquire a connection cost Not require an active connection to the network To allow faster routing, the wireless device can query the wireless network server for traffic congestion information. To allow faster routing of the wireless device in regards to time to the destination or for multiple waypoints and then a destination, a query to the server could be requested if a network connection is available. This would allow the network to access traffic databases that contain information on traffic congestion along a route to be analyzed. Each segment of a route could be analyzed and assigned a numerical figure representing the expected amount of time to travel through the segment. The routing at the server could then send corrections to the device and make alterations to the routing information to improve the results given to the user. The connection to the network by a device would require any, but not limited to, the following connections that could be resolved and eventually routed to TCP/IP or other I routing protocols: TCP/IP Network Connection IPX/ULD PPP/SLIP Wireless Networks 2G 3G 2.5G GSM TDMA CDMA CDMA2000 Direct Connection To make the computations the wireless network the following are required: a database of a plurality of geographic locations with addressing correlated to latitude and longitudes; software to determine the time to travel on a given route; logistic software to determine a faster route; interface with the requesting software. The logistics software works by accessing traffic condition databases not claimed by this patent. The basic requirement of the databases is to return information that corresponds to the traffic density of a roadway or other geographic location. When the logistics software acquires this information, the software compares the current traffic density to a predetermihed normal level. The resulting route can then (after being calculated) be sent to the wireless device or may already exist there and will not need to be updated in this case. The route will then be graphically reproduced or printed as text and displayed to the user. The user can then travel to the location. Description of Figures FIG. 81 FIG. 81 describes the structure of the DAN 8100. The figure shows the DAN 8100 with all the components logically connected. In addition, the figure illustrates the connectivity of the DAN 8100 to external sources. The figure also illustrates other devices internal to the DAN 8100. The DAN 8100 contains two external connectivity points. The tandardization/conversion hardware/software 8160 connects to an external network connection 8165 and connects the DAN 8100 to friendly networks used to obtain additional data. The external directional assistance network query interface software 8135 connects to external connections to query devices 8140. The connection point connects to devices/entities that can remotely query the DAN 8100. Both the standardization/conversion hardware/software 8160 and the external DAN network query interface software 8140 interface with the primary logic software 8101. The primary logic software 8101 handles the primary control and processing for the DAN 8100. The primary logic software 8101 controls the interaction between the different internal components and external interfaces, and processes all requests by the different components. The data interface software 8130 and voice interface software 8105 allow interactivity to external entities accessing the DAN 8100. Both components interface with the primary logic software 8101. The voice interface software 8105 utilizes the voice mapping software 8110. The voice mapping software also interfaces with the primary logic center 8101. The routing software 8120 component interfaces directly with the primary logic software 8101. The routing software 8120 utilizes the traffic monitoring software 8125. The routing software 8120 utilizes the device location software 8115 indirectly. The device location software 8115 interfaces with the primary logic software 8101. Any access of the device location software 8115 must be done through the primary logic software 8101. The database attached to the DAN 8100 is the criss-cross latllong geographic database 8150. The geographic database mapping software 8155 controls and interfaces with the criss-cross at/long geographic database 8150. Both of these components interface with the primary logic software 8101. The primary logic software 8101 also interfaces with the PSTN phone location database 8145. FIG. 82 FIG. 82 illustrates the primary embodiment of the invention; the DAN 8100 co-located at a wireless network. FIG. 82 displays devices that interact with the DAN 8100. Wireless communication device 8205 connects to cellular towers 8235, Via Ti/other connection links 8232 from the BTS 108, the wireless communication device 8205 connects with the cellular base station controller (BSC) 206. The BSC 206 links 8227 to the MTX 130. The MTX 130 links to the e-mobility services 144. The e-mobility services 144 links to the DAN 8100. The user location database (ULD) 900 and the wireless communications device location software 8270 also connect to the MTX 130. The MTX 130 links to the packet data network (PDN) 156, and to an internet gateway, 8255 and finally to the Internet 8260. The MTX 130 also links to a publicly switched telephony network (PSTN) 138. The PSTN 138 contains the PSTN phone location database 8145. The PSTN 138 connects to fixed location phones 8220 via land lines 142. FIG. 83 FIG. 83 illustrates the primary embodiment's alternate location; the DAN 8100 located remotely via the Internet 8260 at a remote server. FIG. 83 displays devices that ultimately interact with the DAN 8100. Wireless communication devices 8205 connect to cellular towers (BTS) 108. Via Ti/other connection link 8232 from the BTS 108, the wireless communication devices connect with the base station controller (BSC) 206. The BSC 206 links 8227 to the MTX 130. The MTX 130 links to the packet data network (PDN) 156 that links to the internet gateway 8255. The internet gateway 8225 links to the Internet 8260. The DAN 8100 interfaces 8310 the wireless network through the Internet 8200. The ULD 900 and the wireless communications device location software 8270 also connects to the MTX 130. The MTX 130 links to the e-mobility services 144. The e-mobility services 144 links to the DAN linking software, 8300. The MTX 130 also links to a publicly switched telephony network (PSTN) 138. The PSTN 138 contains the PSTN phone location database 8145. The PSTN connects to fixed location phones 8220 via land lines 142. FIG. 84 FIG. 84 illustrates the DAN 8100 remotely located at the PSTN 215. FIG. 84 displays devices that ultimately interact with the DAN 8100. Wireless communication devices 8205 connect to cellular towers (BTS) 108. Via Ti/other connection link 8232 from the BTS 108, the wireless communication devices 8205 connect with the wireless base station controller (BSC) 206. The BSC 206 links 8227 to the MIX 130. The MTX 130 connects to the PSTN 138 and then to the DAN 8100. The PSTN connects to other remote PSTN switching centers also. The PSTN 138 contains the PSTN Phone Location Database 8145. The PSTN 138 connects to fixed location phones 8220 via land lines 142. The MIX 130 links to the e-mobility services 144. The e-mobility services 144 links to the DAN linking software 8300. The user location database (ULD) 900 and the wireless communications device location software 8270 also connect to the MIX 130. FIG. 85 FIG. 85 illustrates the DAN linking software 8300 used by the DAN 8100. The DAN linking software, 8300, allows the DAN 8100 to interface with wireless networks, when it is remotely located. Wireless communications devices 8205 send requests to the DAN 8100 signals via e-mobility services, 144. The interim linking software 8515 receives the signals and routes them to the packet rerouting software/hardware 8520. Packets are then routed to the remotely located DAN 8100. The DAN data query software 8525 connects to the interim linking software 8515. The DAN data query software 8525 allows the DAN 8100 to remotely pass queries to the MTX, 130, which via the e-mobility services 144. FIG. 86 FIG. 86 shows the Traffic Time Calculation Performance Based on user or network-defined variables. The figure shows the alpha, an experimentally obtained scaling factor, on the traffic density-time algorithm. The network engineer determines the value of the variables. As shown, the effects of alpha are linearly proportional to the output of the algorithm. So an increase in one variable proportionally affects the output of the equation. FIG. 87 FIG. 87 shows the traffic time calculation performance based on a variable traffic density ratio. The effects of Dr, the density ratio is shown to produce an exponential result for the expected time to travel on any given route. When the traffic density compared to the normal density level increases, as expected the time to travel along that route increases exponentially as well. Pro-Active Traffic Routing System Overview The traffic control system allows network traffic engineers to optimize traffic flow in real-time based on feedback from systems such as the DAN and the LTS. Both of these system poll on data from other resources such as the ULD/ULDC and GPS data from mobile devices. The location tracking system allows network software located (physically or virtually) at the MTX to access information on the movement of mobile devices on a cellular network. These moving devices, tracked by the LTS, can be filtered to include only devices on roadways, which is of interest and is used by programs such as the DAN to route users from one location to the next allowing them to avoid traffic congestion. This congestion is based on mobile unit density on the roadways. Of interest to the traffic control software is the density of traffic along roadway section that have various traffic control devices that can be altered remotely. Altering their parameters would allow traffic flow to be altered and ease congestion. Automating this process, the traffic control software would, in real time, allow traffic congestion reduction over many roadways that otherwise would take much longer to implement. These changes are based on various methodologies described in the following text. Additionally, basic software architecture for such a system is recommended, but does not limit the spirit of this invention. Traffic Control Devices To discuss the ability to monitor or control traffic flow, the devices that control this factor should be discussed. Not all devices that control traffic flow can be remotely controlled, and thus cannot be used by the traffic control software. The devices that can work in this system will be listed and discussed in broad terms, as to allow them to apply to many design n a generic sense. Particular devices may be extruded from these descriptions and easily adapted to any specific setup. The following generic devices are usable for the traffic control system: Intersection Traffic Control Lights Highway Inlet Traffic Control Lights Variable Speed Limit Roadway Signs Intersection traffic control lights are defined as those lighting systems that include roadway intersection of two or more roadways at a single point, with a lighting system that directs what road way should cross at any given time. Variables that are affected here are the length any roadway may go cross the intersection, and the length of a turn lane being able to direct traffic from one lane to the next during that cycle. Highway inlet traffic control lights are a simple way to moderate and control the inlet of traffic onto major roadways. These roadways are typically one directional and the inlet is also one directional. The lighting system is usually an on/off system. A red light moderates traffic by allowing one car though at a time, and then stopping the next car for a time limit, then allowing it to pass and enter the highway. The control variable is the hold time between letting cars though. Variable speed limit roadways signs are signs that can alter posted speed limits based on a remote signal. The speed limit can be controlled remotely thus allowing the posted limit to change and thus control the flow of traffic. The variable here is the posted speed limit. Detecting Traffic Congestion Traffic congestion that can be alleviated by a controllable traffic control device must exist at the geographic site of the device. In other words, a device cannot alter congestion for which its function plays no role. The congestion must be co-located at the devices location, or in its field of control. Many devices have a range of control. The specific devices must have their characteristics programmed into the software. These characteristics include range and in what direction, that the device affects flow control. Also, the flow control depends on the type of device. To detect the traffic congestion the traffic control software must know the location of each device. The system must then know the range and direction to monitor for congestion. These characteristics, as described above, will allow a profile to be sent to the LTS for each device. The LTS can return the traffic density and average velocity of the mobiles in this region. This information will show the levels of congestion. There should be limits at which the system will modify default values. It should not be necessary to modify the defaults if there is little congestion, as it would result in little or no change to the roadway traffic. More specifically, for a generic system, the traffic can be monitored in all indicated directions for the defined distance for each. Some default traffic density value should be defined for all directions. Some speed value for traffic can also be assigned. Four possible methods of congestion can be used. The first is to use the system in the DAN. The second is to look at the average velocity of the devices on a roadway. The third is to look at the density of the mobile devices against some default value. The fourth is to look at both the density and the velocity of the devices. Using the forth method, a formula such as multiplying the average speed and density together to result in a number could allow a basis for more accurate congestion detection. Again a default value could be defined as to indicate when it is exceed that traffic congestion is bad. An additional value that indicates the severity of congestion could be the percent that the roadway is congested over its default value. These methods should be chosen based on need and function on any particular design. Further in this description, it will be implied that this method results in two categories, pass and fail. Pass is that the threshold is not met and normal traffic exists. Fail indicates that the limit has been exceeded and the traffic is above tolerable limits. Described as follows are methods to control and alleviate congestion based on device type. Methodology for Alleviating Congestion Various methods are needed based on the type of traffic control device. Described for each classification of device, are the methodologies to reduce congestion. Intersection Traffic Control Lights The congestion of traffic control lights should be monitored in the direction of the lighting system along the intersecting roadways for a reasonable distance. This distance can be defined and included in software programming, but a typical value may be 50% of the distance to the next intersection controlled by a traffic control light. This value could vary from one traffic lighting system to the next. The system should start by analyzing traffic congestion along all roadways at the intersection. The roadways should then either be classified as pass or fail. All fail roadways should have a percentage calculated that indicates the amount over the default value that they are congested. To alleviate the traffic, the roadways that are above the limit should be placed in order of descending percent over-congestion. The most congested roadways should have the timing adjusted such that they are allowed additional time on the crossing direction of the intersection. This would represent a longer green light. This would also scale the turn signal direction. The time increase could be proportional to the percent over-congestion. The second, and descending congestion roadways could function in a similar manner, but give less than the same increase. The roadways with no congestion would have the time crossing decreased. One additional factor is the time to cycle between all roadways (green light offered for every roadway in intersection). This should increase by some defined amount based on the number of congested roads. There should be a limit though programmed into the software. All timings for individual directions should sum up to this time. To accomplish this, it would be necessary to decrease the total time allowed for crossing on the non congested directions, when and increase occurs in the congested directions. Note, that if no directions are congested, then no changing in timing occurs. Highway Inlet Traffic Control Lights This system is relatively simple and is based on the ability of the traffic control system to use the LTS to determine only the traffic density of the roadway that the inlet lets into. The density should examine the average density along the roadway, again using some distance defined for the inlet control device. The period that the device allows cars to pass is inversely proportional to the density of the traffic along this distance. A set of criteria should be established that would adjust the timing for various densities. Lesser densities mean more cars per unit time can safely enter the highway. The converse is similarly true. These exact timings depend on particular roadways and should be unique to every device and configured initially based on field experiments. Below is an example that demonstrates these criteria for a generic system, using generic values: Traffic Density Inlet Entrance Rate 10 cars/100 m 20 cars/minute 20 cars/100 m 15 cars/minute 30 cars/100 m 10 cars/minute 40 cars/100 m 5 cars/minute Variable Speed Limit Roadway Signs This is a method very similar to above, but is mainly a safety feature that can reduce the possibility of an accident, and thus the primary case for traffic delays, roadside accidents. The system is inversely proportional to traffic density as above. The system should poll the LTS for device density for a distance defined for the specific device. The speed then should be adjusted to levels that are safe for various traffic densities. As cars are closer together, the safe speed limit decreases. Various brackets of speed to indicate for various ranges of traffic density could be defined and integrated into the software. The traffic control software than can automatically adjust the speed values based on traffic density. Basic Software Requirements The software architecture of this system is designed so it can be collocated at the MTX or virtually hosted elsewhere but assessable to the MTX. The software should have access to the LTS and have subroutines written to allow it to submit tracking queries to the LTS to determine traffic density and other necessary factors. The system should be designed to have an administrator's option to enable and disable the system and any particular devices. The system should allow a device to be added and all its parameters added as well. As each device is added, a device ID can be associated. This device ID would allow each device to be distinguished among each other. The system could then send electronic signals to the devices though direct or indirect routes to modify parameters on each device. These routes can be custom design or pass over public or private networks that connect the two points. The devices and their modification methodology are not the focus of this patent, however these devices are commonly known technology and software can easily be integrated into this that allows remote control to occur. Call Routing System Overview The call routing system allows a user to have calls that are intended for the users mobile device, routed to alternate location, based on the current location or the device and its proximity to the said alternate locations. The user has the option to supply the phone numbers of devices that the user would like it devices to auto-route incoming calls to when the user is near those locations, and when the feature is activated. The user also submits a geographic distance from the device that when the user's device enters into, will activate the routing feature and allow the user the option of having its calls routed to the new device (user is asked if the new location, is acceptable for routing by SMS or similar 2-way message from server). When the user exits the region near the device (as listed in his preferences) the system again asks if the user wants call to be routed back to the users mobile device. If the user has no devices near them, a feature also allows nearby public devices to be offered to the user as alternate locations for routing. The call routing system also allows for outing call routing which allows a user, service provider or manufacturer to route outgoing calls to selected phone numbers based on the location of the wireless device. For example, if a user dials “911” for emergency services, the call will be routed to the closest “911” call center, based on the location of the wireless device. An other example of the outgoing call routing system would be a user accessing the internet. When the user dials to connect to the internet, her call may be routed to a local internet access number based on the location of the wireless device. This outgoing call routing system will enable a user of a wireless device to optimize the use of his wireless device by receiving better service at a lower cost. System Design and Function For the routing system to function, the system must deploy its software at the MTX of a cellular provider. An alternate location on a intranet or internet is possible, but would require the MTX to link to that service and transport method. The software would rely on a service such as the LTS to allow monitoring and tracking of mobile devices. It also requires a database of user preferences that include: routing numbers and distance from routing numbers to activate routing. Authentication and other system level information for users should also exist. A plurality of users may activate the system, and the system will function for all active users. The LTS acts as an cooperative program that helps the current embodiment in many ways, as listed below. This software requires the flowing methods and function as listed below to be carried out to function properly. Determining Location of User To allow the system to operate the user of a mobile device must have his or her devices location monitored by the network. To do this, various methods exist such as the directional assistance network (DAN). The DAN allows a device to be monitored for location and additionally allows system events to be triggered based on the location of the device. The main requirement is that the location of the device be stored in a database or other location such that an external program can queue this information. A possible way to implement this is to use a User Location Database or a User Location Database Network. Other methods would be direct querying of the MTX or BSC to determine the location of a said mobile device, or a mobile device equipped with location information such as GPS or triangulation. Determining Phones Near to User To determine the fixed phones near a mobile device the system must first obtain the location of the said mobile device. When the system, using any of the above methods as further explained in accompanying documentation (on LTS, ULD, ULDC), has acquired the devices location, it stores it to a temporary register (software variable). The system must then check the user preferences, as stored in a local or remote configuration file, to determine the routing protocols. In this case, it must check the configuration to see if the user has indicated a phone number to route calls to. If no number exists then the system can attempt to route the call to any public telephone device in the vicinity. Routing to a private phone system would also be possible, but security and privacy concerns would hamper this. But for completeness, the methodology here applies to all cases. If the system checks the configuration and no devices are listed, or no devices near the mobile device (near implies a distance parameter that is in the configuration file) exist, then the mobile devices can be sent a message alerting the user that private devices were found. If this is the case, then the user can reply with three options: Route to nearest public device Route to new private device (user must enter new device ID) Turn off Routing Determining Public Phones Near to User The user has the option to have the call routed to the nearest public device. If the user chooses this option than the system would query the PSTN and retrieve all public phones within the following parameters. The system currently would have the geographic location of the mobile device. Using the PSTN's public phone network database it would query for a list of devices within the mobile devices telecommunication sub-region. These sub-regions are determined by the telecommunications company, and having indicated a particular region, the system can then retrieve all public device phone numbers. Having done this, the phone numbers can then be submitted again to the PSTN to resolve their addresses. Using commonly known techniques the system can then calculate the distance form the user (user's device) to the public phone(s) retrieved from the PSTN. The nearest device would then be chosen. This device and its address would then be sent to the user via the messaging capability of the phone, possible using wireless internet or other e-mobility techniques. The user may accept or reject the location. If the user accepts the location then the user would have calls that were routed to his mobile devices, rerouted to the public device. If the user rejects the location, subsequent locations based on distance can be presented (closest to furthest). The user may again either at any time, add a private number, accept the public location, or turn off routing. Determining Fixed (Private) Phones Near to User If the user has entered a list of private numbers in the configuration file, or adds a private number when no device in its proximity is found, the system can apply a simpler technique than above. The system can use the features of the LTS to its advantage by setting alert modes. These alert modes will be to create a custom tracking criteria for the device. The tracking criteria would be to create circular regions with a radius found in the configuration file, and instruct the LTS to alert the program when a user enters/exists these regions. Thus two options can exist when a user activates tracking: a user turns on tracking while in a region, a user turns on tracking while not in a region. If the user is not in a region then the system will not receive a message from the LTS, it can then as above, ask the user if they wish to search for a public device. A second option should be to allow the user to disable public device searching. Thus, a user may not be near a routable location (based on locations in a configuration file) but when a user does enter a region, the system will be alerted by the LTS. When the system is alerted of a user entering a specific region near a listed private phone, then the system will route calls to this device. Conversely, when the user exists this region, the LTS will again notify the system and the users calls will not be routed. As before with the public system, the user (user's device) will be sent a message to ask if routing preferences should be changed. The user can chose to accept new routing or decline it. If routing is declined, then the system will ignore the LTS alert when the user exists the region of the private line. It should however then receive the alert when a user enters another private device region and again prompt the user. Determining Mobile Phone Near to User When in the above case a user places in his configuration, or when prompted to add a private device (via a message sent to the mobile device), a routing destination that is itself a mobile device the system must add another subroutine to handle this. The procedure above for a private fixed land phone is the same until the location for the device at the PSTN is queried. At this point, the PSTN would return a result that indicates that the device is a mobile phone. The PSTN would also indicate the service provider for the device. With this information there are 3 different ways to obtain the location of the device. The first approach is to use the ULDC network to retrieve the devices location. A second, is to query the service provider (possibly the same service provider as the active user) through a cooperative data sharing agreement and retrieve the mobile location on a ULD. The third option is to directly query a BSCIMTX for information to resolve the mobiles location. When the tracking system is activated, all number indicated to be mobile numbers will require the system to periodically refresh the location of the devices. This time between refreshing can be configured by a system configuration parameter. When the device is refreshed, a new tracking criteria will be submitted to the LTS and the old criteria deleted. Besides these alteration, the system works just as it did for the land fixed device routing. System Routing Change When the mobile device has a new forwarding location the system then forwards this new phone number to the routing ability function of the cellular network. This allows external requests from outside the MTX (incoming calls) to be forwarded to a new number supplied from the current embodiment. Methods to Alert User of Device of Routing Information Many methods in current software and hardware designs of cellular networks exists to allow 2 direction communication from a software program on a MTX/lntranet to communicative with a mobile device. Methods which exist now that can accomplish the necessary tasks are: SMS Wireless Internet WML Proprietary Software These methods would require the user to respond in some cases. The system would then receive a response from the user, which would contain the users phone ID thus allowing the system to route the response to the particular mobiles preferences and routing queues. Geographic Advertising System Summary The geographic advertising system (GAS) is a geographically based advertising system which enables the delivery of targeted advertising to and from wireless device users based on their geographic location. GAS monitors the movement of wireless users via monitoring hardware and software connected to a wireless network or user location database, and when a wireless device meets a certain criteria, the wireless device user may by targeted for an advertising solicitation. For example, a user of a wireless device who has traveled outside his home calling area, may receive a text message on his wireless device telling him of a discount on a hotel room in the area. A business initiated solicitation to a wireless device may be triggered by: Distance between wireless device and soliciting business Location of the wireless device's home calling area Demographic information (age, sex, race, etc.) Historic travel patterns If wireless device is currently geographically located at a particular location (For example, shopping at the competition's store) Other defined criteria The solicitation may be delivered by; A text message to the wireless device A phone call to a wireless device A message deposited in the users voice mail An e-mail Postal mail A user of a wireless device may also initiate a solicitation by, for example, requesting the prices of hotel rooms within a given geographic radius. For a user initiated solicitation, the user may sort by: Type of goods and services Name of business providing goods and services Price of goods and services Distance to goods and services Other defined criteria This GAS can work in conjunction with the DAN or other mapping software to provide driving directions, for example, to the hotel which is soliciting the user. BSC BASE STATION CONTROLER BSS MANAGER BASE STATION SUBSYSTEM MANAGER BTS BASESTATION TRANSCIEVER SUBSYSTEM GPS GLOBAL POSITIONING SYSTEM HLR HOME LOCATION REGISTER MTX METROPOLITAN TELEPHONY EXCHANGE PSTN PULBLIC SWITCH TELEPHONY NETWORK RF RADIO FREQUENCY RSSI RECEIVE STRENGTH SIGNAL TDOA TIME DIFFERENCE OF ARRIVAL ULD USER LOCATION DATABASE ULDC USER LOCATION DATABASE COORDINATOR ULDCN USER LOCATION DATABASE COORDINATOR NETWORK USER LOCATION DATAB SE MANAGER ULDM"},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE INVENTION <EOH>Wireless networks 100 are becoming increasingly important worldwide. Wireless networks 100 are rapidly replacing conventional wire-based telecommunications systems in many applications. Cellular radio telephone networks (“CRT”), and specialized mobile radio and mobile data radio networks are examples. The general principles of wireless cellular telephony have been described variously, for example in U.S. Pat. No. 5,295, 180 to Vendetti, et al., which is incorporated herein by reference. There is great interest in using existing infrastructures of wireless networks 100 for locating people and/or objects in a cost effective manner. Such a capability would be invaluable in a variety of situations, especially in emergency or crime situations. Due to the substantial benefits of such a location system, several attempts have been made to design and implement such a system. Systems have been proposed that rely upon signal strength and triangulation techniques to permit location include those disclosed in U.S. Pat. Nos. 4,818,998 and 4,908,629 to Apsell et al. (“the Apsell patents”) and U.S. Pat. No. 4,891,650 to Sheffer (“the Sheffer patent”). However, these systems have drawbacks that include high expense in that special purpose electronics are required. Furthermore, the systems are generally only effective in line-of-sight conditions, such as rural settings. Radio wave multipath, refractions and ground clutter cause significant problems in determining the location of a signal source in most geographical areas that are more than sparsely populated. Moreover, these drawbacks are particularly exacerbated in dense urban canyon (city) areas, where errors and/or conflicts in location measurements can result in substantial inaccuracies. Another example of a location system using time difference of arrival (TDOA) and triangulation for location are satellite-based systems, such as the military and commercial versions of the global positioning satellite system (GPS). GPS can provide accurate position from a time-based signal received simultaneously from at least three satellites. A ground-based GPS receiver at or near the object to be located determines the difference between the time at which each satellite transmits a time signal and the time at which the signal is received and, based on the time differentials, determines the object's location. However, the GPS is impractical in many applications. The signal power levels from the satellites are low and the GPS receiver requires a clear, line-of-sight path to at least three satellites above a horizon greater than about 60 degrees for effective operation. Accordingly, inclement weather conditions, such as clouds_, terrain features, such as hills and trees, and buildings restrict the ability of the GPS receiver to determine its position. Furthermore, the initial GPS signal detection process for a GPS receiver can be relatively long (i.e., several minutes) for determining the receiver's position. Such delays are unacceptable in many applications such as, for example, emergency response and vehicle tracking. Additionally there exists no one place that this location information is stored such that a plurality of wireless devices 104 could be located on a geographic basis."},"summary":{"kind":"string","value":"<SOH> Summary of Factors Affecting Rf Propagation <EOH>The physical radio propagation channel perturbs signal strength, causing rate changes, phase delay, low signal to noise ratios (e.g., ell for the analog case, or E b /no, RF energy per bit, over average noise density ratio for the digital case) and doppler-shift. Signal strength is usually characterized by: Free space path loss (L p ) Slow fading loss or margin (L slow ) Fast fading loss or margin (L fast ) Loss due to slow fading includes shadowing due to clutter blockage (sometimes included in 1.p). Fast fading is composed of multipath reflections which cause: 1) delay spread; 2) random phase shift or rayleigh fading, and 3) random frequency modulation due to different doppler shifts on different paths. Summing the path loss and the two fading margin loss components from the above yields a total path loss of: in-line-formulae description=\"In-line Formulae\" end=\"lead\"? L total =L p ±L slow +L fast in-line-formulae description=\"In-line Formulae\" end=\"tail\"? Referring to FIG. 3 , the figure illustrates key components of a typical cellular and PCS power budget design process. The cell designer increases the transmitted power P TX by the shadow fading margin L slow which is usually chosen to be within the 1−2 percentile of the slow fading probability density function (PDF) to minimize the probability of unsatisfactorily low received power level P RX at the receiver. The P RX level must have enough signal to noise energy level (e.g., 10 dB) to overcome the receiver's internal noise level (e.g., −118 dBm in the case of cellular 0.9 GHz), for a minimum voice quality standard. Thus in the example P Rx must never be below −108 dBm, in order to maintain the quality standard. Additionally the short term fast signal fading due to multipath propagation is taken into account by deploying fast fading margin L fast , which is typically also chosen to be a few percentiles of the fast fading distribution. The 1 to 2 percentiles compliment other network blockage guidelines. For example the cell base station traffic loading capacity and network transport facilities are usually designed for a 1−2 percentile blockage factor as well. However, in the worst-case scenario both fading margins are simultaneously exceeded, thus causing a fading margin overload."},"cpc_label":{"kind":"string","value":"H04W4023"},"filing_date":{"kind":"string","value":"20170927"},"patent_issue_date":{"kind":"string","value":"20180313"},"date_published":{"kind":"string","value":"20180208"},"examiner_id":{"kind":"string","value":"67921.0"},"ipc_label":{"kind":"string","value":"H04W402"},"npe_litigated_count":{"kind":"number","value":5,"string":"5"},"examiner_full_name":{"kind":"string","value":"PATEL, AJIT"},"invention_title":{"kind":"string","value":"INTERNET QUERIED DIRECTIONAL NAVIGATION SYSTEM WITH MOBILE AND FIXED ORIGINATING LOCATION DETERMINATION"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"H04W"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32887,"cells":{"application_number":{"kind":"number","value":15717359,"string":"15,717,359"},"decision":{"kind":"string","value":"ACCEPTED"},"title":{"kind":"string","value":"PROTOCOL FOR LIGHTING CONTROL VIA A WIRELESS NETWORK"},"abstract":{"kind":"string","value":"A monitor lighting control device receives a state change event message that includes a payload specifying: (i) a state change event of an occupancy, audio, or daylight sensor, or a switch to turn lighting on/off, dim up/down, set scene or the like; (ii) an identifier of a member lighting control device that detected the state change event; and (iii) a lighting control group identifier of a lighting control group that includes the member lighting control device and the monitor lighting control device. The monitor lighting control device transmits an acknowledgement of receipt of the state change event message to the member lighting control device. The monitor lighting control device generates a state change multicast message that includes the state change event of the payload. Also, the monitor lighting control device transmits the generated state change multicast message to the lighting control group."},"claims":{"kind":"string","value":"1. A lighting control system comprising: a lighting control group, including a group monitor, a member lighting control device, and a luminaire; wherein the group monitor comprises: a wireless radio communication interface system configured for wireless communication over a wireless lighting control network communication band; a processor; a memory accessible to the processor; and programming in the memory which configures the processor to: receive via the wireless radio communication interface a state change event message including: (i) a state change event of an occupancy sensor, an audio sensor, a daylight sensor, or a switch to turn lighting on/off, dim up/down, or set scene; and (ii) an identifier of the member lighting control device that detected the state change event; generate a state change message that includes the state change event; and transmit via the wireless radio communication interface the generated state change message to members of the lighting control group. 2. The lighting control system of claim 1, wherein the state change event message further includes: (iii) a lighting control group identifier of the lighting control group that includes the member lighting control device and the group monitor. 3. The lighting control system of claim 1, wherein the state change event message is received via unicast communication. 4. The lighting control system of claim 1, wherein the generated state change message is transmitted via multicast communication. 5. The lighting control system of claim 1, wherein the generated state change message is transmitted via broadcast communication. 6. The lighting control system of claim 1, wherein the programming in the memory further configures the processor to: transmit the generated state change message to the members of the lighting control group at least two times. 7. The lighting control system of claim 1, wherein the programming in the memory further configures the processor to: look up identification for a set of lighting control devices that are members of the lighting control group in a lighting control group network table; generate a check message for the identified set of lighting control devices to confirm receipt of the generated state change message; and send the check message to each of the identified set of lighting control devices. 8. The lighting control system of claim 7, wherein the check message is unicasted to each of the identified set of lighting control devices in order as specified in the lighting control group network table. 9. The lighting control system of claim 8, wherein the programming in the memory further configures the processor to: in response to unicasting the check message, receive an acknowledgement message from each of the identified set of lighting control devices indicating success or failure to execute illumination operation based on the state change event. 10. A member lighting control device comprising: a wireless radio communication interface system configured for wireless communication over a wireless lighting control network communication band; drive/sense circuitry to detect a state change of an occupancy sensor, an audio sensor, a daylight sensor, or a switch to turn lighting on/off, dim up/down, or set scene; a processor coupled to the drive/sense circuitry; a memory accessible to the processor; and programming in the memory which configures the processor to: detect a state change event of the occupancy sensor, the audio sensor, the daylight sensor, or the switch via the drive/sense circuitry; in response to the detected state change event, generate a state change event message including: (i) an identifier of the member lighting control device, (ii) the state change event, and (iii) a lighting control group identifier of a lighting control group that includes the member lighting control device; transmit via the wireless radio communication interface the state change event message to a group monitor of the lighting control group; and upon failing to receive an acknowledgement of the state change event message from the group monitor within a predetermined time period, transmit via the wireless radio communication interface the state change event message including the state change event to members of the lighting control group. 11. The member lighting control device of claim 10, wherein the state event message is transmitted to the group monitor via unicast communication. 12. The member lighting control device of claim 11, wherein the programming in the memory further configures the processor to: upon failing to receive the acknowledgement of the state change event message from the group monitor within the predetermined time period, determine the failure to receive the acknowledgement of the state change event message from the group monitor is a communication fault. 13. The member lighting control device of claim 10, wherein the state event message is transmitted to the members of the lighting control group listening on a broadcast channel or an address of the lighting control group. 14. The member lighting control device of claim 10, wherein the state event message is transmitted to the members of the lighting control group via multicast communication. 15. The member lighting control device of claim 10, wherein the programming in the memory further configures the processor to: upon failing to receive the acknowledgement of the state change event message from the group monitor, increase power of the wireless radio communication interface prior to transmitting the state change event message to the members of the lighting control group. 16. The member lighting control device of claim 10, wherein the programming in the memory further configures the processor to: after transmitting the state change event message to the members of the lighting control group, initiate a re-survey of radio frequency (RF) connectivity with the group monitor. 17. A luminaire comprising: a wireless radio communication interface system configured for wireless communication over a wireless lighting control network communication band; a processor; a light emitting diode (LED) light source; an LED driver circuit to drive the LED light source; a memory accessible to the processor; and programming in the memory which configures the processor to: receive via the wireless radio communication interface a state change message from a group monitor including: (i) a state change event of an occupancy, an audio sensor, a daylight sensor, or a switch to turn lighting on/off, dim up/down, or set scene; and (ii) a lighting control group identifier of a lighting control group; receive via the wireless radio communication interface a confirmation message from the group monitor to confirm receipt of the state change message; send an acknowledgement message of the confirmation message via the wireless radio communication to the group monitor to confirm receipt of the state change message; check the lighting control group identifier to determine whether the luminaire is a member of the lighting control group specified in the state change message; and upon determining that the luminaire is a member of the lighting control group, adjust illumination light output of the LED light source via the LED driver circuit in accordance with the state change event. 18. The luminaire of claim 17, wherein the state change message is received via multicast communication. 19. The luminaire of claim 17, wherein the confirmation message is received via unicast communication. 20. The luminaire of claim 17, wherein the programming in the memory further configures the processor to: before adjusting illumination light output of the LED light source via the LED driver circuit in accordance with the state change event, determine that the luminaire has not already acted in accordance with the state change event specified in the state change message."},"description":{"kind":"string","value":"CROSS-REFERENCE TO RELATED APPLICATION This application is a continuation of U.S. patent application Ser. No. 15/214,962, filed on Jul. 20, 2016, the entire disclosure of which is incorporated herein by reference. BACKGROUND Traditional luminaires can be turned ON and OFF, and in some cases may be dimmed, usually in response to user activation of a relatively simple input device. Often traditional luminaires are controlled individually or as relatively small groups at separate locations. More sophisticated lighting control systems automate the operation of the luminaires throughout a building or residence based upon preset time schedules, occupancy, and/or daylight sensing. Such lighting control systems receive sensor signals at a central lighting control panel, which responds to the received signals by deciding which, if any, relays, switching devices, and/or dimming ballasts to drive in order to turn on or off and/or adjust the light levels of one or more luminaires. More recent lighting systems are wireless; however, operating luminaires to operate over wireless communication systems using group based controls can be difficult. For example, multiple simultaneous control requests can ovewhelm a node that is tasked with managing the group. Accordingly, a system is needed to overcome these and other limitations in the art. BRIEF DESCRIPTION OF THE DRAWINGS The drawing figures depict one or more implementations in accord with the present teachings, by way of example only, not by way of limitation. In the figures, like reference numerals refer to the same or similar elements. FIG. 1A is a high-level functional block diagram of an example of a system of networks and devices that provide a variety of lighting controls, including communications in support of turning lights on/off, dimming, set scene, and sensor trip events. FIG. 1B is another high-level functional block diagram of an example of a system of networks and devices that further includes plug load controller and power pack devices and various lighting control groups. FIG. 2 is a state change event protocol procedure for the lighting control system of FIGS. 1A-B. FIGS. 3A-C are block diagrams of luminaires that communicate via the lighting control system of FIG. 1A or FIG. 1B. FIGS. 4A-C are block diagrams of different examples of a wall switch that communicates via the lighting control system of FIG. 1A or FIG. 1B. FIG. 5 is a block diagram of a plug load controller that communicates via the lighting control system of FIG. 1B. FIG. 6 is a block diagram of a power pack that communicates via the lighting control system of FIG. 1B. FIG. 7 is a flow chart presenting the states and transitions for the various lighting control devices of FIGS. 1A-B. FIG. 8 is a high-level functional block diagram of a mobile device for commissioning and maintenance of the lighting control system of FIGS. 1A-B. FIG. 9A is a media access control (MAC) layer message for communicating a state change event to a lighting control device on a lighting control network. FIG. 9B is a transport layer message for communicating a state change event to a lighting control device on a lighting control network. FIG. 9C is an application layer message for communicating a state change event to a lighting control device on a lighting control network. DETAILED DESCRIPTION In the following detailed description, numerous specific details are set forth by way of examples in order to provide a thorough understanding of the relevant teachings. However, it should be apparent to those skilled in the art that the present teachings may be practiced without such details. In other instances, well known methods, procedures, components, and/or circuitry have been described at a relatively high-level, without detail, in order to avoid unnecessarily obscuring aspects of the present teachings. Reference now is made in detail to the examples illustrated in the accompanying drawings and discussed below. FIGS. 1A-B are functional block diagrams illustrating examples, each relating to a system of networks and devices that provide a variety of lighting control capabilities, including communications in support of turning lights on/off, dimming, set scene, and sensor trip events. FIG. 1B is the same as FIG. 1A, but further includes additional lighting control devices (LCDs): a plug load controller 30 and a power pack 35; and illustrates exemplary lighting control groups. It should be understood that the term “lighting control device” means a device that includes a controller (sensor/control module or micro-control unit) as shown in FIGS. 3A-C, 4A-C, 5, and 6 that executes a lighting application for communication over a wireless lighting control network communication band, of control and systems operations information during control network operation over the lighting control network communication band. For example, a luminaire (FIGS. 3A-C) that includes a sensor/control module 315 having a micro-control unit 330 that executes lighting application 327 is a lighting control device. A wall switch or touch panel (FIGS. 4A-C) that includes a sensor/control module 415 having a micro-control unit 430 that executes lighting application 427 is a lighting control device. A plug load controller (FIG. 5) that includes a micro-control unit 530 that executes lighting application 527 is a lighting control device. A power pack (FIG. 6) that includes a micro-control unit 630 that executes lighting application 627 is a lighting control device. The lighting control system 1 may be designed for indoor commercial spaces. As shown, system 1 includes a variety of lighting control devices, such as a set of luminaires 10A-N (lighting fixtures) and a set of wall switches 20A-N. Daylight, occupancy, and audio sensors are embedded in lighting control devices, in this case luminaires 10A-N to enable controls for occupancy and dimming. Luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35 communicate control over a 900MHz (sub-GHz) wireless control network 5 and accordingly each include a first radio in the sub-GHz range. A variety of controls are transmitted over wireless control network 5, including, for example, turn lights on/off, dim up/down, set scene (e.g., a predetermined light setting), and sensor trip events. Each luminaire 10A-N, wall switch 20A-N, plug load controller 30, and power pack 35, is also equipped with a second near range Bluetooth Low Energy (BLE) radio that communicate over commissioning network 7 for purposes commissioning and maintenance the wireless lighting control system 1, however no controls pass over this commissioning network 7. Plug load controller 30 plugs into existing AC wall outlets, for example, and allows existing wired lighting devices, such as table lamps or floor lamps that plug into a wall outlet, to operate in the lighting control system 1. The plug load controller 30 instantiates the table lamp or floor lamp by allowing for commissioning and maintenance operations and processes wireless lighting controls in order to the allow the lighting device to operate in the lighting control system 1. Power pack 35 retrofits with existing wired light fixtures (luminaires). The power pack 35 instantiates the wired light fixture by allowing for commissioning and maintenance operations and processes wireless lighting controls in order to allow the lighting device to operate in the lighting control system 1. Both plug load controller 30 and power pack 35 can include the same circuitry, hardware, and software as light fixtures 10A-N and wall switches 20A-N. The system 1 is provisioned with a mobile device 25 that includes a commissioning/maintenance application 22 for commissioning and maintenance functions of the lighting control system 1. For example, mobile device 25 enables mobile commissioning, configuration, and maintenance functions and can be a PDA or smartphone type of device with human interfacing mechanisms sufficient to perform clear and uncluttered user directed operations. Mobile device 25 runs mobile type applications on iOS7, Android KitKat, and windows 10 operating systems and commissioning/maintenance application 22 to support commissioning. Web enabled (cloud) services for facilitating commissioning and maintenance activities is also provided by mobile device 25. The commissioning/maintenance application 22 of mobile commissioning device 25 interfaces with the cloud services to acquire installation and configuration information for upload to luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35. The installation and configuration information is received by mobile device 25 from the gateway 55. The gateway 50 engages in communication through the wide area network (WAN) 55. Lighting control system 1 can leverage existing sensor and fixture control capabilities of Acuity Brands Lighting's commercially available nLight® wired product through firmware reuse. In general, Acuity Brands Lighting's nLight® wired product provides the lighting control applications. However, the illustrated lighting control system 1 includes a communications backbone and includes model - transport, network, media access control (MAC) /physical layer (PHY) functions. The sub-GHz communications of the wireless control network 5 features are built on a near 802.15.4 MAC and PHY implantation with network and transport features architected for special purpose control and air time optimizations to limit chatter. The lighting control system 1 can be deployed in standalone or integrated environments. System 1 can be a an integrated deployment, or a deployment of standalone groups with no gateway 50. One or more groups of lighting control system 1 may operate independently of one another with no backhaul connections to other networks. Lighting control system 1 may comprise a mix and match of various indoor systems, wired lighting systems (nLight® wired), emergency, and outdoor (dark to light) products that are networked together to form a collaborative and unified lighting solution. Additional control devices and lighting fixtures, gateway(s) 50 for backhaul connection, time sync control, data collection and management capabilities, and interoperation with the Acuity Brands Lighting's commercially available SensorView product may also be provided. As shown in FIG. 1B, control, configuration, and maintenance operations of the lighting control system 1 involve networked collaboration between the luminaires 10A-N, wall switches 20A-N, plug load controller(s) 30, and power pack(s) 35 that comprise a lighting control group. An installation is comprised of one or more lighting control groups each operating independently of one another. One or more lighting control groups may exist in the wireless control network 5. Each lighting control group will have a group monitor, and this is shown in FIG. 1B where there a two groups and each group has a monitor. Groups are formed during commissioning of the lighting control system 1 where all members of the group are connected together over wireless control network 5, which in our example is a sub-GHz subnetwork defined by an RF channel and a lighting control group identifier. The lighting control devices subscribe to channels and only listen for/react to messages on the RF channel with the identifier (ID) of the subscribed channel that designates the lighting control group that the lighting control device is a member of For example, the lighting control devices subscribe to a multicast group as identified by the lighting control group identifier and only react to messages on the RF channel of the lighting control group. In general, groups do not share RF channels and thus form their own RF subnetwork, however with only 10 available channels some overlap is inevitable. Analysis and simulation have indicated that group distribution and spatial separation will mitigate the congestion and collision side effects that can occur when many lighting control devices 10A-N, 20A-N, 30, 35 share a singular RF enclave. A group can be further divided to address control to specific control zones within the group defined by a control zone identifier. Zone communications are managed as addressable features at run time. Up to 16 independent zones of control are available for each group and each group can support up to 128 addressable elements (luminaires 10A-N, wall switches 20A-N, plug load controller 30, power pack 35). The wireless control network 5 distributes control messages and events, network management messages and events, health and failover events, and group commissioning and maintenance communications, such as firmware update distributions and group membership changes. Wireless control network 5 provides a secure control network (Sub-GHz) on which to operate. Devices are manually added to the wireless control network 5 via the commissioning process via commissioning/maintenance application 22 of mobile device 25. The commissioning process includes authorization and authentication features that allow only trusted and known entities to add confirmed devices 10A-N, 20A-N, 30, 35 to the network. Requirements relating to network modification (device add/delete/modify) are allocated to the mobile device 25 and its interface (commissioning/maintenance application 22) to the lighting control system 1. Message authentication in the lighting control system 1 is provided by the 802.15.4 compliant MAC layer solution commercially available from Silicon Labs. The solution uses the AES CCM block cypher mode of operation to secure over the air frames. The mode of operation provides NIST compliant authentication, encryption, and integrity assurance to defeat replay attacks as well as device and message spoofing. Lighting control system 1 also implements an additional layer of authentication by performing checks on the message source and addressing mechanisms to reject messages from unknown sources (i.e. sources that are not authorized members of a lighting control group network). An intrusion detection scheme using the above schemes and that reports such events will be made via the gateway 50. The sub-GHz MAC/PHY (wireless control network 5) thus provides secure communication features (authentication, data integrity, and encryption assurance) based on the 802.15.4 standard. The lighting control devices over the wireless control network 5 together may engage in any-to-many (unicast and multicast) communication and can implement a non-mesh wireless network topology. In our example, wireless control network 5 is a star topology network. Although other network schemes may be utilized, a star topology may be the best fit for aligning the required control communications features with the characteristics of sub-GHz wireless radio. At the center of each lighting control group in a star topology wireless control network 5 is a singular group monitor as shown in FIG. 1B. In FIG. 1B, luminaire 10A is the group monitor for lighting control group 1 and luminaire 10B is the group monitor for lighting control group 2. Lighting control group 1 further comprises luminaire 10N, wall switch 20A, and plug load controller 30. Lighting control group 2 further comprises wall switch 20B and power pack 35. The monitor is responsible for receiving control events from their source (luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35) and ensuring reliable and timely delivery of the event to the other members of the group. The monitor uses a quick best effort 0 mechanism for fast high-probability delivery. The monitor follows up the multicast with a reliable point to point communication to ensure that all destination devices received the event. Commissioning Commissioning is the process that sets the lighting control configuration and settings that drive the behavior of the lighting control system 1. One or more mobile devices 25 can be used to commission the installation of lighting control system 1. During setup, commissioning/maintenance application 22 of the mobile device 25 provides a secure method for a system installer to configure the lighting control devices (LCDs) for installation commissioning. The lighting control devices include luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35. General behavioral settings and network addressing information are stored on the mobile device 25 for upload and allocation to the installation's lighting control devices via commissioning/maintenance application 22. The installation information is managed by commissioning/maintenance application 22 of mobile device 25 to ensure correctness and to eliminate common errors such as assignment of duplicate network addresses. Communication between the mobile device 25 for commissioning/maintenance and the lighting control devices is over the commissioning network 7, such as a BLE network. The lighting control devices are initially in an installation state, beaconing their advertisements when the commissioning starts. Upon connection with the mobile device 25, the commissioning/maintenance application 22 of mobile device 25 transitions the lighting control devices to a commissioning state. Further upon connection, the lighting control device authenticates the mobile device 25 and is ready to accept commands over the commissioning network 7. The wall switches 20A-N suppress sleep mode until completion of the commissioning process and transition to operational mode. Wall switches 20A-N will re-enter sleep mode if the commissioning process is interrupted—two elapsed hours with no activity. An installation is commissioned according to lighting control groups. A group is a collection of LCDs sharing the same space within an installation (e.g. a room or area). Each lighting control group in the installation has a special lighting control device called the group monitor. The group monitor keeps tabs on the overall state and health of the lighting control devices within the group and assists in the communication of lighting control events between group elements. In general, one can visualize the group network topology as a star with the group monitor as the central node and the remainder of the group's lighting control devices at points of the star. A group is commissioned by first establishing the group's lighting control network 5 and then configuring the group's control behavior. The lighting control network 5 is established over a 802.15.4 based MAC riding on top of a sub-GHz (904 MHz to 926MHz) PHY. The commissioning network 7, such as a Bluetooth Low Energy MAC/PHY, is used to as the point to point connection medium to transfer control network configuration from the commissioning/maintenance application 22 of the mobile device 25 to a lighting control device The commissioning/maintenance application 22 of mobile device 25 builds a network table of the group devices while establishing the lighting control network 5. The network table, used by the group monitor in the execution of its responsibilities, is uploaded from the mobile device 25 to the group's lighting control devices via commissioning/maintenance application 22. Each lighting control device also has a behavioral configuration. The configuration is specified by a group of settings that define control characteristics such as sensor set points, delays, modes, and ranges. The control characteristics also specify independent zones of control within the group. These characteristics and settings are customized as necessary and uploaded from the mobile device 25 to each lighting control device via commissioning/maintenance application 22. During the commissioning process, line powered lighting control devices are installed, powered, and advertising over BLE. Battery powered lighting control devices, such as wall switches 20A-N, are installed and in sleep mode to conserve power. After the mobile device 25 is setup, an installer opens the commissioning/maintenance application 22 on the mobile device 25 and walks into an area of the installation that is ready to commission as a lighting control group. Configuring a Group Network Wall switches 20A-N and luminaires 10A-N are under the command of the mobile device 25 and respond to a sequence of commands to configure a group network. The wall switches 20A-N respond to a blink request by rapidly blinking an LED. The LED pilot light brightness level is set to a maximum. The luminaires 10A-N responds to a blink request by rapidly blinking an LED light pack. At any time, the lighting control device, including luminaires 10A-N, wall switches 20A-N, plug load controller 30, plug pack 35, etc., ceases blinking upon command. The device then accepts the sub-GHz short MAC address, group number, group name, group RF channel, and personal area network (PAN) ID from the mobile device 25. The device persists this information in non-volatile memory (NVM). The device ceases blinking. The lighting control device accepts the settings from the commissioning/maintenance application 22 of mobile device 25 and persists the settings in non-volatile memory. Additionally, lighting control devices that are luminaires 10A-N also receive settings for an on-board controller (MCU) and on-board integrated sensors. The lighting control device may also receive a request to execute an RF spectrum scan to determine the group RF channel. If so, the lighting control device executes the scan and returns the results to the mobile device 25 for distribution to the other group devices. The above sequence of commands issued from the commissioning/maintenance application 22 of mobile device 25 are expected to be in order. Commands received out of order are consider to be an intrusion attempt. The lighting control device configures its media access control (MAC) layer device circuitry and its physical layer circuitry for the OSI model (PHY) with the data transferred from the mobile device 25 and remains in commissioning state. Connecting a Group Network To connect to the group network, the lighting control devices accept the group address table from the mobile device 25. The group address table identifies all of the lighting control devices in the group. The device persists this information in non-volatile memory. The device uses the lighting control network 5 (e.g., sub-GHz network) to pass the group address table to the other lighting control devices, such as luminaires 10A-N and wall switches 20A-N, in the group. The communication over the lighting control network 5 is reliable-unicast and may involve some message segmenting if the table size exceeds transport protocol data unit (PDU) size. The lighting control device returns a status to the mobile device 25 indicating success or failures encountered while distributing the table. The lighting control device accepts a command to tune the group RF transmission (TX) power levels and executes the tune according to the discussion below. The commissioning/maintenance application 22 of mobile device 25 disconnects after issuing the command to tune the group RF TX power levels. The above sequence of commands issued from the mobile device 25 are expected to be in order. As noted previously, commands received out of order are consider to be an intrusion attempt. Upon completion, the lighting control devices in the group transition to an operational state. Radio Frequency Channel Selection The group RF channel is determined at commissioning time by a line powered lighting fixture, such as luminaires 10A-N. The commissioning/maintenance application 22 of mobile device 25 requests the A spectrum scan of the available channels (10) seeking the channel with the lowest average noise level measured over a short period of time. The process is as follows. Mobile device 25 is connected to a luminaire 10A-N via the commission network 7 (e.g., BLE). The mobile device 25 requests a spectrum scan indicating the number of samples/per channel to be produced. The luminaire 10A-N executes a passive scan of the following channels (channel number, center frequency): 1 904 MHz 2 906 MHz 3 908 MHz 4 910 MHz 5 912 MHz 6 914 MHz 7 916 MHz 8 918 MHz 9 920 MHz 10 922 MHz 11 924 MHz 12 926 MHz The luminaire 10A-N returns the average energy and peak energy detected for each channel. The commissioning/maintenance application 22 of mobile device 25 determines the optimum RF channel from the average and peak energy samples giving preference (via a weighting factor) to channels 5-8. The commissioning/maintenance application 22 of mobile device 25 commands the lighting control device to configure its MAC/PHY to use the optimum RF channel. A modified method that replaces the above method with one that uses a discovery and link quality measurement to join the optimum gateway subnetwork may also be used. Whatever the method (gateway 50 or non-gateway), the RF channel selection scheme is timely to meet the user experience requirements for commissioning. Alternatively, this procedure may be decoupled from mobile device 25 so that channel selection can also execute independently by lighting control devices, such as luminaires 10A-N and wall switches 20A-N. Transmission Power Adjustment Sub-GHz RF TX power levels are managed to optimize intra-group communications in a way that limits adverse effects (collisions, retries, corrupt packets, etc.) on adjacent group subnetworks that happen to be sharing the RF channel. The group monitor executes a link test with each lighting control device in the group as follows. The group monitor sends a link test message to the lighting control device. The device returns a link test response to the group monitor indicating the received strength signal indicator (RSSI-1) of the received message in 1. The group monitor receives the response and notes the RSSI of the received message (RSSI-2). If RSSI-1 is less than the minimum RSSI-1s recorded so far, it records the new minimum RSSI. The group monitor returns a link test response acknowledgment to the device indicating RSSI-2. The device receives the acknowledgement. The device adjusts it RF TX power appropriately if the RSSI-2 does not fall within the desired range. The device returns a link test status (continue) to the group monitor. The device returns a link test status (complete) if the RSSI-2 is within the desired range. The group monitor receives the link test status. The process repeats if the status indicates continue (is within the desired range). Steps 1 through 6 are repeated until all devices in the group have been tested. The transmission (TX) power adjustment can also be invoked for a single group monitor—device link. In this case, all devices in the group do not need to be tested. Lighting Control Device Health The group monitor periodically checks the health of each lighting control device, such as luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35, in the group. The group monitor runs a round robin check of each group device such that every device receives a request to report health once every hour. In an example, given a group with a maximum number of devices (128), the group monitor will issue a request for health status every ˜28.125 seconds while a group of six will result in a health request every 10 minutes. Clock drift and frequency of over the air messaging are not expected to cause undesirable side effects or performance hits to the network 5, however health requests are delayed via a back off timer of 10 seconds during bursts of network traffic to allow potential congestions to clear and make way for higher priority control operations. The group monitor records faults reported by lighting control devices for later retrieval by commissioning/maintenance application 22 of mobile device 25 for commissioning and maintenance. Communication Failures Wireless messaging failures are possible and expected, however continuous failures indicate a problem that might be rectified by adjusting the RF properties of the communications link of lighting control devices, such as luminaires 10A-N and wall switches 20A-N. Continuous failures may result if there is a change to the environment that alters RF performance or in cases where a lighting control device is experiencing internal failures. Attempts to resolve communications failures are managed by the group monitor rather than separately at each lighting control device. Reliable-unicast messaging acknowledgement is the driver for detecting communications failures. At lighting control devices, a communication failure occurs when the device transmits a reliable-unicast message and fails to receive an acknowledgement within a retry period. Upon detecting such a failure, the lighting control device increments its counters of total failures and attempts. The lighting control device reports the percentage of failures in response to a request for health status from the group monitor. The lighting control device resets its counters after successful report of health status. At a group monitor, the group monitor associates a four bit counter with each lighting control device in the group for purposes of tracking communication failures. A failure occurs when the group monitor receives no acknowledgement back after transmitting a reliable-unicast message to a group device. The group monitor will increment the counter for that lighting control device whenever a failure occurs. The counter is reset whenever a successful transmission occurs. If the counter reaches a value of 0×7 for any lighting control device, the group monitor attempts to correct the consistent communication failure by issuing a command to the lighting control device to incrementally increase its RF TX power level. If the counter reaches a value of 0×E for any lighting control device, the group monitor initiates an RF TX Power adjustment for the link. Counters that reach a max of 0×F remain there and may indicate a dead lighting control device. Power level adjustment trigger may be changed to act on percentage of failures (similar to the device health method below) rather than consecutive failure conditions. The group monitor 10A issues a command to the lighting control device to incrementally increase its RF TX power level if the device's status indicates transmission failures at or greater than 15%. The group monitor initiates an RF TX Power adjustment for any communications link where the lighting control device's status indicates transmission failures at or greater than 25%. FIG. 2 is a state change event protocol procedure for the lighting control system of FIGS. 1A-B. As noted above, a group is a collection of lighting control devices that are managed by a “monitor.” A zone is an operational collection of lighting control devices within the group and may comprise the entire group. The group/zone monitor (luminaire 10A in the example) has knowledge of the group/zone configuration (e.g., handled at the network layer level) to execute a reliable delivery check on sensor/switch state changes. Group membership and management functions may be performed by the application layer or the network layer. Luminaire 10A stores a lighting control group network table that maintains a group/zone list of the group/zone that each lighting control device is a member of. The lighting control group network table may be shared with other luminaires and/or sensors, plug load controllers or switches in the group, e.g. to enable failover to another group member upon failure of the group/zone monitor functionality at the luminaire 10A. Lighting control devices (luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35) go through a series of states, transitions, and engage in communications with each other upon detecting a state change event of the lighting control system. Although luminaires 10A and 10N are shown in this example, it should be understood that the state change event protocol shown applies to all of the other lighting control devices, such as a wall switches 20A-N, plug load controller 30, power pack 35, or other types of switches/sensors. Assumptions of the state change event protocol procedure in this example may be the following. Sensor/switches of lighting control devices (luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35) behave in a similar manner when communicating events at least over the lighting control network 5 (e.g., group and zone network level) and possibly beyond. Battery powered sensors and line powered switches/sensors behave in a similar manner when communicating events at least over the lighting control network 5 and possibly beyond. Lighting control devices, including sensors/switches, attempt to communicate state change of interest directly to gateway 50. A group monitor may communicate group/zone state change to the group/zone devices and the gateway 50 in addition to the sensors/switches. Battery life conservation may drive the design of the communication pattern, e.g. for communications for a battery powered wall switch, sensor or the like. There may be a 1 second maximum time for event detection to lights on/off. State change events involve a state change of an occupancy, audio, or daylight sensor (e.g., a new reading different from a previous reading), or a switch to turn lighting on/off, dim up/down, or set scene. For example, state change includes on/off for switches, occupied/unoccupied for occupancy sensors, and lighting intensity adjustments for dimmers. Groups may be subdivided into zones. Switches and sensors control a group or zones within the group. A zone may comprise an entire group (e.g., all on/off). In the example, luminaire 10N is a member lighting control device of group/zone 1 and zone 1 includes all members of group 1. Beginning in block S200, programming in a memory of the luminaire 10N, specifically lighting application 327, configures a processor of the luminaire 10N to detect a state change event and transmit a state change event message via the lighting control network communication band to a monitor lighting control device of group/zone 1 (luminaire 10A). For example, drive/sense circuitry 335 of luminaire 10N detects a state change event via detector(s) 365. Alternatively, if the lighting control device is a wall switch 20, then drive/sense circuitry 435 detects a state change event via switches 465. Situations may arise that require protection in order to maintain integrity of the lighting control system 1. For example, a rapid fire communication of multiple switch events could overwhelm the ability of the group/zone 1 monitor (luminaire 10A) to issue a state change multicast message and perform a state change check with each lighting control device in the group. Having sensor/switch de-bounce capability addresses this potential problem. The de-bounce mechanism limits the rate at which state change event messages can be initiated by a sensor/switch. Luminaire 10N checks the hardware state of detector(s) 365 and, if a state change is detected, luminaire 10N performs the following two steps. First, the luminaire 10N unicasts a state change event message to the group 1 monitor (luminaire 10A) using a reliable effort. Reliable effort means that if an acknowledgement is not received from the recipient, then a retry effort is made to resend the message to the recipient. Second, the luminaire 10N also unicasts a state change event message to the gateway 50 using a best effort (not shown). Best effort means that if an acknowledgement is not received from the recipient, then no retry effort is made to resend the message to the recipient. Luminaire 10N then delays for a regular polling period (e.g., 1 second) before re-checking the hardware state of sensors/switches again. Of note, if the group/zone 1 member lighting control device is a wall switch instead of a luminaire, then a switch change similarly results in a state change event message. However, if the member lighting control device that sent the original state change message is battery operated (e.g., a wall switch), then the regular polling period may be extended to a longer period of time (e.g., 10 seconds) or there may not be any polling at all to conserve battery life. Lighting application 327 builds application control messages, such as the state change event message. The state change event message is sent to the transport layer by the lighting application 327 for unicast transmission to luminaire 10A. Moving to block S205, luminaire 10A (monitor of group/zone 1) receives the state change event message and acknowledges receipt of the state change event message. Luminaire 10A examines the application message body, determines that the protocol relates to lighting control operation, and extracts the payload. To handle multiple concurrent group/zone state change requests, luminaire 10A determines if the received message involves a group/zone state change while a state change is in progress for the exact same group/zone. If the received message is for the same group/zone, then luminaire 10A cancels the in-progress activity and executes the new state change. Continuing in block S210, luminaire 10N determines whether an acknowledgement of the state change event message has been received from luminaire 10A acting as the group/zone monitor. If the acknowledgment message has been received, then block S215 is entered. In block S215, luminaire 10A as the group/zone monitor multicasts a state change event message to all of the lighting control group/zone devices in a respective lighting control group/zone. In the example, if the payload indicates an inter-zone group, then the luminaire 10A performs a look up in a zone table to see if any local lighting control devices are members of that group. If the local lighting control devices are members of the inter-zone group or if the payload indicates an intra-zone group, then luminaire 10A (zone monitor) broadcasts the message (e.g., 3 times), with the zone set to the zone identifier and the protocol set to lighting control operation. The multicast message may be addressed to a group/zone broadcast group address or channel. Luminaire 10A may push up the transmission (TX) power for the multicast. Proceeding now to block S220, luminaire 10A begins a unicast check with each local lighting control device participating in the group to confirm receipt of the multicast message. Luminaire 10A unicasts (reliable effort) a check to each lighting control device in the group/zone to confirm state change. The luminaire 10A may unicast in order beginning with the lighting control device with the lowest received strength signal indicator (RSSI) and then proceed in ascending order. Alternatively, luminaire 10A may unicast in order beginning with the lighting control device with the highest round-trip time (RTT) and then proceed in descending order. Moving now to block S225, the zone lighting control devices receive the broadcast message and determine whether the device itself is in the targeted lighting control group/zone. If the lighting control device is not in the targeted lighting control group/zone, then the message is discarded. The message, minus transport header, is passed to the lighting application 327. The lighting application 327 uses the payload of the message and its internal settings to determine whether or not the message is to be processed. If the message is processed, then the LED light source of the lighting control device is adjusted (e.g., turned on/off) in accordance with the state change event. Each lighting control device in the group/zone with exception of the original member lighting control device 10N that sent the original state change message, returns an acknowledgment message (MAC layer) and an application layer message (reliable effort) indicating the success or failure to execute the state change event from the state change event message, thereby enabling tracking. Further, each acknowledgement includes an indication whether the initial multicast message from block S215 was received by the respective lighting control device. The acknowledgment message is received by luminaire 10A. In an example, if a switch controls 15 light fixtures then the group monitor of the respective lighting control group would receive 15 acknowledgment messages back after communicating the state change, thereby tracking the output of the light fixtures. Continuing to block S230, luminaire 10A also sends the state change event message to gateway computer 50, for example, via unicast and using a reliable effort. However, if the member lighting control device that sent the original state change message is battery operated (e.g., a wall switch), then the monitor lighting control device sends the state change event message to gateway computer 50, for example, via unicast and using a reliable effort to conserve battery power. Moving back to step S210, if luminaire 10N determines that no acknowledgement of the state change event message has been received from luminaire 10A (group monitor), then block S235 is entered. This indicates that the group monitor received the state change event message in block S205, but the sensor/switch (luminaire 10N) did not hear an acknowledgement message back from the group monitor. Alternatively, this means that the group monitor never actually received the state change event message. In either case, luminaire 10N powers a wireless radio communication interface up to full power and multicasts a state change event message to group/zone lighting control devices listening on a respective broadcast channel or address. Next, in block S240, luminaire 10N initiates a re-survey of its RF connectivity with luminaire 10A. The group monitor tracks RF net degradation over time using aggregated stats and then initiates the RF re-scan. As shown in block S245, if a response from luminaire 10A is received, then block S250 is entered, which indicates luminaire 10A is now operating correctly. Accordingly, in block S250 the protocol branches to block S215 so that luminaire 10A proceeds to execute the steps shown as S215-S230. Any time luminaire 10A hears the multicast message of block S235 without hearing the unicast message of block S200, the group/zone monitor branches to block S220 and unicasts a check to each group/zone device to confirm state change (as shown in block S220). Blocks S225 and S230 will subsequently be entered as well. However, if a response is not received luminaire 10A in block S245, then luminaire 10N assumes that luminaire 10A has failed operating. Accordingly, in block S255, the luminaire 10N unicasts a fault message to the backup group/zone monitor, for example, the backup group/zone monitor is the second entry listed in the lighting control group network table, A table of different state change event message communication types and transmission protocols is shown below. Various message exchanges that occur upon control actions (e.g., wall switch activated), including the number and nature (source, destination, type—unicast/broadcast/multicast) is shown. Pattern Source Destination Transport Scheme Use One to one Sensor/Switch Zone monitor Redbox unicast/MAC Occupancy, reliable (all) unicast with ack/retry photo sensor state change One to one best Sensor/Switch Gateway Redbox unicast/MAC On selected effort (all) unicast state change One to many Zone monitor Selected zone Redbox unicast/MAC Occupancy, best effort devices broadcast, addressed to photo sensor zone/broadcast channel state change One to one Zone monitor Selected zone Redbox unicast/MAC Zone monitor reliable devices unicast with ack/retry checks devices to confirm state change One to one Selected zone Zone monitor Redbox unicast/MAC Application reliable devices unicast with ack/retry layer confirmation of state change One to one Zone monitor Gateway Redbox unicast/MAC On selected reliable unicast state change One to many Sensor/Switch Selected zone Redbox unicast/MAC On failure to best effort (all) devices broadcast, addressed to hear ack zone/broadcast channel from zone monitor on occupancy, photo sensor state change One to one Sensor/Switch Zone monitor Redbox unicast/MAC Request RF reliable (all) unicast survey One to one Zone monitor Sensor/Switch Redbox unicast/MAC Response to reliable (all) unicast RF survey request One to many Sensor/Switch All zone Redbox unicast/MAC Zone monitor best effort (sleepy) devices broadcast, addressed to discover zone message One to one Zone monitor Sensor/Switch With ack/retry Reply to reliable (sleepy) zone monitor discover FIGS. 3A-C are block diagrams of a luminaire 10 that communicate via the lighting control system of FIGS. 1A-B. Luminaire 10 is an integrated light fixture that generally includes a power supply 305 driven by a power source 300. Power supply 305 receives power from the power source 300, such as an AC mains, battery, solar panel, or any other AC or DC source. Power supply 305 may include a magnetic transformer, electronic transformer, switching converter, rectifier, or any other similar type of circuit to convert an input power signal into a power signal suitable for luminaire 10. Luminaire 10 furthers include an intelligent LED driver circuit 310, sensor/control module 315, and a light emitting diode (LED) light source 320. Intelligent LED driver circuit 310 is coupled to LED light source 320 and drives that LED light source 320 by regulating the power to LED light source 320 by providing a constant quantity or power to LED light source 320 as its electrical properties change with temperature, for example. The intelligent LED driver circuit 310 includes a driver circuit that provides power to LED light source 320 and a pilot LED 317. The pilot LED 317 may be included as part of the sensor/control module 315. Intelligent LED driver circuit 310 may be a constant-voltage driver, constant-current driver, or AC LED driver type circuit that provides dimming through a pulse width modulation circuit and may have many channels for separate control of different LEDs or LED arrays. An example of a commercially available intelligent LED driver circuit 310 is manufactured by EldoLED. LED driver circuit 310 can further include an AC or DC current source or voltage source, a regulator, an amplifier (such as a linear amplifier or switching amplifier), a buck, boost, or buck/boost converter, or any other similar type of circuit or component. LED driver circuit 310 outputs a variable voltage or current to the LED light source 320 that may include a DC offset, such that its average value is nonzero, and/or a AC voltage. The pilot LED 317 indicates the state of the luminaire 10, for example, during the commissioning and maintenance process. For purposes of communication and control, luminaire 10 is treated as single addressable device that can be configured to operate as a member of one or more lighting control groups or zones. The luminaire 10 is line powered and remains operational as long as power is available. Sensor/control module 315 includes power distribution circuitry 325, a micro-control unit (MCU) 330, drive/sense circuitry 335, and detector(s) 365. As shown, MCU 330 is coupled to LED driver circuit 310 and controls the light source operation of the LED light source 320. MCU 330 includes a memory 322 (volatile and non-volatile) and a central processing unit (CPU) 323. The memory 322 includes a lighting application 327 (which can be firmware) for both lighting control operations and commissioning, maintenance, and diagnostic operations. The power distribution circuitry 325 distributes power and ground voltages to the MCU 330, drive/sense circuitry 335, wireless transceivers 345 and 350, and detector(s) 365 to provide reliable operation of the various circuitry on the sensor/control module 315 chip. Luminaire 10 also includes a dual-band wireless radio communication interface system configured for two way wireless communication. It should be understood that “dual-band” means communications over two separate RF bands. The communication over the two separate RF bands can occur simultaneously (concurrently); however, it should be understood that the communication over the two separate RF bands may not actually occur simultaneously. In our example, luminaire 10 has a radio set that includes radio 345 for sub-GHz communications and another radio 350 for Bluetooth RF communications. A first transceiver 345, such as a 900 MHz wireless transceiver, issues control operations on the lighting control network. This first transceiver 345 is for any-to-many (unicast and multicast) communication, over a first of the two different wireless communication bands, of control and systems operations information, during luminaire operation and during control network operation over the first wireless communication band. Two transport methods ride on the network layer function of the first transceiver 345: unicast and multicast. The first transceiver 345 engages in multicast group communication of a one-to-many or a many-to-many distribution where group communication is addressed to a group simultaneously. A second transceiver 350, such as a 2.4 GHz BLE (Bluetooth) wireless transceiver carries out commissioning, maintenance, and diagnostics of the lighting control network. This second transceiver 350 is for point-to-point communication, over a second of the two different wireless communication bands, of information other than the control and systems operations information, concurrently with at least some communications over the first wireless communication band. As shown, the MCU 330 includes programming in the memory 322 which configures the CPU (processor) 323 to control operations of the respective luminaire 10, including the communications over the two different wireless communication bands via the dual-band wireless radio communication interface system 345, 350. The programming in the memory 322 includes a real-time operating system (RTOS) and further includes a lighting application 327 which is firmware/software that engages in communications with the commissioning/maintenance application 22 of mobile device 25 over the commissioning network 7 of FIGS. 1A-B. The lighting application 327 programming in the memory 322 carries out lighting control operations over the lighting control network 5 of FIGS. 1A-B. The RTOS supports multiple concurrent processing threads for different simultaneous control or communication operations of the luminaire 10. Three different CPU and memory architectures are shown for the sensor/control module 315 and the MCU 330 of the luminaire 10 in FIGS. 3A-C. In FIG. 3A, in addition to the memory 322 and the CPU 323 of the MCU 330 itself, the first transceiver 345 and the second transceiver 350 each include a separate memory (not shown) and a processor (not shown). Hence, in the example of FIG. 3A, the sensor/control module 15 includes a total of three processors and three sets of memory. In FIG. 3B, the MCU 330 itself does not include a separate memory 322 and a CPU 323. Instead, only the first transceiver 345 and the second transceiver 350 each include a separate memory 322 and a processor 323. For efficiency purposes, such as to save manufacturing costs and conserve power (e.g., line power or battery power), the memory 322 and CPU 323 of the first transceiver 345 is selected to perform processing because the majority of processing (normal lighting control operations) occur over the sub-GHz wireless control network 5. Hence, in the example of FIG. 3B, the sensor/control module 315 includes a total of two processors and two sets of memory. In FIG. 3C, the MCU 330 comprises a dual band system on chip (SOC) 345, 350 and the MCU 330 itself does not include a separate memory 322 and a CPU 323. Instead, the first transceiver 345 and the second transceiver 350 are integrated and combined into the chipset of the MCU 330. Hence, in the example of FIG. 3C, the sensor/control module 315 includes a total of one processor and one set of memory. Integrating the first transceiver 345 and second transceiver 350 into a dual band SOC chipset of the MCU 330, saves manufacturing costs and conserves power (e.g., line power or battery power). As shown, luminaire 10 includes detector(s) 365, such as an in-fixture daylight sensor, an occupancy sensor, an audio sensor, a temperature sensor, or other environmental sensor. Detector(s) 365 may be based on Acuity Brands Lighting's commercially available xPoint® Wireless ES7 product. Drive/sense circuitry 335, such as application firmware, drives the in-fixture occupancy, audio, and photo sensor hardware. Outlined below are lighting controls and communications in the lighting control network that occur when drive/sense circuitry 335 of luminaire 10 detects state changes in the detector(s) 365, such as occupancy, daylight, and audio sensors. Sensor State Change When an occupancy sensor, daylight sensor, or audio sensor state change occurs is detected by drive/sense circuitry 335, MCU 330 of the luminaire 10 generates a network packet(s) and a wireless message is created with a state change event as at least part of the payload. The message is sent to the group monitor via the transceiver radio 345 as reliable unicast (unless luminaire 10 is hosting the group monitor) by the lighting application 327 running on MCU. If a gateway 50 (shown in FIGS. 1A-B) is present, a wireless gateway notification is created indicating the sensor, the sensor state (occupied or unoccupied, inhibiting or not inhibiting), the group, and the zone. The message is then unicast to the gateway 50 by the lighting application 327 running on MCU 330. If the luminaire 10 misses acknowledgement of the wireless message indicating the sensor state change that luminaire 10 unicasted to group monitor within a predetermined time period, for example, then the luminaire 10 generates and issues/transmits a group multicast message indicating the sensor state change. No check message follow up is issued from the luminaire 10 following this multicast message, but such communication faults and anomalies are tallied by the luminaire 10 for health status reporting as described with reference to FIGS. 1A-B. Group Monitor The group monitor acknowledges receipt of the unicast message (MAC layer) from the luminaire 10 indicating the sensor state change. The group monitor extracts the payload of the network packet(s) from the unicast message and creates a multicast message in response using the extracted payload of the unicast message. The group monitor interrogates the extracted payload of the unicast message to determine the type of control and the zone. The payload of the multicast message indicates or specifies a lighting control event (e.g., turn on/off or dim a light source) and specifies a lighting control group, for example, using a lighting control group identifier. The created multicast message and extracted payload of the unicast message are temporarily saved. The group monitor transmits the multicast message at least two or three times, for example. The group monitor also sends the extracted payload to the applications that share the processor with the group monitor. If a gateway 50 (see FIG. 1A) is present and the type of control is occupancy, daylight, or audio sensor related or the zone to make the adjustment to is global, a gateway notification is created indicating the sensor, its state (occupied or unoccupied, inhibiting or not inhibiting), the group, and the zone. The message is then reliably unicast to the gateway 50. After interrogating the extracted payload to determine the type of control and zone, the group monitor uses the group table to look up the set of lighting control devices that are members of the zone. The group monitor forms a check message using at least part of the extracted payload of the unicast message as the payload. The group monitor sends the message reliable unicast to each device in the zone as a check to confirm the receipt of the multicast in order as specified in the lighting control group network table. This confirmation check is not made with the luminaire 10 that has the sensor that actually initiated the state change event. The group monitor service accommodates concurrent multiple occupancy, daylighting, or audio events irrespective of zone. The group monitor service cancels a confirmation check if it receives a state that obsolesces an active state in progress. In this case, the group monitor service starts a new confirmation check based on the latest state. If the group monitor misses the unicast message from the luminaire 10 but gets the multicast issued by the luminaire 10—the group monitor executes the gateway and zone check described above. Recipient Lighting Control Devices Upon receipt of a multicast message from the group monitor at a recipient lighting control device (e.g., luminaire, wall switch, plug load controller, or power pack) that was sent in response to the original message from luminaire 10, the recipient device checks the group indication and the counter. The message is discarded if the lighting control device is not a member of the identified lighting control group specified in the message. The message is also discarded if it is a duplicate (multicast switch state change events are transmitted at least two or three times, for example, by the group monitor). The payload is extracted from the multicast message and processed by the lighting application 327 running on the MCU 330. Upon receipt of the confirmation check, the message is acknowledged (MAC). The recipient lighting control device determines if it has already acted on the event. If not, then the payload is extracted from the unicast message and processed by the lighting application 327 running on the MCU 330. Applications are responsible for either processing the extracted payload or discarding it as out of zone scope. For example, upon receipt of the multicast message from the lighting control group monitor at a respective recipient lighting control device, the respective recipient lighting control device checks a lighting control group identifier to determine whether the respective recipient control device is a member of the identified lighting control group in the message. The recipient lighting control device then determines whether the recipient lighting control device has already acted on a lighting control event (e.g., turn on/off or dim a light source) for lighting control network operation that is similar or identical to the event in the multicast message. If the recipient lighting control device has not already acted in accordance with the control event for lighting control operation, the recipient lighting control device adjusts one of its own LED light source(s) in accordance with the control event. Alternatively, if the recipient lighting control device has already acted on the lighting control event specified in the multicast message, no further action is taken in response by discarding the multicast message. In an example, the scope of daylight light sensor control is that of the hosting luminaire 10 itself. Therefore events of this type may only be processed locally and not distributed over the lighting control network 5. FIGS. 4A-C are block diagrams of a wall switch 20 that communicate via the lighting control system of FIGS. 1A-B. The circuitry, hardware, and software of wall switch 20 shown is similar to the luminaire 10 of FIG. 3. However, wall switch 20 is a controller that can be a battery powered device. Wall switch 20 is similar to luminaire 10 in that they are singularly addressable devices that can be configured to operate as a member of one or more lighting control groups or zones. As shown, wall switch 20 includes a power supply 405, such as a battery or line power, to power itself. Wall switch 10 furthers include an LED driver circuit 410, and a light emitting diode(s) (LED) 420. LED driver circuit 410 is coupled to LED(s) 420 and drives that LED(s) 420 by regulating the power to LED(s) 420 by providing a constant quantity or power to LED light source 420 as its electrical properties change with temperature, for example. The LED driver circuit 410 includes a driver circuit that provides power to LED(s) 420 and a pilot LED 417. LED driver circuit 410 may be a constant-voltage driver, constant-current driver, or AC LED driver type circuit that provides dimming through a pulse width modulation circuit and may have many channels for separate control of different LEDs or LED arrays. An example of a commercially available intelligent LED driver circuit 410 is manufactured by EldoLED. LED driver circuit 410 can further include an AC or DC current source or voltage source, a regulator, an amplifier (such as a linear amplifier or switching amplifier), a buck, boost, or buck/boost converter, or any other similar type of circuit or component. LED driver circuit 410 outputs a variable voltage or current to the LED light source 420 that may include a DC offset, such that its average value is nonzero, and/or a AC voltage. The pilot LED 417 indicates the state of the wall switch 20, for example, during the commissioning and maintenance process. As shown, an MCU 430 is coupled to LED driver circuit 410 and controls the light source operation of the LED(s) 420. MCU 430 includes a memory 422 (volatile and non-volatile) and a central processing unit (CPU) 423. The memory 422 includes a lighting application 427 (which can be firmware) for both lighting control operations and commissioning/maintenance operations. The power distribution circuitry 425 distributes power and ground voltages to the LED driver circuit 410, MCU 430, drive/sense circuitry 435, wireless transceivers 445 and 450, and switches 465 to provide reliable operation of the various circuitry on the wall switch 20. Wall switch 20 also includes a dual-band wireless radio communication interface system configured for two way wireless communication. In our example, wall switch 12 has a radio set that includes radio 445 for sub-GHz communications an another radio 450 for Bluetooth RF communication. A first transceiver 445, such as a 900 MHz wireless transceiver, issues control operations on the lighting control network. This first transceiver 445 is for any-to-many (unicast and multicast) communication, over a first of the two different wireless communication bands, of control and systems operations information, during luminaire operation and during control network operation over the first wireless communication band. A second transceiver 450, such as a 2.4 GHz BLE (Bluetooth) wireless transceiver carries out commissioning and maintenance of the lighting control network. This second transceiver 450 is for point-to-point communication, over a second of the two different wireless communication bands, of information other than the control and systems operations information, concurrently with at least some communications over the first wireless communication band. As shown, the MCU 430 includes programming in the memory 422 which configures the CPU (processor) 423 to control operations of the respective wall switch 20, including the communications over the two different wireless communication bands via the dual-band wireless radio communication interface system 445, 450. The programming in the memory 422 includes a real-time operating system (RTOS) and further includes a lighting application 427 which is firmware/software that engages in communications with the commissioning/maintenance application 22 of mobile device 25 over the commissioning network 7 of FIGS. 1A-B. The lighting application 427 programming in the memory 422 carries out lighting control operations over the lighting control network 5 of FIGS. 1A-B. The RTOS supports multiple concurrent processing threads for different simultaneous control or communication operations of the wall switch 20. Three different CPU and memory architectures are shown for the MCU 430 of the wall switch 20 in FIGS. 4A-C. In FIG. 4A, in addition to the memory 422 and the CPU 423 of the MCU 430 itself, the first transceiver 445 and the second transceiver 450 each include a separate memory (not shown) and a processor (not shown). Hence, in the example of FIG. 4A, the MCU 430, first transceiver 445, and second transceiver 450 combine to include a total of three processors and three sets of memory. In FIG. 4B, the MCU 430 itself does not include a separate memory 422 and a CPU 423. Instead, only the first transceiver 445 and the second transceiver 450 each include a separate memory 422 and a processor 423. For efficiency purposes, such as to save manufacturing costs and conserve power (e.g., line power or battery power), the memory 422 and CPU 423 of the first transceiver 445 is selected to perform processing because the majority of processing (normal lighting control operations) occur over the sub-GHz wireless control network 5. Hence, in the example of FIG. 4B, the sensor/control module 415 includes a total of two processors and two sets of memory. In FIG. 4C, the MCU 430 comprises a dual band system on chip (SOC) 445, 450 and the MCU 430 itself does not include a separate memory 422 and a CPU 423. Instead, the first transceiver 445 and the second transceiver 450 are integrated and combined into the chipset of the MCU 430. Hence, in the example of FIG. 4C, the MCU 430 includes a total of one processor and one set of memory. Integrating the first transceiver 445 and second transceiver 450 into a dual band SOC chipset of the MCU 330, saves manufacturing costs and conserves power (e.g., line power or battery power). As shown, wall switch 20 includes switches 465, such as a dimmer switch, set scene switch. Switches 465 can be or include sensors, such as infrared sensors for occupancy or motion detection, an in-fixture daylight sensor, an audio sensor, a temperature sensor, or other environmental sensor. Switches 465 may be based on Acuity Brands Lighting's commercially available xPoint® Wireless ES7 product. Drive/sense circuitry 435, such as application firmware, drives the occupancy, audio, and photo sensor hardware. In our example, wall switch 20 includes a single shared button switch 465 for on/off functions that requires knowledge of state to differentiate between on and off. The wireless control network 5 communicates output device (luminaire 10, plug load controller 30, power pack 35) state to the wall switches 20 as a means of providing the differentiating state. However, the wireless control network 5 suppresses the communication of output devices to constrain network traffic. Therefore control network 5 will rely on the default mechanism (tracked on the device) for determining on/off on all of the types of wall switch. It is therefore possible for the wall switch 20 to occasionally be out of sync with the actual state of the zone particularly at installation commissioning time. Toggling the switch button 465 one or more times will clear any mismatched state. In our example, wireless control network 5 does not communicate load state via the pilot LED 417 of wall switch 20) 20; however, in other examples wireless control network 5 communicates load state via the pilot LED 417 of wall switch 20. Outlined below are lighting controls and communications in the lighting control network that occur when drive/sense circuitry 435 detects state changes in the switches 365 of wall switch 20. Wall Switch Button Pushed When the on switch 465 is pushed, the lighting application 427 running on MCU 430 generates a network packet(s) having a payload indicating the control event. A wireless message is created with the network packet(s) having the payload indicating the control event. The message is sent to the group monitor as reliable unicast. If a gateway 50 (see FIG. 1A) is present and if the message is a switch on/off control, then a gateway notification is created indicating the wall switch 20, the state of the wall switch 20, the group, and the zone. The message is unicasted to the gateway 50. If the wall switch 20 is a battery powered (sleepy) type wall switch which uses a sleep feature as a means of power conservation and thus requires a special mechanism to acquire certain communications upon wake up, the following extension is used. The wall switch 20 detects the button push and turns on the transceiver radio 445 and transmits the wireless message with the network packet(s) having the payload indicating the control event. Next, the wall switch 20 cancels its wake up timer. The timer wakes the device to check its mailbox in the case where no button push has occurred for a while. The wall switch 20 sends a request for communications to the mail box server on the group monitor. The group monitor returns the contents of the mailbox addressed to the wall switch. The wall switch 20 processes each request. Examples include a request for health status or a state change request. The wall switch sets it wake up timer and the timer period is directly related to the frequency of system health reporting. The lighting application 427 de-bounces a continual or rapid button depress sequence so as to not create a message storm at the group monitor. If the wall switch 20 doesn't receive the acknowledgment from the group monitor when the message having the payload indicating the control event is unicasted to the group monitor, then the switch will generate and issue the group multicast. In this instance, no check message follow up is issued from the wall switch 20. Communication faults and anomalies are tallied by the switch for health status reporting as described previously with reference to luminaire 10. Group Monitor The group monitor acknowledges (MAC layer) receipt of the unicast message from the wall switch 20 indicating pushing of the on switch 465. The group monitor extracts the payload of the network packet(s) from the unicast message and creates a multicast message in response using the extracted payload of the unicast message. The group monitor interrogates the extracted payload of the unicast message to determine the type of control and the zone. The payload of the multicast message indicates or specifies a lighting control event (e.g., turn on/off or dim a light source) and specifies a lighting control group, for example, using a lighting control group identifier. The created multicast message and extracted payload of the unicast message are temporarily saved. The group monitor transmits the multicast message at least two or three times, for example. The group monitor also sends the extracted payload to the applications that share the processor with the group monitor. If a gateway 50 (see FIG. 1A) is present and the type of control is a switch on/off or the zone to make the adjustment to is global, then a gateway notification is created indicating the state of the switch, the group, and the zone. The message is reliably unicast to the gateway 50. The group monitor uses the group table to look up the set of devices that are members of the zone. The group monitor forms a check message using at least part of the saved extracted payload of the unicast message as the payload. The group monitor sends the message (reliable unicast) to each lighting control device in the zone as a check to confirm the receipt of the multicast. Of note, the confirmation check is not made with the wall switch 20 that actually initiated the control event. The group monitor service accommodates concurrent multiple switch on/off events irrespective of zone. The group monitor service cancels a confirmation check if it receives a state that obsolesces an active state in progress. In this case the group monitor service starts a new confirmation check based on the latest state. If the group monitor misses the unicast message from the switch but gets the multicast issued by the switch - the group monitor executes the gateway and zone check described above. Recipient Lighting Control Devices Upon receipt of a multicast message from the group monitor at a recipient lighting control device (e.g., luminaire, wall switch, plug load controller, or power pack) that was sent in response to the original message from wall switch 20, the recipient device checks the group indication and the counter. The message is discarded if the recipient device is not a member of the identified lighting control group specified in the message. The message is also discarded if it is a duplicate (multicast switch state change events are transmitted at least two or three times, for example, by the group monitor). The payload is extracted from the multicast message and processed by the lighting application 427 running on the MCU 430. Upon receipt of the confirmation check, the message is acknowledged (MAC). The recipient lighting control device determines if it has already acted on the event. If not then the payload is extracted from the unicast message and processed by the lighting application 427. The applications are responsible for either processing the extracted payload or discarding it as out of zone scope. For example, upon receipt of the multicast message from the lighting control group monitor at a respective recipient lighting control device, the respective recipient lighting control device checks a lighting control group identifier to determine whether the respective recipient control device is a member of the identified lighting control group in the message. The recipient lighting control device then determines whether the recipient lighting control device has already acted on a lighting control event (turn on/off or dim) for lighting control network operation that is similar or identical to the event in the multicast message. If the recipient lighting control device has not already acted in accordance with the control event for lighting control operation, the recipient lighting control device adjusts one of its own LED light source(s) in accordance with the control event. Alternatively, if the recipient lighting control device has already acted on the lighting control event specified in the multicast message, no further action is taken in response by discarding the multicast message. FIG. 5 is a block diagram of a plug load controller 30 that communicates via the lighting control system of FIG. 1B. The circuitry, hardware, and software of plug load controller 30 shown is similar to the luminaire 10 of FIG. 3. However, plug load controller 30 is a retrofit device that plugs into existing AC wall outlets, for example, and allows existing wired lighting devices, such as table lamps or floor lamps that plug into a wall outlet, to operate in the lighting control system. The plug load controller 30 instantiates the table lamp or floor lamp by allowing for commissioning and maintenance operations and processes wireless lighting controls in order to the allow the lighting device to operate in the lighting control system. Plug load controller 30 is similar to luminaire 10 in that they are singularly addressable devices that can be configured to operate as a member of one or more lighting control groups or zones. As shown, plug load controller 30 includes a DC conversion circuit 505 (which may instead be a power supply) driven by a power source 500, in our example, an AC line or mains. Power source 500, however, may be a battery, solar panel, or any other AC or DC source. DC conversion circuit 505 receives power from the power source 500, and may include a magnetic transformer, electronic transformer, switching converter, rectifier, or any other similar type of circuit to convert an input power signal into a suitable power signal to power itself. Plug load controller 500 further comprises an AC power relay 560 which relays incoming AC power from power source 500 to other devices that may plug into the receptacle of plug load controller 30 thus providing an AC power outlet 570. Plug load controller 30 furthers include an LED driver circuit 510 and a light emitting diode(s) (LED) 520. LED driver circuit 510 is coupled to LED(s) 520 and drives that LED(s) 520 by regulating the power to LED(s) 520 by providing a constant quantity or power to LED(s) 520 as its electrical properties change with temperature, for example. The LED driver circuit 510 includes a driver circuit that provides power to LED(s) 520 and a pilot LED 517. LED driver circuit 510 may be a constant-voltage driver, constant-current driver, or AC LED driver type circuit that provides dimming through a pulse width modulation circuit and may have many channels for separate control of different LEDs or LED arrays. An example of a commercially available intelligent LED driver circuit 510 is manufactured by EldoLED. LED driver circuit 510 can further include an AC or DC current source or voltage source, a regulator, an amplifier (such as a linear amplifier or switching amplifier), a buck, boost, or buck/boost converter, or any other similar type of circuit or component. LED driver circuit 510 outputs a variable voltage or current to the LED(s) 520 that may include a DC offset, such that its average value is nonzero, and/or a AC voltage. The pilot LED 417 indicates the state of the plug load controller 30, for example, during the commissioning and maintenance process. For purposes of communication and control, plug load controller 30 is treated as single addressable device that can be configured to operate as a member of one or more lighting control groups or zones. The plug load controller 30 is line powered and remains operational as long as power is available. Plug load controller 30 includes power distribution circuitry 525 and a micro-control unit (MCU) 530. As shown, MCU 530 is coupled to LED driver circuit 510 and controls the light source operation of the LED(s) 520. MCU 530 includes a memory 522 (volatile and non-volatile) and a central processing unit (CPU) 523. The memory 522 includes a lighting application 527 (which can be firmware) for both lighting control operations and commissioning/maintenance operations. The power distribution circuitry 525 distributes power and ground voltages to the LED driver circuit 510, MCU 530, and wireless transceivers 545 and 550 to provide reliable operation of the various circuitry on the plug load controller 30 chip. Plug load controller 30 also includes a dual-band wireless radio communication interface system configured for two way wireless communication. In our example, plug load controller 30 has a radio set that includes radio 545 for sub-GHz communications and another radio 550 for Bluetooth RF communications. A first transceiver 545, such as a 900 MHz wireless transceiver, issues control operations on the lighting control network. This first transceiver 545 is for any-to-many (unicast and multicast) communication, over a first of the two different wireless communication bands, of control and systems operations information, during luminaire operation and during control network operation over the first wireless communication band. A second transceiver 550, such as a 2.4 GHz BLE (Bluetooth) wireless transceiver carries out commissioning and maintenance of the lighting control network. This second transceiver 550 is for point-to-point communication, over a second of the two different wireless communication bands, of information other than the control and systems operations information, concurrently with at least some communications over the first wireless communication band. As shown, the MCU 530 includes programming in the memory 522 which configures the CPU (processor) 523 to control operations of the respective plug load controller 30, including the communications over the two different wireless communication bands via the dual-band wireless radio communication interface system 545, 550. The programming in the memory 522 includes a real-time operating system (RTOS) and further includes a lighting application 527 which is firmware/software that engages in communications with the commissioning/maintenance application 22 of mobile device 25 over the commissioning network 7 of FIGS. 1A-B. The lighting application 527 programming in the memory 522 carries out lighting control operations over the lighting control network 5 of FIGS. 1A-B. The RTOS supports multiple concurrent processing threads for different simultaneous control or communication operations of the plug load controller 30. Although not shown, it should be understood that the MCU 530 of plug load controller 30 may be of the three different CPU and memory architectures depicted and described for the luminaire 10 in FIGS. 3A-C and the wall switch 20 in FIGS. 4A-C. As explained earlier, integrating the first transceiver 545 and second transceiver 550, for example, into a dual band SOC chipset of the MCU 530, saves manufacturing costs and conserves power (e.g., line power or battery power). Plug load controller 30 may include detector(s), such as a daylight sensor, an occupancy sensor, an audio sensor, a temperature sensor, or other environmental sensor (not shown). Detector(s) may be based on Acuity Brands Lighting's commercially available xPoint® Wireless ES7 product. Drive/sense circuitry (not shown), such as application firmware, can drive the occupancy and photo sensor hardware. FIG. 6 is a block diagram of a power pack 35 that communicates via the lighting control system of FIG. 1B. The circuitry, hardware, and software of power pack 35 shown is similar to the luminaire 10 of FIG. 3. However, power pack 35 is a device that retrofits with existing wired light fixtures (luminaires). The power pack 35 instantiates the wired light fixture by allowing for commissioning and maintenance operations and processes wireless lighting controls in order to allow the lighting device to operate in the lighting control system. Power pack 35 is similar to luminaire 10 in that they are singularly addressable devices that can be configured to operate as a member of one or more lighting control groups or zones. As shown, power pack 35 includes a DC conversion circuit 605 (which may instead be a power supply) driven by a power source 600, in our example, an AC line or mains. Power source 600, however, may be a battery, solar panel, or any other AC or DC source. DC conversion circuit 605 receives power from the power source 600, and may include a magnetic transformer, electronic transformer, switching converter, rectifier, or any other similar type of circuit to convert an input power signal into a suitable power signal to power itself. Power pack 35 further comprises an AC power relay 660 which relays incoming AC power from power source 600 to the existing wired luminaire. Power pack 35 furthers include an LED driver circuit 610. LED driver circuit 610 is coupled to luminaire and drives that luminaire by regulating a driving signal, in our example, a 0-10V dimming signal 620. The LED driver circuit 610 includes a driver circuit that provides power to a pilot LED 617 and a dimming signal to luminaire 620. LED driver circuit 610 may be a constant-voltage driver, constant-current driver, or AC LED driver type circuit that provides dimming through a pulse width modulation circuit and may have many channels for separate control of different LEDs or LED arrays. An example of a commercially available intelligent LED driver circuit 610 is manufactured by EldoLED. LED driver circuit 610 can further include an AC or DC current source or voltage source, a regulator, an amplifier (such as a linear amplifier or switching amplifier), a buck, boost, or buck/boost converter, or any other similar type of circuit or component. LED driver circuit 610 outputs a variable voltage or current as the dimming signal to luminaire(s) 620 that may include a DC offset, such that its average value is nonzero, and/or a AC voltage. The pilot LED 617 indicates the state of the power pack 35, for example, during the commissioning and maintenance process. For purposes of communication and control, power pack 35 is treated as single addressable device that can be configured to operate as a member of one or more lighting control groups or zones. The power pack 35 is line powered and remains operational as long as power is available. Power pack 35 includes power distribution circuitry 625 and a micro-control unit (MCU) 630. As shown, MCU 630 is coupled to LED driver circuit 610 and controls the light source operation of the luminaire via the dimming signal to luminaire 620. MCU 630 includes a memory 622 (volatile and non-volatile) and a central processing unit (CPU) 623. The memory 622 includes a lighting application 627 (which can be firmware) for both lighting control operations and commissioning/maintenance operations. The power distribution circuitry 625 distributes power and ground voltages to the LED driver circuit 610, MCU 630, and wireless transceivers 645 and 650 to provide reliable operation of the various circuitry on the power pack 35 chip. Power pack 35 also includes a dual-band wireless radio communication interface system configured for two way wireless communication. In our example, power pack 35 has a radio set that includes radio 645 for sub-GHz communications and another radio 650 for Bluetooth RF communications. A first transceiver 645, such as a 900 MHz wireless transceiver, issues control operations on the lighting control network. This first transceiver 645 is for any-to-many (unicast and multicast) communication, over a first of the two different wireless communication bands, of control and systems operations information, during luminaire operation and during control network operation over the first wireless communication band. A second transceiver 650, such as a 2.4 GHz BLE (Bluetooth) wireless transceiver carries out commissioning and maintenance of the lighting control network. This second transceiver 650 is for point-to-point communication, over a second of the two different wireless communication bands, of information other than the control and systems operations information, concurrently with at least some communications over the first wireless communication band. As shown, the MCU 630 includes programming in the memory 622 which configures the CPU (processor) 623 to control operations of the respective power pack 35, including the communications over the two different wireless communication bands via the dual-band wireless radio communication interface system 645, 650. The programming in the memory 622 includes a real-time operating system (RTOS) and further includes a lighting application 627 which is firmware/software that engages in communications with the commissioning/maintenance application 22 of mobile device 25 over the commissioning network 7 of FIGS. 1A-B. The lighting application 627 programming in the memory 622 carries out lighting control operations over the lighting control network 5 of FIGS. 1A-B. The RTOS supports multiple concurrent processing threads for different simultaneous control or communication operations of the power pack 35. Although not shown, it should be understood that the MCU 630 of power pack 35 may be of the three different CPU and memory architectures depicted and described for the luminaire 10 in FIGS. 3A-C and the wall switch 20 in FIGS. 4A-C. As explained earlier, integrating the first transceiver 645 and second transceiver 650, for example, into a dual band SOC chipset of the MCU 630, saves manufacturing costs and conserves power (e.g., line power or battery power). Power pack 35 may include detector(s), such as a daylight sensor, an occupancy sensor, an audio sensor, a temperature sensor, or other environmental sensor (not shown). Detector(s) may be based on Acuity Brands Lighting's commercially available xPoint® Wireless ES7 product. Drive/sense circuitry (not shown), such as application firmware, can drive the occupancy and photo sensor hardware. FIG. 7 is a flow chart presenting the states and transitions for the various lighting control devices of FIGS. 1A-B. As shown in FIG. 7, the various lighting control devices (luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35) go through a series of states and transitions during commissioning of the lighting control system, when lighting control operations are executed, and during maintenance. Beginning in block 700, lighting control devices are not yet powered up or installed. Moving now to block 710, upon power up after installation the lighting control devices behave as autonomous devices. There is no sub-GHz subnetwork to provide collaborative control, however the lighting control devices begin BLE beaconing to identify themselves to a commissioning/maintenance application 22 executing on a mobile device 25. Upon power up, luminaries 10A-N enter an autonomous control mode that permits the integrated detector(s) (e.g., occupancy, daylight/photo, or audio sensors) to exert limited control (lights on/off, dim up/down) of the light fixture. The control behavior is defined as default settings for the device. After power up, wall switches 20A-N may turn off their beacons after a predetermined time period (e.g., one hour) after powering up in order to conserve battery life. While in an installed state, the wall switches 20A-N can be induced to restart their beacons by pushing any button offered. For example, the wall switches 20A-N switch off their beacons after a predetermined time period (e.g., one hour) after a button push. On board pilot LEDs of the luminaires 10A-N, wall switches 20A-N, and other lighting control devices visually signal the state of the lighting control device (for all states) as an aid to the system installer and maintainer that is operating the commissioning/maintenance application 22 on the mobile device 25. The pilot LED goes off when the lighting control device is in an installed state. Continuing now to block 720, the luminaires 10A-N, wall switches 20A-N, and other lighting control devices enter a commissioning state from the installed state upon connection to the commissioning/maintenance application 22 of the mobile device 25. The luminaires 10A-N, wall switches 20A-N, and other lighting control devices receive configuration information via the commissioning/maintenance application 22 and will transition to an operational state upon completing the commissioning process and connecting to the group subnetwork. The advertising beacon signals a sub-state while the luminaires 10A-N and wall switches 20A-N undergo commissioning. The luminaires 10A-N, wall switches 20A-N, and other lighting control devices advertise an un-configured sub-state until completion of MAC-PHY configuration. Afterwards and until operational, the wall switches 20A-N or luminaires 10A-N advertise a waiting-connect (sub-GHz net) sub-state. Each of the luminaires 10A-N, wall switches 20A-N, and other lighting control devices is commanded to issue a blink during its commissioning phase, otherwise the LED is off. Proceeding now to block 730, the luminaires 10A-N, wall switches 20A-N, and other lighting control devices participate in collaborative group and zone lighting control while in an operational state. For example, sensors 365 of luminaires 10A-N, wall switches 20A-N, and other lighting control devices affect zone behavior by signaling control measures to the lighting elements in the zone's fixtures. As a security measure all luminaires 10A-N, wall switches 20A-N, and other lighting control devices, with the exception of the group monitor, cease BLE beaconing during the operational state. The group monitor changes its advertisement to indicate its role as the group monitor and its state (operational). The pilot LED remains off during the operational state. Continuing now to block 740, depending on condition, luminaires 10A-N, wall switches 20A-N, and other lighting control devices experiencing faults may enter a degraded state where partial capability is available. It may be possible to correct a degraded state through the commissioning/maintenance application 22 of the mobile device 25. In this case, the degraded luminaires 10A-N, wall switches 20A-N, and other lighting control devices are commanded to switch to the maintenance state, the commissioning/maintenance application 22 of the mobile device 25 is connected, a fix is attempted, and the device transitions to either operational state or back to degraded state depending on outcome of fix. Pilot LEDs can issue a bright S-O-S indication of three rapid blinks, three off counts, and three rapid blinks while in degraded state. Upon button push, wall switches issue the same S-O-S type of signal 5 times and then cease activity to conserve battery power. Moving now to block 750, luminaires 10A-N, wall switches 20A-N, and other lighting control devices can be commanded to enter a maintenance state. The command arrives over the lighting control network (sub-GHz network) from the group monitor. The luminaires 10A-N, wall switches 20A-N, and other lighting control devices maintain full or degraded operating capability while in the maintenance state. The luminaires 10A-N, wall switches 20A-N, and other lighting control devices resume BLE advertising (state=maintenance) seeking connection with commissioning/maintenance application 22 of the mobile device 25. Luminaires 10A-N, wall switches 20A-N, and other lighting control devices can then be re-configured via the commissioning/maintenance application 22 of the mobile device 25. The luminaires 10A-N, wall switches 20A-N, and other lighting control devices transition to an operational (or degraded) state upon command to exit the maintenance state. The pilot LED executes a continuous bright blink when in the maintenance state. Upon button push, wall switches 20A-N issue the same continuous bright blink type of signal 5 times and then cease LED activity to conserve battery power. FIG. 8 is a high-level functional block diagram of a mobile device 25 for commissioning and maintenance of the lighting control system of FIGS. 1A-B. Shown are elements of a touch screen type of mobile device 25 having the commissioning/maintenance application 22 loaded, although other non-touch type mobile devices can be used in the prior token-based communications under consideration here. Examples of touch screen type mobile devices that may be used include (but are not limited to) a smart phone, a personal digital assistant (PDA), a tablet computer or other portable device. However, the structure and operation of the touch screen type devices 25 is provided by way of example; and the subject technology as described herein is not intended to be limited thereto. For purposes of this discussion, FIG. 8 therefore provides a block diagram illustration of the example of mobile device 25 having a touch screen display for displaying content and receiving user input as (or as part of) the user interface. The activities that are the focus of discussions here typically involve data communications. As shown in FIG. 8, the mobile device 25 includes a first digital transceiver (XCVR) 809a, for digital wireless communications via a wide area wireless mobile communication network and second digital XCVR 810a for digital wireless communications via a Bluetooth network, although the mobile device 25 may include additional digital or analog transceivers (not shown). The transceiver 810a (network communication interface) conforms to one or more of the various digital wireless communication standards for Bluetooth communications. As discussed previously, communications through the Bluetooth transceiver 810a and the commissioning network 7 shown in FIGS. 1A-B relate to protocols and procedures in support of commissioning and maintaining lighting control devices, including luminaires 10A-N, wall switches 20A-N, plug load controller 30, and power pack 35. In addition, communications to gateway 50 are also supported. Such communications, for example, may utilize IP packet data transport utilizing the digital wireless transceiver (XCVR) 810a and over the air communications via commissioning network 7 shown in FIGS. 1A-B. Transceiver 810a connects through radio frequency (RF) send-and-receive amplifiers (not shown) to an antenna 810b. The transceiver 809a (network communication interface) conforms to one or more of the various digital wireless communication standards utilized by modern mobile networks. Examples of such transceivers include (but are not limited to) transceivers configured to operate in accordance with Code Division Multiple Access (CDMA) and 3rd Generation Partnership Project (3GPP) network technologies including, for example and without limitation, 3GPP type 2 (or 3GPP2) and LTE, at times referred to as “4G.” For example, transceiver 809a provides two-way wireless communication of information including digitized audio signals, still image and/or video signals, web page information for display as well as web related inputs, and various types of mobile message communications to/from the mobile device 25. In one example, the transceiver 809a sends and receives a variety of signaling messages in support of various data services provided by a network of a wireless service provider, to user(s) of mobile device 25 via a mobile communication network (not shown). Transceiver 809a also connects through radio frequency (RF) send-and-receive amplifiers (not shown) to an antenna 809b. Many modern mobile device(s) 25 also support wireless local area network communications over WiFi, instead of or in addition to data communications using the wide area mobile communication network. Hence, in the example of FIG. 8, for packet data communications, mobile device 25 may also include a WiFi transceiver 811a and associated antenna 811b. Although WiFi is used here as the example, the transceiver 811a may take the form of any available two-way wireless local area network (WLAN) transceiver of a type that is compatible with one or more standard protocols of communication implemented in wireless local area networks, such as one of the WiFi standards under IEEE 802.11 and/or WiMAX. The transceiver 811a, for example, may provide two-way data transport for wireless communication with a wireless access point in a residence or enterprise that the user frequents or with any available hotspot offered in a public venue. A WiFi access point (not shown), communicates with compatible user equipment, such as the mobile device 25, over the air using the applicable WiFi protocol. The WiFi access point provides network connectivity, usually to a wide area network 55 (as shown in FIGS. 1A-B), such as the Internet. In a home or office premises, for example, the WiFi access point would connect directly or via a local area network (LAN) to a line providing internet access service. In a more public venue, an access point configured as a hotspot may offer similar connectivity for customers or others using the venue, on terms and conditions set by the venue operator. Although communicating through a different network or networks, the transceiver 811a supports various types of data communications similar to the packet data communications supported via the mobile network transceiver 809a, including communications to and from gateway 50 and the other devices shown in FIGS. 1A-B. The mobile device 25 further includes a microprocessor, sometimes referred to herein as the host controller 802. A processor 802 is a circuit having elements structured and arranged to perform one or more processing functions, typically various data processing functions. Although discrete logic components could be used, the examples utilize components forming a programmable CPU. A microprocessor 802 for example includes one or more integrated circuit (IC) chips incorporating the electronic elements to perform the functions of the CPU. The processor 802, for example, may be based on any known or available microprocessor architecture, such as a Reduced Instruction Set Computing (RISC) using an ARM architecture, as commonly used today in mobile devices and other portable electronic devices. Of course, other processor circuitry may be used to form the CPU or processor hardware in mobile device 25, other devices and server computers (e.g., gateway 50), network elements, etc. Returning more specifically to the mobile device 25 example of FIG. 8, the microprocessor 802 serves as a programmable host controller for mobile device 25 by configuring device 25 to perform various operations, for example, in accordance with instructions or programming executable by processor 802. For example, such operations may include various general operations of the mobile device 25, as well as operations related to communications with luminaires 10A-N, wall switches 20A-N and other lighting control devices during commissioning and maintenance performed by the commissioning/maintenance application 22. Although a processor may be configured by use of hardwired logic, typical processors in mobile devices are general processing circuits configured by execution of programming. The mobile device 25 includes a memory or storage system 804, for storing data and programming. In the example, the memory system 804 may include a flash memory 804a and a random access memory (RAM) 804b. The RAM 804b serves as short term storage for instructions and data being handled by the processor 802, e.g. as a working data processing memory. The flash memory 804a typically provides longer term storage. Hence, in the example of mobile device 25, the flash memory 804a is used to store programming or instructions for execution by the processor 802. Depending on the type of device, the mobile device 25 stores and runs a mobile operating system through which specific applications, including commissioning/maintenance application 22 (which may be a web browser executing a dynamic web page) or a native application, run on the mobile device 25. Examples of mobile operating systems include Google Android, Apple iOS (I-Phone or iPad devices), Windows Mobile, Amazon Fire OS, RIM BlackBerry operating system, or the like. Flash memory 804a may also be used to store mobile configuration settings for different mobile applications or services executable at device 25 using processor 802. Of course, other storage devices or configurations may be added to or substituted for those in the example. Such other storage devices may be implemented using any type of storage medium having computer or processor readable instructions or programming stored therein and may include, for example, any or all of the tangible memory of the computers, processors or the like, or associated modules. The instructions or programming may be used to implement any other device functions associated with communications for commissioning and maintenance on mobile device 25. Program aspects of the technology may be thought of as “products” or “articles of manufacture” typically in the form of executable code or process instructions and/or associated data that is stored on or embodied in a type of machine or processor readable medium (e.g., transitory or non-transitory), such as one of the memories 804a, 804b of memory system 804, or a memory of a computer used to download or otherwise install such programming into the mobile device, or a transportable storage device or a communications medium for carrying program for installation in the mobile device 25. In the example, the flash memory 804a stores applications for execution by the microprocessor-based host controller 802, typically through operation/execution of the device operating system. Of note, for purposes of the present discussion, the flash memory 804 stores a commissioning/maintenance application 22 as one of the programs for execution by the microprocessor 802. Execution of commissioning/maintenance application 22 by the microprocessor 802 configures mobile device 25 to perform a variety of functions, particularly to commission and maintain the lighting control devices over the commissioning network 7. In the example, commissioning/maintenance application 22 also engages in communications with the gateway 50. In the illustrated example, the mobile device 25 includes a secure component 800. The secure component 800 (e.g. a secure element or “SE”) may be provisioned as a section within the memory 804 or may take the form of a universal integrated circuit card (UICC) located within the device 25. A common example of a UICC implementation of the SE 800 is a subscriber identity module (SIM). As discussed above, the SE provides secure storage for various identifiers associated with mobile device 25. The SE typically has a unique identifier and is provisioned for operation of the mobile device 25 by storage of a mobile directory number (MDN) and/or mobile identification number (MIN) assigned to the device 25 by the carrier network operator. The secure component contains applications that use secure keys running inside the secure processor. Although similar to other applications, the applications for the secure processor are sometimes smaller and sometimes referred to as applets 843. In an example, commissioning/maintenance application 22 may be an applet residing in the SE 800. For example, there may be at least one applet 842 to engage in communications. The mobile device 25 may include a variety of different types of physical user interface elements to interact with the commissioning/maintenance application 22. For discussion purposes, in the mobile device 25 shown in FIG. 8, the physical user interface elements of device 20 includes a touch screen display 820 (also referred to herein as “touch screen 820” or “display 820”) to support gestures. For output purposes, the touch screen 820 includes a display screen, such as a liquid crystal display (LCD) or the like. For input purposes, touch screen display 820 includes a plurality of touch sensors 822. A keypad may be implemented in hardware as a physical keyboard of mobile device 25, and keys may correspond to hardware keys of such a keyboard. Alternatively, some or all of the keys 830 (and keyboard) of device 25 may be implemented as “soft keys” of a virtual keyboard graphically represented in an appropriate arrangement via touch screen display 820. The soft keys presented on the touch screen display 820 may allow the user of device 25 to invoke the same user interface functions as with the physical hardware keys for authentication purposes. In general, touch screen display 820 and touch sensors 822 (and one or more keys 630, if included) are used to provide a textual and graphical user interface for the mobile device 25. In an example, touch screen display 820 provides viewable content to the user at device 25. Touch screen display 820 also enables the user to interact directly with the viewable content provided in the content display area, typically by touching the surface of the screen with a finger or an implement such as a stylus. As shown in FIG. 8, the mobile device 25 also includes a sense circuit 828 coupled to touch sensors 822 for detecting the occurrence and relative location/position of each touch with respect to a content display area of touch screen display 820. In this example, sense circuit 828 is configured to provide processor 802 with touch-position information based on user input received via touch sensors 822. In some implementations, processor 802 is configured to correlate the touch position information to specific content being displayed within the content display area on touch screen display 820. The touch-position information captured by the sense circuit 828 and provided to processor 802 may include, but is not limited to, coordinates identifying the location of each detected touch with respect to the display area of touch screen display 820 and a timestamp corresponding to each detected touch position. Accordingly, the processor 802 may determine input of a phone number, a token, or menu identifiers selected during audible scripts, for example. Various packet formats are shown in FIGS. 9A-C. In FIG. 9A, a media access control (MAC) layer message for communicating a state change event to a lighting control device on a lighting control network is shown. As shown, a MAC layer message 900 includes the following fields: option(s) 905, a source identifier 910, an RSSI/tag 915, a length of message 920, and a protocol data unit (PDU) or payload. In an example, the protocol for communicating the state change event is the AT command-response protocol defined in the SiLabs SPP-Over-BLE Application Note, 15, Nov. 2013, version 1.0, section 7. Options 905 may include a namespace field that has a command identifier. Source 910 identifies the lighting control device that has detected the state change event, for example, the source is the short sub-GHz MAC address of the detecting lighting control device. Length 920 specifies the length of the message, for example, number of bytes of the whole message (header plus payload plus checksum). Payload 925 is device specific and the form of the payload 925 is interpreted and managed by the lighting application 327. The MAC layer message 900 may further include a destination address (not shown) which is the sub-GHz short MAC address of the destination lighting control device (e.g., group/zone monitor). FIG. 9B is a transport layer message for communicating a state change event to a lighting control device on a lighting control network. As shown, the transport layer message 930 includes the following fields: version 935, protocol 940, multicast identification 945, and lighting control group/zone identification 950. Version 935 specifies the firmware protocol version of the lighting application 327, for example. Protocol 940 specifies the lighting control network command communication protocol. Multicast identification 945 specifies the broadcast channel or an address of the lighting control group/zone. Lighting control group/zone 950 identifies the lighting control group or zone of the lighting control device that detected the state change event. FIG. 9C is an application layer message for communicating a state change event to a lighting control device on a lighting control network. As shown, the application layer message 960 includes the broadcast channel or address of all of the lighting control group(s)/zone(s) that should receive the message. A lighting control group/zone monitor peaks into the application layer message 960 body and extracts the payload to pass the message to local and downstream lighting control devices. It will be understood that the terms and expressions used herein have the ordinary meaning as is accorded to such terms and expressions with respect to their corresponding respective areas of inquiry and study except where specific meanings have otherwise been set forth herein. Relational terms such as first and second and the like may be used solely to distinguish one entity or action from another without necessarily requiring or implying any actual such relationship or order between such entities or actions. The terms “comprises,” “comprising,” “includes,” “including,” or any other variation thereof, are intended to cover a non-exclusive inclusion, such that a process, method, article, or apparatus that comprises a list of elements does not include only those elements but may include other elements not expressly listed or inherent to such process, method, article, or apparatus. An element preceded by “a” or “an” does not, without further constraints, preclude the existence of additional identical elements in the process, method, article, or apparatus that comprises the element. Unless otherwise stated, any and all measurements, values, ratings, positions, magnitudes, sizes, and other specifications that are set forth in this specification, including in the claims that follow, are approximate, not exact. They are intended to have a reasonable range that is consistent with the functions to which they relate and with what is customary in the art to which they pertain. While the foregoing has described what are considered to be the best mode and/or other examples, it is understood that various modifications may be made therein and that the subject matter disclosed herein may be implemented in various forms and examples, and that they may be applied in numerous applications, only some of which have been described herein. It is intended by the following claims to claim any and all modifications and variations that fall within the true scope of the present concepts."},"background":{"kind":"string","value":"<SOH> BACKGROUND <EOH>Traditional luminaires can be turned ON and OFF, and in some cases may be dimmed, usually in response to user activation of a relatively simple input device. Often traditional luminaires are controlled individually or as relatively small groups at separate locations. More sophisticated lighting control systems automate the operation of the luminaires throughout a building or residence based upon preset time schedules, occupancy, and/or daylight sensing. Such lighting control systems receive sensor signals at a central lighting control panel, which responds to the received signals by deciding which, if any, relays, switching devices, and/or dimming ballasts to drive in order to turn on or off and/or adjust the light levels of one or more luminaires. More recent lighting systems are wireless; however, operating luminaires to operate over wireless communication systems using group based controls can be difficult. For example, multiple simultaneous control requests can ovewhelm a node that is tasked with managing the group. Accordingly, a system is needed to overcome these and other limitations in the art."},"summary":{"kind":"string","value":"<SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>The drawing figures depict one or more implementations in accord with the present teachings, by way of example only, not by way of limitation. In the figures, like reference numerals refer to the same or similar elements. FIG. 1A is a high-level functional block diagram of an example of a system of networks and devices that provide a variety of lighting controls, including communications in support of turning lights on/off, dimming, set scene, and sensor trip events. FIG. 1B is another high-level functional block diagram of an example of a system of networks and devices that further includes plug load controller and power pack devices and various lighting control groups. FIG. 2 is a state change event protocol procedure for the lighting control system of FIGS. 1A-B . FIGS. 3A-C are block diagrams of luminaires that communicate via the lighting control system of FIG. 1A or FIG. 1B . FIGS. 4A-C are block diagrams of different examples of a wall switch that communicates via the lighting control system of FIG. 1A or FIG. 1B . FIG. 5 is a block diagram of a plug load controller that communicates via the lighting control system of FIG. 1B . FIG. 6 is a block diagram of a power pack that communicates via the lighting control system of FIG. 1B . FIG. 7 is a flow chart presenting the states and transitions for the various lighting control devices of FIGS. 1A-B . FIG. 8 is a high-level functional block diagram of a mobile device for commissioning and maintenance of the lighting control system of FIGS. 1A-B . FIG. 9A is a media access control (MAC) layer message for communicating a state change event to a lighting control device on a lighting control network. FIG. 9B is a transport layer message for communicating a state change event to a lighting control device on a lighting control network. FIG. 9C is an application layer message for communicating a state change event to a lighting control device on a lighting control network. detailed-description description=\"Detailed Description\" end=\"lead\"?"},"cpc_label":{"kind":"string","value":"H05B370272"},"filing_date":{"kind":"string","value":"20170927"},"patent_issue_date":{"kind":"string","value":"20180626"},"date_published":{"kind":"string","value":"20180201"},"examiner_id":{"kind":"string","value":"57220.0"},"ipc_label":{"kind":"string","value":"H05B3702"},"npe_litigated_count":{"kind":"number","value":0,"string":"0"},"examiner_full_name":{"kind":"string","value":"LE, TUNG X"},"invention_title":{"kind":"string","value":"PROTOCOL FOR LIGHTING CONTROL VIA A WIRELESS NETWORK"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"H05B"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32888,"cells":{"application_number":{"kind":"number","value":15717502,"string":"15,717,502"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"Novel Reagents for Directed Biomarker Signal Amplification"},"abstract":{"kind":"string","value":"Described herein are methods, compositions and articles of manufacture involving neutral conjugated polymers including methods for synthesis of neutral conjugated water-soluble polymers with linkers along the polymer main chain structure and terminal end capping units. Such polymers may serve in the fabrication of novel optoelectronic devices and in the development of highly efficient biosensors. The invention further relates to the application of these polymers in assay methods."},"claims":{"kind":"string","value":"1-40. (canceled) 41. A water soluble conjugated polymer having the structure of the formula: wherein: Ar is an aryl or heteroaryl unit substituted with a non-ionic side group capable of imparting solubility in water; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18 (hetero)aryloxy, C2-C18 (hetero)arylamino, a C2-C18 (hetero)aryl group and (CH2)x′(OCH2CH2)y′OCH3 where x′ is independently an integer from 0-20 and y′ is independently an integer from 0 to 50; optional linkers L1 and L2 are each independently an aryl or a heteroaryl group evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with: i) a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated ester, N-hydroxysuccinimidyl, hydrazine, hydrazide, hydrazone, azide, alkyne, aldehyde, thiol, and protected groups thereof for conjugation to a molecule or biomolecule; or ii) a conjugated organic dye or biomolecule; G1 and G2 are each independently selected from hydrogen, halogen, alkyne, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic ester, boronic acid, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with: i) a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazine, hydrazide, hydrazone, azide, alkyne, aldehyde, thiol, and protected groups thereof for conjugation to a molecule or biomolecule; or ii) a conjugated organic dye or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated ester, N-hydroxysuccinimidyl, hydrazines, hydrazide, hydrazone, azide, alkyne, aldehyde, and thiol within G1, G2, L1 or L2, or a conjugated organic dye or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. 42. The water soluble conjugated polymer according to claim 41, wherein MU is selected from optionally substituted benzothiadiazole, benzoxidazole, benzoselenadiazole, benzotellurodiazole, naphthoselenadiazole, 4,7-di(thien-2-yl)-2,1,3-benzothiadiazole, squaraine dyes, quinoxaline, perylene, perylene diimide, diketopyrrolopyrrole, thienopyrazine low bandgap commercial dyes, olefin, and cyano-substituted olefins and isomers thereof. 43. The water soluble conjugated polymer according to claim 41, wherein MU is selected from the group consisting of a′- k′ having the structure: wherein * is a site for covalent attachment to unsaturated backbone and each R is a non-ionic side group capable of imparting solubility in water. 44. The water soluble conjugated polymer according to claim 43, wherein MU is selected from one of the following: wherein * is site for covalent attachment to unsaturated backbone. 45. The water soluble conjugated polymer according to claim 41, wherein MU is a phenyl. 46. The water soluble conjugated polymer according to claim 45, wherein MU is wherein *=site for covalent attachment to unsaturated backbone. 47. The water soluble conjugated polymer according to claim 41, wherein the non-ionic side group comprises an ethylene glycol oligomer. 48. The water soluble conjugated polymer according to claim 47, wherein the non-ionic side group comprises mPEG5, mPEG8, mPEG11 or mPEG24. 49. The water soluble conjugated polymer according to claim 47, wherein Ar is substituted with one or more groups selected from (CH2)x′(OCH2CH2)y′OCH3 where x′ is independently an integer from 0-20 and y′ is independently an integer from 0 to 50, and a benzyl substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)zOCH3 where z is independently an integer from 0 to 50. 50. The water soluble conjugated polymer according to claim 47, wherein Ar is substituted with one or more (CH2)x′(OCH2CH2)y′OCH3 where x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50. 51. The water soluble conjugated polymer according to claim 47, wherein Ar is substituted with a dendrimer of PAMAM, PEA, PEHAM, PPI, tri-branched benzoate, or glycerol with a generation of 1 to 4 and optional terminal substitutions selected from (- - - - -)CH2CH2O)jCH3 and (- - - - -)OCH2CH2)jCH3 where j is an integer from 0 to 25 and the dotted lines (- - - - -) are each independently selected from any one or a combination of, C1-C12 alkyl, C1-C12 alkoxy, C2-C12 alkene, amido, amino, aryl, (CH2)r(OCH2CH2)s(CH2)r where each r is independently an integer from 0-20, s is independently an integer from 0 to 50, carbamate, carboxylate, C3-C12 cycloalkyl, imido, phenoxy and C4-C18(hetero)aryl group. 52. The water soluble conjugated polymer according to claim 41, wherein Ar is a substituted fluorene unit. 53. The water soluble conjugated polymer according to claim 41, wherein L1 and/or L2 are present. 54. The water soluble conjugated polymer according to claim 53, wherein L1 and/or L2 is conjugated to a signaling chromophore. 55. The water soluble conjugated polymer according to claim 53, wherein L1 and/or L2 have the structure: wherein: *=site for covalent attachment to backbone; each R25 is independently a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl; (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50; aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups; and at least one R25 is terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated ester, N-hydroxysuccinimidyl, hydrazine, hydrazide, hydrazone, azide, alkyne, aldehyde and thiols, or a conjugated organic dye or biomolecule. 56. The water soluble conjugated polymer according to claim 55, wherein L1 and/or L2 have the structure: 57. The water soluble conjugated polymer according to claim 41, wherein at least one of G1 and G2 comprises a functional conjugation site. 58. The water soluble conjugated polymer according to claim 57, wherein at least one of G1 and G2 has the structure: wherein: *=site for covalent attachment to backbone; and R11 is a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x wherein each x is independently an integer from 0-20 and p is an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonate, sulfide, disulfide, or imido groups; and is terminated with: i) a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof, or ii) a conjugated organic dye or biomolecule. 59. The water soluble conjugated polymer according to claim 41, wherein at least one of G1 and G2 is selected from the group consisting of capping units 1-31 having the structures: wherein: *=site for covalent attachment to backbone; k is 2, 4, 8, 12 or 24; and R15 is selected from the group consisting of 1-t having the structures: 60. The water soluble conjugated polymer according to claim 59, wherein at least one of G1 and G2 is selected from one of the following structures:"},"description":{"kind":"string","value":"CROSS-REFERENCE This application is a continuation of application Ser. No. 15/239,713, filed Aug. 17, 2016; which application is a continuation of application Ser. No. 14/821,386, filed Aug. 7, 2015 and issued as U.S. Pat. No. 9,547,008; which application is a continuation of application Ser. No. 14/018,985, filed Sep. 5, 2013 and issued as U.S. Pat. No. 9,139,869; which application is a continuation of application Ser. No. 13/009,764, filed Jan. 19, 2011 and issued as U.S. Pat. No. 8,575,303, which claims the benefit of U.S. Provisional Application Ser. No. 61/296,379, filed Jan. 19, 2010 and U.S. Provisional Application Ser. No. 61/358,406, filed Jun. 24, 2010, which applications are incorporated herein by reference in their entireties. BACKGROUND OF THE INVENTION Fluorescent hybridization probes have developed into an important tool in the sequence-specific detection of DNA and RNA. The signals generated by the appended fluorescent labels (or dyes) can be monitored in real time and provide simple, rapid, and robust methods for the detection of biological targets and events. Utility has been seen in applications ranging from microarrays and real time PCR to fluorescence in situ hybridization (FISH). Recent work in the area of multichromophores, particularly regarding conjugated polymers (CPs) has highlighted the potential these materials have in significantly improving the detection sensitivity of such methods (Liu and Bazan, Chem. Mater., 2004). The light harvesting structures of these materials can be made water soluble and adapted to amplify the fluorescent output of various probe labels (See U.S. patent application Ser. No. 10/600,286, filed Jun. 20, 2003 and Gaylord, Heeger, and Bazan, Proc. Natl. Acad. Sci., 2002, both of which are incorporated herein by reference in their entirety). Results such as these indicate CPs to be highly promising in the field of nucleic acid diagnostics, particularly where sample quantities are scarce. However, there exist methods for the amplification (or replication) of nucleic acid targets, i.e., PCR. Comparatively, in the field of protein recognition, there are no such simple methods for amplifying the targeted materials. As such, signal enhancement arising from CP application is of high consequence in this area. Dye-labeled antibodies are regularly used for the detection of protein targets in applications such as immunohistochemistry, protein arrays, ELISA tests, and flow cytometry. Integrating CP materials into such methodologies promises to provide a dramatic boost in the performance of such assays, enabling detection levels previously unattainable with conventional fluorescent reporters (e.g., dyes). Beyond addition signal, one of the other key drivers in biological detection formats is the ability to detect multiple analytes in the same test or multiplexing. This is commonly achieved by using fluorescent reporters with operate at different, decernable wavelengths. CP materials are ideally suited to provide a platform for expanded multiplexing. This can be achieved by tuning the structure of different CPs to operate at different wavelengths or by incorporating a dye within the polymer-biomolecule conjugate. The material and methods to produce higher sensitivity biological assays and increase multiplexing are highly desired in both molecular (nucleic acid) and immunoassay formats. SUMMARY OF THE INVENTION Provided herein are water soluble conjugated polymers of Formula (I): wherein: each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x′(OCH2CH2)y′OCH3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C2-C18(hetero)aryl group; each optional linker L1 and L2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another substrate, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G1 and G2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, and thiols within G1, G2, L1 or L2 that allows, for functional conjugation to another molecule, substrate or biomolecule; each dashed bond, - - - - - - , is independently a single bond, triple bond or optionally substituted vinylene (—CR5═CR5—) wherein each R5 is independently hydrogen, cyano, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. In one aspect, water soluble conjugated polymers of Formula (I) have the structure of Formula (Ia): wherein R, L1, L2, G1, G2, MU, a, b, c, d and n are described previously for formula (I). In some embodiments, each R is independently (CH2)x(OCH2CH2)yOCH3 where each x is independently an integer from 0-20, each y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)zOCH3 where each z is independently an integer from 0 to 50. In some instances, each R is (CH2)3(OCH2CH2)11OCH3. In other embodiments, each R is a benzyl substituted with at least one (OCH2CH2)10OCH3 group. In some instances, the benzyl is substituted with two (OCH2CH2)10OCH3 groups. In other instances, the benzyl is substituted with three (OCH2CH2)10OCH3 groups. In some embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to unsaturated backbone; wherein R3 is independently hydrogen, halogen, alkoxy(C1-C12), C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and q is an integer from 0 to 4. In other embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to unsaturated backbone wherein A is a site for conjugation, chain extension or crosslinking and is [O—CH2—CH2]q—W, or (C1-C12)alkoxy-X or C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule.; W is —OH or —COOH; X is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]tNH2; q is an integer from 1 to 20; and t is an integer from 1 to 8. In yet other embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to backbone wherein R25 are each independently any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups; wherein at least one R25 is terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In further embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to unsaturated backbone; wherein R35 is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In further embodiments, optional linkers L1 or L2 are selected from the group consisting of a-h having the structures: *=site for covalent attachment to unsaturated backbone; wherein R′ is independently H, halogen, C1-C12 alkyl, (C1-C12 alkyl)NH2, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C2-C18(hetero)aryl, C2-C18(hetero)arylamino, —[CH2—CH2]r′—Z1, or (C1-C12)alkoxy-X1; and wherein Z1 is —OH or —COOH; X1 is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]s′(CH2)s′NH2; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH2)3(OCH2CH2)x″OCH3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)y—OCH3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein k is 2, 4, 8, 12 or 24; wherein R15 is selected from the group consisting of 1-t having the structure: *=site for covalent attachment to backbone. In yet further embodiments, optional linkers L1 or L2 are In some embodiments, G1 and G2 are each independently selected from hydrogen, halogen, alkyne, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorine and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In some embodiments, G1 and G2 each independently have the structure wherein R11 is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In other embodiments, G1 and G2 are each independently selected from the group consisting of 1-31 having the structures: *=site for covalent attachment to backbone wherein R15 is selected from the group consisting of 1-t having the structure: and k is 2, 4, 8, 12 or 24. In further embodiments, G1 and G2 are optionally substituted aryl or heteroaryl wherein the optional substituent is selected from halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiol, boronic acid, boronate radical, boronic esters and optionally substituted fluorene. In some embodiments, G1 and G2 are the same. In other embodiments, G1 and G2 are different. In further embodiments, the polymer contains a single conjugation site at only one terminus of the polymer chain G1 or G2. In yet further embodiments, G1 and G2 is In some embodiments, MU is selected from the group consisting of a′-k′ having the structure: *=site for covalent attachment to unsaturated backbone wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein at least one of G1 or G2 comprises a functional conjugation site. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein L1 comprises a functional conjugation site. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein at least one of G1 or G2 comprises a functional conjugation site. In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In some instances, a signaling chromophore is attached to the polymer via the NH2 group. In certain instances, the signaling chromophore is Cy3 or Dylight 594 dye. In certain instances, the linker, is about 10% of the entire polymer. In other instances, the polymer is conjugated to a secondary dye reporter and an antibody. In some embodiments of conjugated polymers described herein, the polymer is further conjugated to additional molecules. In some embodiments, the polymer is conjugated to a streptavidin, antibody or nucleic acid and used as a direct fluorescent reporter. In certain embodiments, the polymer is conjugated to a streptavidin. In other embodiments, the polymer is conjugated to thiol groups at the hinge region of an antibody. In yet other embodiments, the polymer is conjugated to an amine group on a protein which is modified with a heterobifuntional linker. In further embodiments, the polymer is conjugated to a nucleic acid. In yet further embodiments, the polymer is conjugated to an antibody. In certain instances, the polymer is conjugated to a monoclonal antibody, a secondary antibody or a primary antibody. In other instances, a polymer antibody conjugate is excited at about 405 nm in a flow cytometry assay where the specific signal is at least 3 fold greater than the same antibody conjugated to Pacific Blue. In some embodiments of conjugated polymers described herein, the polymer is purified by ion exchange chromatography. In other embodiments, the polymer is >95% pure. In some embodiments of conjugated polymers described herein, the polymer is used in flow cytometry assays to identify different cell markers or cell types. In other embodiments, the polymer is used to sort cells. In yet other embodiments, the polymer is used to sort cells for use in therapeutics. In some embodiments of conjugated polymers described herein, the polymer is used for intracellular staining. In certain instances, the polymer is used in flow cytometry assays to identify different cell markers or cell types. In some embodiments of conjugated polymers described herein, the polymer comprises a minimum number average molecular weight of greater than 40,000 g/mol and a water solubility of greater than 50 mg/mL in pure water or a phosphate buffered saline solution. In some embodiments of conjugated polymers described herein, the polymer comprises at least two unique conjugation linkers which can conjugated to two unique materials. Also provided herein are assay methods comprising providing a sample that is suspected of containing a target biomolecule; providing a sensor protein conjugated to at least one signaling chromophore and is capable of interacting with the target biomolecule or a target-associated biomolecule; providing a water soluble conjugated polymer described herein; contacting the sample with the sensor protein and the conjugated polymer in a solution under conditions in which the sensor protein can bind to the target biomolecule or a target-associated biomolecule if present; applying a light source to the sample that can excite the conjugated polymer; and detecting whether light is emitted from the signaling chromophore. In some embodiments, the sensor protein is an antibody. In other embodiments, the sensor protein comprises a plurality of sensor proteins conjugated to a plurality of signaling chromophores, wherein at least two of the plurality of chromophores emit different wavelengths of light upon energy transfer from the multichromophore. Also provided herein are conjugated polymer complexes comprising a polymer coupled to at least one biomolecule selected from the group consisting of a sensor biomolecule, a bioconjugate and a target biomolecule wherein the polymer is covalently bound by at least one bioconjugation site pendant thereto, and the polymer comprises a signaling chromophore or a signaling chromophore optionally is covalently bound to the polymer or the sensor biomolecule; wherein the polymer comprises the structure of formula: wherein: each R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x′(OCH2CH2)y′OCH3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C2-C18(hetero)aryl group; each optional linker L1 and L2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another molecule, substrate or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G1 and G2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, and thiols within G1, G2, L1 or L2 that allows, for functional conjugation to another molecule, substrate or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. In some embodiments, the sensor biomolecule is selected from the group consisting of an avidin, streptavidin, neutravidin, avidinDN, and avidinD. In other embodiments, the conjugated polymer complex is further configured to bind to a complex selected from the group consisting of a biotin-labeled antibody, biotin-labeled protein, and biotin-labeled target biomolecule. In further embodiments, the sensor biomolecule is an antibody. In yet further embodiments, both the signaling chromophore and the sensor biomolecule are covalently linked to the multichromophore through a plurality of linkers. In some other embodiments, both the signaling chromophore and the sensor biomolecule are covalently linked to the polymer through a central linking site that covalently binds the polymer, the signaling chromophore and the sensor biomolecule. In yet other embodiments, the signaling chromophore, when covalently bound to the polymer or the sensor biomolecule, is an organic dye. Also provided herein are water soluble conjugated polymer having the structure of Formula (Ia): wherein: each R is independently (CH2)x(OCH2CH2)yOCH3 where each x is independently an integer from 0-20, y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)zOCH3 where each z is independently an integer from 0 to 50; each optional linker L1 or L2 is selected from the group consisting of a-i having the structure *=site for covalent attachment to unsaturated backbone wherein R′ is independently H, halogen, C1-C12 alkyl, (C1-C12 alkyl)NH2, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C2-C18(hetero)aryl, C2-C18(hetero)arylamino, —[CH2—CH2]r′—Z1, or (C1-C12)alkoxy-X1; and wherein Z1 is —OH or —COOH; X1 is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]s′(CH2)s′NH2; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH2)3(OCH2CH2)x″OCH3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)y″OCH3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein R15 is selected from the group consisting of 1-t having the structure: and k is 2, 4, 8, 12 or 24; *=site for covalent attachment to backbone MU is a polymer modifying unit or band gap modifying unit that is selected from the group consisting of a′-k′ having the structure: *=site for covalent attachment to unsaturated backbone; wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; G1 and G2 are each independently selected from the group consisting of 1-31 having the structures: wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, and thiols within G1, G2, L1 or L2 that allows, for functional conjugation to another molecule, substrate or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. Also provided herein are water soluble conjugated polymer having the structure of Formula: wherein Ar is an aryl or heteroaryl and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x′(OCH2CH2)y′OCH3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50; and dashed bonds, L1, L2, G1, G2, MU, a, b, c, d and n are described previously for formula (I). INCORPORATION BY REFERENCE All publications, patents, and patent applications mentioned in this specification are herein incorporated by reference to the same extent as if each individual publication, patent, or patent application was specifically and individually indicated to be incorporated by reference. BRIEF DESCRIPTION OF THE DRAWINGS The novel features of the invention are set forth with particularity in the appended claims. A better understanding of the features and advantages of the present invention will be obtained by reference to the following detailed description that sets forth illustrative embodiments, in which the principles of the invention are utilized, and the accompanying drawings of which: FIG. 1. Schematic of binding of a conjugated polymer in one embodiment of the invention. FIG. 2. Schematic of a bioconjugated polymer of one embodiment of the invention. FIG. 3. Schematic of exemplary conjugated polymers conjugated (A) antibody; (B) an avidin; (C) nucleic acid; (D) dye, e.g., chromophore. FIG. 4. Schematic of (A) a polymer conjugated to dye-labeled antibody resulting in FRET; (B) a polymer conjugated dye-labeled strepavidin resulting in FRET; (C) nucleic acid probe sequences labeled with a quencher molecule conjugated to a conjugated polymer; (D) nucleic acid probe sequences labeled with a quencher molecule conjugated polymer-dye tandem complex. FIG. 5. Schematic of various methods of assaying for a target biomolecule or target associated biomolecule. (A) Conjugated polymer linked to a bioconjugate; (B) polymer and dye labeled antibodies recognize a common target; (C) sensor biomolecule conjugated to both a dye and a second bioconjugate; (D) second bioconjugate and the signaling chromopohre both conjugated to a nucleic acid. FIG. 6. Schematic of an addition of a second linking site within the polymer. FIG. 7. Schematic of a polymer conjugated to a dye and a biomolecule and resulting energy transfer (A) polymer is conjugated to both a bioconjugate; (B) polymer is conjugated to a strepavidin and a dye; (C) polymer is conjugated to a nucleic acid and a dye. FIG. 8. Schematic of indirect associations with a sensor biomolecule or target associated biomolecule. (A) biotinylated antibody interacting with a covalent conjugate of the conjugated polymer; (B) biotinylated antibody conjugated polymer-dye tandem complex; (C) biotinylated nucleic acid interacting with a covalent conjugate of the conjugated polymer; (D) biotinylated nucleic conjugated polymer-dye tandem complex; (E) nucleic acid with digoxygenin moiety interacting with a covalent conjugate of the conjugated polymer; (F) nucleic acid with digoxygenin moiety conjugated polymer-dye tandem complex. FIG. 9. Schematic of exemplary conjugated polymers conjugated to secondary antibodies ( ) and primary antibodies (B). FIG. 10. Schematic of a sandwich-type complex. (A) conjugated polymer complex bioconjugated to a strepavidin; (B) biotin-labeled 1° antibody e used to probe the target protein directly. FIG. 11. Schematic of appending one or two phenyl capping units to a fluorene polymer. FIG. 12. Block diagram showing a representative example logic device. FIG. 13. Block diagram showing a representative example of a kit. FIG. 14. Schematic of a streptavidin conjugation with a conjugated polymer and the resulting conjugate structure (top) and Coomassie stained agarose gel representative of the streptavidin-attached CP (below). FIG. 15. Representative acrylamide gel depiction of biotinylated polymer alone or bound to Cy5-labeled streptavidin. FIG. 16. Schematic of streptavidin-attached conjugated polymer of FIG. 14 binding to biotinylated microspheres (top) and plot of fluorescence excitation of control biotinylated microspheres and microspheres bound to streptavidin conjugated polymer. FIG. 17. Schematic of streptavidin-attached conjugated polymer of FIG. 14 selectively bound to biotinylated microspheres and energy transfer to dye acceptors on co-localized streptavidin-dye conjugates (top) and plot of energy transfer from streptavidin-attached conjugated polymer to dye acceptor (bottom). FIG. 18. Schematic of biotinylated polymer of FIG. 14 binding to streptavidin coated microspheres (top) and plot of fluorescence excitation of control streptavidin coated microspheres and microspheres bound to biotinylated polymer. FIG. 19. Schematic of biotinylated polymer of FIG. 14 binding to dye-labeled streptavidin conjugates and FRET (top); plot of energy transfer from biotinylated polymer to two different dye acceptors (bottom left) and titration plot of polymer saturation (bottom right). FIG. 20. Flow cytometry analysis of CD4 marking of Cyto-trol cells with 440 nm polymer-streptavidin-conjugates. FIG. 21. (A) Polymer structure of Example 38b conjugated to (from left to right) FITC, Cy3, DyLight 594 and DyLight633; (B) Comparison of the fluorescence of the dye (DyLight594) excited near its absorbance maximum (lower curve) and polymer-dye conjugate excited at 405 nm (upper curve); (C) Comparison of the fluorescent signal of the base polymer (no dye, peak emission near 420 nm) to that of the polymer-dye conjugate (peak emission near 620 nm). FIG. 22. Plot of flow testing of monoclonal antibody (antiCD4) conjugates on whole lysed blood samples. FIG. 23. Plot of florescence of a dye (DyLight594) and a polymer-dye conjugate by excitation of dye at 594 nm and the polymer-dye conjugate at 380 nm. FIG. 24. Plot of fluorescent immunoassay (ELISA) with streptavidin-attached conjugated polymer. FIG. 25. Plot of fluorescent intensity vs. temperature of a DNA oligomer-polymer conjugate hybridized to a target. FIG. 26. Ion exchange chromatogram for a polymer antibody conjugate to remove free polymer (left) and an SEC chromatogram showing the separation of final conjugate from free antibody. In both chromatograms absorbance was monitored at 280 nm (lower curves) and 407 nm (upper curves). FIG. 27. Sandwich immunoassay on Luminex assay (left) and corresponding results on the Luminex system using 532 nm excitation of both the conjugated polymer and PE streptavidin detection conjugates. FIG. 28. Data on left show results obtained with compensation beads while the data set on the right results from a 4 color assay on human blood samples. FIGS. 29. (A) and (B) Schematic of covalent linkage of conjugated polymer to 2° antibody. FIG. 30. Schematic of conjugated polymers in Fluorescent Immuno Assay (FIA). (A) conjugated polymer covalently linked to a detection antibody; (B) biotin binding protein covalently bound to the conjugated polymer and interacting with a biotinylated detection antibody; (C) secondary antibody covalently linked to the conjugated polymer and interacting with a detection antibody. FIG. 31. (A) Schematic of nucleic acid probe sequences labeled with a quencher molecule conjugated to a conjugated polymer; (B) nucleic acid probe sequences labeled with a quencher molecule conjugated to a conjugated polymer-dye tandem complex. FIG. 32. Schematic of modifications of the HybProbe detection technique. (A) conjugated polymer covalently linked to the donor probe and resulting energy transfer to acceptor probe; (B) “Signal off” modification of the HybProbe approach where the conjugated polymer is quenched by an acceptor probe. FIG. 33. Comparison of non-specific binding in various polymers (top) in a Jurkat cell (lymphocyte cell line) model; (bottom) plot ranking the polymers in terms of signal generated purely by non-specific binding (NSB). FIG. 34. Histograms collected from flow cytometry analysis (405 nm excitation in a BD LSR-II cytometer) using a Jurkat cell line; (left) unstained cells and a negative control, anionic P4 polymer; (middle) range of different polymer and polymer side chain combinations tested on the same cells; (right) neutral polymer P20 showed almost no off set from the untreated cells. FIG. 35. Gel electrophoresis depicting relative mobility of avidin as a function of the degree of conjugation with polymer AA1. FIG. 36. Fractionation of crude polymer-avidin conjugate mixtures on a Superdex 200 size exclusion column; (top) monitoring fractions by UV absorbance; (bottom) gel electrophoresis of selected fractions to visualize the degree to which avidin was attached to polymer. FIG. 37. Gel electrophoresis of conjugation reactions performed with polymer in varying molar excess to streptavidin; (left) UV illumination; (right) 532 nm excitation. FIG. 38. Plot depicting purification of polymer streptavidin conjugates with polymers exemplified in Example 9, denoted P30, (top) crude samples; (bottom) purified conjugates). DETAILED DESCRIPTION OF THE INVENTION Before the present invention is described in further detail, it is to be understood that this invention is not limited to the particular methodology, devices, solutions or apparatuses described, as such methods, devices, solutions or apparatuses can, of course, vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the present invention. Use of the singular forms “a,” “an,” and “the” include plural references unless the context clearly dictates otherwise. Thus, for example, reference to “an aggregation sensor” includes a plurality of aggregation sensors, reference to “a probe” includes a plurality of probes, and the like. Additionally, use of specific plural references, such as “two,” “three,” etc., read on larger numbers of the same subject less the context clearly dictates otherwise. Terms such as “connected,” “attached,” “conjugated” and “linked” are used interchangeably herein and encompass direct as well as indirect connection, attachment, linkage or conjugation unless the context clearly dictates otherwise; in one example, the phrase “conjugated polymer” is used in accordance with its ordinary meaning in the art and refers to a polymer containing an extended series of unsaturated bonds, and that context dictates that the term “conjugated” should be interpreted as something more than simply a direct or indirect connection, attachment or linkage. Where a range of values is recited, it is to be understood that each intervening integer value, and each fraction thereof, between the recited upper and lower limits of that range is also specifically disclosed, along with each subrange between such values. The upper and lower limits of any range can independently be included in or excluded from the range, and each range where either, neither or both limits are included is also encompassed within the invention. Where a value being discussed has inherent limits, for example where a component can be present at a concentration of from 0 to 100%, or where the pH of an aqueous solution can range from 1 to 14, those inherent limits are specifically disclosed. Where a value is explicitly recited, it is to be understood that values which are about the same quantity or amount as the recited value are also within the scope of the invention, as are ranges based thereon. Where a combination is disclosed, each subcombination of the elements of that combination is also specifically disclosed and is within the scope of the invention. Conversely, where different elements or groups of elements are disclosed, combinations thereof are also disclosed. Where any element of an invention is disclosed as having a plurality of alternatives, examples of that invention in which each alternative is excluded singly or in any combination with the other alternatives are also hereby disclosed; more than one element of an invention can have such exclusions, and all combinations of elements having such exclusions are hereby disclosed. Unless defined otherwise or the context clearly dictates otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the invention, the preferred methods and materials are now described. All publications mentioned herein are hereby incorporated by reference for the purpose of disclosing and describing the particular materials and methodologies for which the reference was cited. The publications discussed herein are provided solely for their disclosure prior to the filing date of the present application. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention. Definitions In describing the present invention, the following terms will be employed, and are intended to be defined as indicated below. “Alkyl” refers to a branched, unbranched or cyclic saturated hydrocarbon group of 1 to 24 carbon atoms optionally substituted at one or more positions, and includes polycyclic compounds. Examples of alkyl groups include optionally substituted methyl, ethyl, n-propyl, isopropyl, n-butyl, s-butyl, t-butyl, n-pentyl, isopentyl, neopentyl, n-hexyl, n-heptyl, n-octyl, n-decyl, hexyloctyl, tetradecyl, hexadecyl, eicosyl, tetracosyl and the like, as well as cycloalkyl groups such as cyclopropyl, cyclobutyl, cyclopentyl, cyclohexyl, cycloheptyl, cyclooctyl, adamantyl, and norbornyl. The term “lower alkyl” refers to an alkyl group of 1 to 6 carbon atoms, preferably 1 to 4 carbon atoms. Exemplary substituents on substituted alkyl groups include hydroxyl, cyano, alkoxy, ═O, ═S, —NO2, halogen, haloalkyl, heteroalkyl, carboxyalkyl, amine, amide, thioether and —SH. “Alkoxy” refers to an “—Oalkyl” group, where alkyl is as defined above. A “lower alkoxy” group intends an alkoxy group containing one to six, more preferably one to four, carbon atoms. “Alkenyl” refers to a branched, unbranched or cyclic hydrocarbon group of 2 to 24 carbon atoms containing at least one carbon-carbon double bond optionally substituted at one or more positions. Examples of alkenyl groups include ethenyl, 1-propenyl, 2-propenyl (allyl), 1-methylvinyl, cyclopropenyl, 1-butenyl, 2-butenyl, isobutenyl, 1,4-butadienyl, cyclobutenyl, 1-methylbut-2-enyl, 2-methylbut-2-en-4-yl, prenyl, pent-1-enyl, pent-3-enyl, 1,1-dimethylallyl, cyclopentenyl, hex-2-enyl, 1-methyl-1-ethylallyl, cyclohexenyl, heptenyl, cycloheptenyl, octenyl, cyclooctenyl, decenyl, tetradecenyl, hexadecenyl, eicosenyl, tetracosenyl and the like. Preferred alkenyl groups herein contain 2 to 12 carbon atoms. The term “lower alkenyl” intends an alkenyl group of 2 to 6 carbon atoms, preferably 2 to 4 carbon atoms. The term “cycloalkenyl” intends a cyclic alkenyl group of 3 to 8, preferably 5 or 6, carbon atoms. Exemplary substituents on substituted alkenyl groups include hydroxyl, cyano, alkoxy, ═O, ═S, —NO2, halogen, haloalkyl, heteroalkyl, amine, thioether and —SH. “Alkenyloxy” refers to an “—Oalkenyl” group, wherein alkenyl is as defined above. “Alkylaryl” refers to an alkyl group that is covalently joined to an aryl group. Preferably, the alkyl is a lower alkyl. Exemplary alkylaryl groups include benzyl, phenethyl, phenopropyl, 1-benzylethyl, phenobutyl, 2-benzylpropyl and the like. “Alkylaryloxy” refers to an “—Oalkylaryl” group, where alkylaryl is as defined above. “Alkynyl” refers to a branched or unbranched hydrocarbon group of 2 to 24 carbon atoms containing at least one —C “Amide” refers to —C(O)NR′R″, where R′ and R″ are independently selected from hydrogen, alkyl, aryl, and alkylaryl. “Amine” refers to an —N(R′)R″ group, where R′ and R″ are independently selected from hydrogen, alkyl, aryl, and alkylaryl. “Aryl” refers to an aromatic group that has at least one ring having a conjugated pi electron system and includes carbocyclic, heterocyclic, bridged and/or polycyclic aryl groups, and can be optionally substituted at one or more positions. Typical aryl groups contain 1 to 5 aromatic rings, which may be fused and/or linked. Exemplary aryl groups include phenyl, furanyl, azolyl, thiofuranyl, pyridyl, pyrimidyl, pyrazinyl, triazinyl, biphenyl, indenyl, benzofuranyl, indolyl, naphthyl, quinolinyl, isoquinolinyl, quinazolinyl, pyridopyridinyl, pyrrolopyridinyl, purinyl, tetralinyl and the like. Exemplary substituents on optionally substituted aryl groups include alkyl, alkoxy, alkyl carboxy, alkenyl, alkenyloxy, alkenylcarboxy, aryl, aryloxy, alkylaryl, alkylaryloxy, fused saturated or unsaturated optionally substituted rings, halogen, haloalkyl, heteroalkyl, —S(O)R, sulfonyl, —SO3R, —SR, —NO2, —NRR′, —OH, —CN, —C(O)R, —OC(O)R, —NHC(O)R, —(CH2)nCO2R or —(CH2)nCONRR′ where n is 0-4, and wherein R and R′ are independently H, alkyl, aryl or alkylaryl. “Aryloxy” refers to an “—Oaryl” group, where aryl is as defined above. “Carbocyclic” refers to an optionally substituted compound containing at least one ring and wherein all ring atoms are carbon, and can be saturated or unsaturated. “Carbocyclic aryl” refers to an optionally substituted aryl group wherein the ring atoms are carbon. “Halo” or “halogen” refers to fluoro, chloro, bromo or iodo. “Halide” refers to the anionic form of the halogens. “Haloalkyl” refers to an alkyl group substituted at one or more positions with a halogen, and includes alkyl groups substituted with only one type of halogen atom as well as alkyl groups substituted with a mixture of different types of halogen atoms. Exemplary haloalkyl groups include trihalomethyl groups, for example trifluoromemyl. “Heteroalkyl” refers to an alkyl group wherein one or more carbon atoms and associated hydrogen atom(s) are replaced by an optionally substituted heteroatom, and includes alkyl groups substituted with only one type of heteroatom as well as alkyl groups substituted with a mixture of different types of heteroatoms. Heteroatoms include oxygen, sulfur, and nitrogen. As used herein, nitrogen heteroatoms and sulfur heteroatoms include any oxidized form of nitrogen and sulfur, and any form of nitrogen having four covalent bonds including protonated forms. An optionally substituted heteroatom refers to replacement of one or more hydrogens attached to a nitrogen atom with alkyl, aryl, alkylaryl or hydroxyl. “Heterocyclic” refers to a compound containing at least one saturated or unsaturated ring having at least one heteroatom and optionally substituted at one or more positions. Typical heterocyclic groups contain 1 to 5 rings, which may be fused and/or linked, where the rings each contain five or six atoms. Examples of heterocyclic groups include piperidinyl, morpholinyl and pyrrolidinyl. Exemplary substituents for optionally substituted heterocyclic groups are as for alkyl and aryl at ring carbons and as for heteroalkyl at heteroatoms. “Heterocyclic aryl” refers to an aryl group having at least 1 heteroatom in at least one aromatic ring. Exemplary heterocyclic aryl groups include furanyl, thienyl, pyridyl, pyridazinyl, pyrrolyl, N-lower alkyl-pyrrolo, pyrimidyl, pyrazinyl, triazinyl, tetrazinyl, triazolyl, tetrazolyl, imidazolyl, bipyridyl, tripyridyl, tetrapyridyl, phenazinyl, phenanthrolinyl, purinyl, perylene, perylene diimide, diketopyrrolopyrrole, benzothiodiazol, benzoxadiazol, thienopyrazine and the like. “Hydrocarbyl” refers to hydrocarbyl substituents containing 1 to about 20 carbon atoms, including branched, unbranched and cyclic species as well as saturated and unsaturated species, for example alkyl groups, alkylidenyl groups, alkenyl groups, alkylaryl groups, aryl groups, and the like. The term “lower hydrocarbyl” intends a hydrocarbyl group of one to six carbon atoms, preferably one to four carbon atoms. A “substituent” refers to a group that replaces one or more hydrogens attached to a carbon or nitrogen. Exemplary substituents include alkyl, alkylidenyl, alkylcarboxy, alkoxy, alkenyl, alkenylcarboxy, alkenyloxy, aryl, aryloxy, alkylaryl, alkylaryloxy, —OH, amide, carboxamide, carboxy, sulfonyl, ═O, ═S, —NO2, halogen, haloalkyl, fused saturated or unsaturated optionally substituted rings, —S(O)R, —SO3R, —SR, —NRR′, —OH, —CN, —C(O)R, —OC(O)R, —NHC(O)R, —(CH2)nCO2R or —(CH2)nCONRR′ where n is 0-4, and wherein R and R′ are independently H, alkyl, aryl or alkylaryl. Substituents also include replacement of a carbon atom and one or more associated hydrogen atoms with an optionally substituted heteroatom. “Sulfonyl” refers to —S(O)2R, where R is alkyl, aryl, —C(CN)═C-aryl, —CH2CN, alkylaryl, or amine. “Thioamide” refers to —C(S)NR′R″, where R′ and R″ are independently selected from hydrogen, alkyl, aryl, and alkylaryl. “Thioether” refers to —SR, where R is alkyl, aryl, or alkylaryl. As used herein, the term “binding pair” refers to first and second molecules that bind specifically to each other with greater affinity than to other components in the sample. The binding between the members of the binding pair is typically noncovalent. Exemplary binding pairs include immunological binding pairs (e.g. any haptenic or antigenic compound in combination with a corresponding antibody or binding portion or fragment thereof, for example digoxigenin and anti-digoxigenin, fluorescein and anti-fluorescein, dinitrophenol and anti-dinitrophenol, bromodeoxyuridine and anti-bromodeoxyuridine, mouse immunoglobulin and goat anti-mouse immunoglobulin) and nonimmunological binding pairs (e.g., biotin-avidin, biotin-streptavidin, hormone [e.g., thyroxine and cortisol]-hormone binding protein, receptor-receptor agonist or antagonist (e.g., acetylcholine receptor-acetylcholine or an analog thereof) IgG-protein A, lectin-carbohydrate, enzyme-enzyme cofactor, enzyme-enzyme-inhibitor, and complementary polynucleotide pairs capable of forming nucleic acid duplexes) and the like. One or both member of the binding pair can be conjugated to additional molecules. The terms “polynucleotide,” “oligonucleotide,” “nucleic acid” and “nucleic acid molecule” are used interchangeably herein to refer to a polymeric form of nucleotides of any length, and may comprise ribonucleotides, deoxyribonucleotides, analogs thereof, or mixtures thereof. These terms refer only to the primary structure of the molecule. Thus, the terms includes triple-, double- and single-stranded deoxyribonucleic acid (“DNA”), as well as triple-, double- and single-stranded ribonucleic acid (“RNA”). It also includes modified, for example by alkylation, and/or by capping, and unmodified forms of the polynucleotide. Additional details for these terms as well as for details of base pair formation can be found in U.S. application Ser. No. 11/344,942, filed Jan. 31, 2006, which is incorporate herein by reference in its entirety. “Complementary” or “substantially complementary” refers to the ability to hybridize or base pair between nucleotides or nucleic acids, such as, for instance, between a sensor peptide nucleic acid and a target polynucleotide. Complementary nucleotides are, generally, A and T (or A and U), or C and G. Two single-stranded polynucleotides or PNAs are said to be substantially complementary when the bases of one strand, optimally aligned and compared and with appropriate insertions or deletions, pair with at least about 80% of the bases of the other strand, usually at least about 90% to 95%, and more preferably from about 98 to 100%. Alternatively, substantial complementarity exists when a polynucleotide or PNA will hybridize under selective hybridization conditions to its complement. Typically, selective hybridization will occur when there is at least about 65% complementary over a stretch of at least 14 to 25 bases, preferably at least about 75%, more preferably at least about 90% complementary. See, M. Kanehisa Nucleic Acids Res. 12:203(1984). “Preferential binding” or “preferential hybridization” refers to the increased propensity of one polynucleotide or PNA to bind to its complement in a sample as compared to a noncomplementary polymer in the sample. Hybridization conditions for polynucleotides will typically include salt concentrations of less than about 1M, more usually less than about 500 mM and preferably less than about 200 mM. In the case of hybridization between a peptide nucleic acid and a polynucleotide, the hybridization can be done in solutions containing little or no salt. Hybridization temperatures can be as low as 5° C., but are typically greater than 22° C., more typically greater than about 30° C., and preferably in excess of about 37° C. Longer fragments may require higher hybridization temperatures for specific hybridization. Other factors may affect the stringency of hybridization, including base composition and length of the complementary strands, presence of organic solvents and extent of base mismatching, and the combination of parameters used is more important than the absolute measure of any one alone. Other hybridization conditions which may be controlled include buffer type and concentration, solution pH, presence and concentration of blocking reagents to decrease background binding such as repeat sequences or blocking protein solutions, detergent type(s) and concentrations, molecules such as polymers which increase the relative concentration of the polynucleotides, metal ion(s) and their concentration(s), chelator(s) and their concentrations, and other conditions known in the art. “Multiplexing” herein refers to an assay or other analytical method in which multiple analytes can be assayed simultaneously. “Having” is an open ended phrase like “comprising” and “including,” and includes circumstances where additional elements are included and circumstances where they are not. “Optional” or “optionally” means that the subsequently described event or circumstance may or may not occur, and that the description includes instances where the event or circumstance occurs and instances in which it does not. The embodiments disclosed herein relate generally to compositions of conjugated polymer materials that contain active functional groups for conjugation (or attachment) to other molecules, substrates or the like. Certain embodiments describe methods and compositions that provide for specific control of the incorporation and subsequent conjugation of such functional sites. Linkers can be incorporated at one or both ends of a conjugated polymer chain or internally controlled by ratio of monomers used in the polymerizations. Such linkers can be the same or different to allow for more than one distinct entity to be attached to the conjugated polymer structure. Further embodiments describe conjugated polymer compositions that not only provide for active conjugation sites but also are solublized through the use of non-ionic side chains (no formal charges). Such embodiments exhibit exceptional water solubility and provide minimal interactions with biological molecules and other common biological assay components. The embodiments disclosed herein further relate generally to assays and complexes including conjugated polymers useful for the identification of target biomolecules or biomolecules associated with target molecules through enhanced signal afforded by their unique properties. In certain general embodiments the conjugated polymer serves directly as the optical reporter bound to a biomolecule, substrate or other assay component. The conjugated polymers act as extended light harvesting structures that when excited can absorb more energy than conventional organic dyes. The polymer then re-emits the light which can be detected or measured. The signals generated from such conjugated polymer complexes can be significantly greater than those obtained from other fluorescent reporters. In other embodiments one aspect includes energy transfer from conjugated polymers to dyes bound to the polymer or to a sensor which can be a biomolecule including a bioconjugate (e.g., an antibody, a streptavidin or nucleic acid sequence). In such embodiments it is common to observe amplified dye signal (relative to direct dye excitation) as a result of the conjugated polymer excitation and subsequent energy transfer. Further it is possible to use a range of dyes with varying energy to create a basis for a multicolor or multiplex detection format. In certain embodiments the neutral conjugated polymers are bound to antibodies for the identification of specific cell markers and cell types in flow cytometry and cell sorting assays. In other embodiments the conjugated polymers are further bound to a secondary dye reporter. In further embodiments the polymer and polymer-dye structures are bound to monoclonal antibodies. In other embodiments the neutral conjugated polymers are bound to antibodies for use in various sandwich immunoassays. In one embodiment, an approach modifying a format as followed in relation to nucleic acid sensor assays as described in Gaylord, Heeger, and Bazan, J. Am. Chem. Soc., 2003 can be followed. Specifically, signal amplification of conjugated polymers can be based on binding events to indicate a hybridization event. Any established conjugated polymers can be chosen as the donor, and one or more dye, preferably a dye with a history of efficient energy transfer, for example, fluorescein and Cy3, can be chosen as the acceptors. It is envisioned that the dye can be directly conjugated to a sensor molecule. As shown schematically in FIG. 1, the sensor can be a biomolecule (e.g., an antibody) in a solution or on a substrate, to which conjugated polymers can be added. In the embodiment shown in FIG. 1, a dye can be covalently linked (bioconjugated) to an antibody (Y-shaped structure), which possesses a net negative charge. Addition of conjugated polymers (shown as wavy lines) can result in interaction or binding between the conjugated polymer and the antibody, bringing the conjugated polymers and dye into close proximity. Interaction or binding can be achieved by any known method including, but not limited to, avidin/biotin labeling. Distance requirements for fluorescence resonance energy transfer (FRET) can thus be met, and excitation of the polymer with light (shown as hν) results in amplified dye emission. It is envisioned that the conjugated polymers can be excited at a wavelength where the dye does not have significant absorbance. In one embodiment the dye emission can be at a longer wavelength than the conjugated polymer emission. In use it is envisioned that an assay method can include the steps of providing a sample that is suspected of containing a target biomolecule, providing a sensor conjugated to a signaling chromophore and capable of interacting with the target biomolecule, providing a conjugated polymer that interacts with the sensor and upon excitation is capable of transferring energy to the sensor signaling chromophore and contacting the sample with the sensor and the conjugated polymer in a solution under conditions in which the sensor can bind to the target biomolecule if present. Next, the method can include applying a light source to the sample that can excite the conjugated polymer, and detecting whether light is emitted from the signaling chromophore. As disclosed herein, interaction or binding between conjugated polymers and dye-labeled antibodies can be a viable approach for increasing detection sensitivities, for example of a biomolecule target. In a further embodiment, covalently attaching the conjugated polymers to a dye, biomolecule (e.g., an antibody complex) or both offers several advantages including reduced background and/or improved energy transfer. In the case of direct linkage to a biomolecule, biorecognition events, rather than non-specific polymer interaction or binding events (such as those described above in FIG. 1), should govern conjugated polymer presence. In this manner, nonspecific binding of conjugated polymers to biomolecules can be eliminated, reducing any background emission resulting from the conjugated polymer itself. The abovementioned biomolecules include but are not limited to proteins, peptides, affinity ligands, antibodies, antibody fragments, sugars, lipids, enzymes and nucleic acids (as hybridization probes and/or aptamers). In general, in another aspect the invention includes the bioconjugation of polymers to affinity ligands (affinity ligands describing a biomolecule that has an affinity for another biomolecule). FIG. 2 illustrates a class of materials in which a conjugated polymer (shown as a wavy line) is linked to a dye, biomolecule, or biomolecule/dye complex (labeled X). Linking to the conjugated polymer can be via a first functionality linker A on the conjugated polymer that serves as a bioconjugation site capable of covalently linking with a second functionality linker A′ linked to a biomolecule and/or dye (see X). This arrangement can fix the distance between the conjugated polymer and X, thereby ensuring only specific interactions between polymer and X. It is envisioned that a biomolecule component X in this embodiment can be any of the various biomolecules disclosed herein, including but not limited to an antibody, protein, affinity ligand, enzyme or nucleic acid. Linker A can be anywhere on the conjugated polymer including terminal positions of the polymer, internally on a repeating subunit, in between repeating subunits or any combination thereof. Likewise, Linker A′ can be linked anywhere on a biomolecule and/or dye. The linking chemistry for A-A′ can include, but is not limited to, maleimide/thiol; thiol/thiol; pyridyldithiol/thiol; succinimidyl iodoacetate/thiol; N-succinimidylester (NHS ester), sulfodicholorphenol ester (SDP ester), or pentafluorophenyl-ester (PFP ester)/amine; bissuccinimidylester/amine; imidoesters/amines; hydrazine or amine/aldehyde, dialdehyde or benzaldehyde; isocyanate/hydroxyl or amine; carbohydrate-periodate/hydrazine or amine; diazirine/aryl azide chemistry; pyridyldithiol/aryl azide chemistry; alkyne/azide; carboxy-carbodiimide/amine; amine/Sulfo-SMCC (Sulfosuccinimidyl 4-[N-maleimidomethyl]cyclohexane-1-carboxylate)/thiol; and amine/BMPH (N-[β-Maleimidopropionic acid]hydrazide.TFA)/thiol. It is envisioned that the X in this context can be, but is not limited to, a dye, fluorescence protein, nanomaterial (e.g., Quantum Dot), chemluminescence-generating molecule, a conjugate between dye and chemluminescence-generating molecule, a conjugate between fluorescence protein and chemluminescence-generating molecule, a conjugate between nanomaterial (e.g., Quantum Dot) and chemluminescence-generating molecule, streptavidin, avidin, enzyme, substrate for an enzyme, substrate analog for an enzyme, receptor, ligand for a receptor, ligand analog for a receptor, DNA, RNA, modified nucleic acid, DNA aptamer, RNA aptamer, modified nucleic aptamer, peptide aptamer, antibody, antigen, phage, bacterium or conjugate of any two of the items described above. In another aspect, the invention includes the use of conjugated polymers as direct labels. FIG. 3 shows examples of labeled conjugated polymers. In one embodiment, FIG. 3A, a polymer (shown as encircled hexagons) is shown conjugated to an antibody which can be, for example, a 1° or 2° antibody. The conjugate of the polymer and the antibody can be used as a direct reporter, for example, in an assay. In additional embodiments, the signal from the polymer is not modulated by other assay components rather it is dependent on its presence in the assay at the time of detection as a function of specific biomolecule recognition. Excitation of the polymer with light (not shown) can result in polymer emission, indicating the presence of the antibody (1° or 2°) in the assay or assay solution. FIGS. 3B and 3C further exemplify the use of conjugated polymers as biomolecule labels capable of detecting specific targets and target associated biomolecules. FIG. 3B depicts a polymer avidin (streptavidin, neutraAvidin, etc.) conjugate capable of binding to biotin modified molecules, biomolecules or substrates. FIG. 3C depicts a nucleic acid (DNA, RNA, PNA, etc.) conjugate capable of hybridizing to complementary nucleic acid sequences. Linkage or conjugation of fluorescent conjugated polymer to a molecule capable of recognizing a target biomolecule or target associated molecule (such as those exemplified in FIG. 3) provides a direct means of detection. In additional embodiments, the signals generated from excitation of the conjugated polymer are not modulated by other assay components except those which are directly conjugated to the polymer. In such embodiments the polymer complex is acting directly as a fluorescent label. In another embodiment shown in FIG. 3D, the conjugated polymer is labeled with a dye, for example, a chromophore. In this case, the conjugated polymer can act as a donor and the dye can act as an acceptor in an energy transfer process. Here, the conjugated polymer can act as a light harvester, and excitation of the conjugated polymer is followed by the channeling of the excitations to the dye via an energy transfer process including, but not limited to, FRET. This results in amplified dye emission (as compared to direct excitation of the dye). The fluorescence of the donor conjugated polymer, in one embodiment, can be quenched (e.g., >90% quenching). This is exemplified in Example 38 and shown in FIG. 21, by way of example only. In some instances, the conjugated polymer in FIG. 3D (and similar drawings disclosed herein) can have multiple dye attachments which can be positioned internally or at the terminus of the polymer structure (single dye shown for illustrative purposes only). In the case of direct linkage to a dye (FIG. 3D) or biomolecule/dye complex (as exemplified in FIG. 4), donor-acceptor distances can be fixed, rather than dependent on the strength of interaction or binding, and energy transfer efficiency can be significantly increased. This has significant consequences in the context of improving dye signaling (or quenching) and reducing background fluorescence associated with donor-acceptor cross-talk. Cross-talk in this case refers to the overlap between conjugated polymer (donor) and dye (acceptor) emission peaks. Conjugated polymers which bind non-specifically at distances too great for energy transfer can contribute to the background fluorescence (or crosstalk). Shorter (fixed) distances between the donor and acceptor can not only facilitate direct dye amplification, but also can greatly quench the donor emission, as depicted in FIG. 21 by way of example only. This results in less donor emission at the acceptor emission wavelengths, which subsequently reduces or even eliminates the need for cross-talk correction. In further embodiments the localization of the conjugated polymer and a signaling chromophore are brought together by recognition event, for example by the binding of two affinity pairs or by co-recognition of the same target molecule or target associated molecule (FIG. 5). Such embodiments could be performed in solution based formats or in such configurations where one or more of elements is bound to another biomolecule (cell, tissue, protein, nucleic acid, etc.) or a substrate (bead, well plate, surface, tube, etc.). In general, another aspect the invention includes a method of assaying for a target biomolecule or target associated biomolecule. As shown in FIG. 5A, in one embodiment a conjugated polymer (shown as a wavy line) can be linked to a first bioconjugate (shown as a Y-shaped object), for example, a 2° antibody that is specific for second a dye-labeled bioconjugate, for example, a 1° antibody. Here, the recognition event between the 1° and 2° antibody will result in the reduction of distance between the donor conjugated polymer and acceptor dye. In a similar embodiment depicted in FIG. 5B, polymer and dye labeled antibodies recognize a common target. After either of these recognition events, excitation of the donor conjugated polymer with light (shown as hν) will result in energy transfer, e.g., FRET, to the acceptor dye (shown as curved arrow), and amplified dye emission (in comparison with direct excitation of the dye) will be observed. In use it is envisioned that an assay method could include providing a sample that is suspected of containing a target biomolecule by the steps of providing a first bioconjugate, for example, a 1° antibody conjugated to a signaling chromophore and capable of interacting with the target biomolecule. This is followed by providing a second bioconjugate, for example, a 2° antibody or 1° antibody, conjugated to a polymer, wherein the second bioconjugate can bind to the first bioconjugate or target and wherein upon such binding excitation of the conjugated polymer is capable of transferring energy to the signaling chromophore. Next, the method includes contacting the sample with the first bioconjugate in a solution under conditions in which the first bioconjugate can bind to the target biomolecule if present and contacting the solution with the second bioconjugate. The method then includes applying a light source to the target biomolecule or tagged target biomolecule, wherein the light source can excite the conjugated polymer and subsequently detecting whether light is emitted from the signaling chromophore. In another aspect, the invention includes a method of assaying a sample using a conjugated polymer and a sensor biomolecule complex. As shown in FIGS. 5C and D, a polymer (shown as a wavy line) can be conjugated to a first bioconjugate, for example, streptavidin (SA) which has a strong affinity for biotin. In FIG. 5C, a sensor biomolecule (e.g., an antibody which can be a 1° or 2° antibody), is conjugated to both a dye and a second bioconjugate (e.g., a biotin moiety). Similar embodiments are depicted in FIG. 5D where the second bioconjugate (e.g., a biotin moiety) and the signaling chromopohre are both conjugated to a nucleic acid. After a biorecognition event between the first and second bioconjugates (e.g. between SA and biotin), the conjugated polymer and dye will be brought into close proximity, and excitation of the donor conjugated polymer will result in energy transfer to the acceptor dye. Dye emission will indicate the presence of the first bioconjugate (e.g., the antibody or nucleic acid). In comparison with direct excitation of the dye, amplification of the dye signal intensity will be observed when excited indirectly through an energy transfer process, e.g., FRET. A method of using the embodiment shown in FIGS. 5C and D can include the steps of providing a sample that is suspected of containing a target biomolecule, providing a conjugated polymer comprising a covalently linked first bioconjugate (e.g., SA), providing a sensor biomolecule complex comprising a sensor biomolecule capable of interacting with the target molecule, a signaling chromophore, and covalently linked second bioconjugate capable of binding with the first bioconjugate, wherein upon such binding excitation of the conjugated polymer is capable of transferring energy to the signaling chromophore. The method can further include the steps of contacting the sample with the sensor biomolecule complex in a solution under conditions in which the sensor biomolecule can bind to the target biomolecule if present, contacting the solution with the conjugated polymer, applying a light source to the sample that can excite the conjugated polymer, and detecting whether light is emitted from the signaling chromophore. Further the conjugated polymer can contain additional linking site suitable for conjugation or attachment to more than one species. FIG. 6 exemplifies the addition of a second linking site within the polymer. Such linkers A and B can be the same or different to allow for orthogonal conjugation of different species. The linkers can be anywhere on the polymer including terminal and internal positions. The linking chemistry for A-A′ and B-B′ (and optionally C-C′, D-D′, etc.) can include, but is not limited to, maleimide/thiol; thiol/thiol; pyridyldithiol/thiol; succinimidyl iodoacetate/thiol; N-succinimidylester (NHS ester), sulfodicholorphenol ester (SDP ester), or pentafluorophenyl-ester (PFP ester)/amine; bissuccinimidylester/amine; imidoesters/amines; hydrazine or amine/aldehyde, dialdehyde or benzaldehyde; isocyanate/hydroxyl or amine; carbohydrate-periodate/hydrazine or amine; diazirine/aryl azide chemistry; pyridyldithiol/aryl azide chemistry; alkyne/azide; carboxy-carbodiimide/amine; amine/Sulfo-SMCC (Sulfosuccinimidyl 4[N-maleimidomethyl]cyclohexane-1-carboxylate)/thiol; and amine/BMPH (N-[β-Maleimidopropionic acid]hydrazide.TFA)/thiol. A tri-functional linker such as the commercially available Sulfo-SBED Sulfosuccinimidyl[2-6-(biotinamido)-2-(p-azidobenzamido)-hexanoamido]-ethyl-1,3′-dithiopropionate can serve well in the three way linkage among X, Y, and conjugated polymer. In the embodiment illustrated in FIG. 6, X or Y can be, but are not limited to, a dye, fluorescence protein, nanomaterial (e.g., Quantum Dot), chemluminescence-generating molecule, a conjugate between dye and chemluminescence-generating molecule, a conjugate between fluorescence protein and chemluminescence-generating molecule, a conjugate between nanomaterial (e.g., Quantum Dot) and chemluminescence-generating molecule, streptavidin, avidin, enzyme, substrate for an enzyme, substrate analog for an enzyme, receptor, ligand for a receptor, ligand analog for a receptor, DNA, RNA, modified nucleic acid, DNA aptamer, RNA aptamer, modified nucleic aptamer, peptide aptamer, antibody, antigen, phage, bacterium or conjugate of any two of the items described above. In general, in another aspect the invention provides a conjugated polymer complex including a polymer, a sensor biomolecule and a signaling chromophore for identifying a target biomolecule. As shown in FIG. 6, in one embodiment a polymer (wavy line) can be bioconjugated to a dye X via linker functionalities A-A′ and a biomolecule Y via linker functionalities B-B′. As depicted in FIG. 7, in one embodiment a polymer can be bioconjugated to both a dye and a biomolecule, for example a biorecognition molecule. Useful biomolecules can include but are not limited to antibodies (FIG. 7A), avidin derivatives (FIG. 7B) affinity ligands, nucleic acids (FIG. 7C), proteins, nanoparticles or substrates for enzymes. The benefits of covalently linking a dye in proximity to a polymer have been described above. By affixing both an acceptor dye and a biorecognition molecule to a polymer, the benefits are two fold, by both fixing donor-acceptor distances, such that an acceptor is guaranteed to be within the vicinity of a donor conjugated polymer (and vice versa), and also increasing the specificity of polymer binding to indicate a biorecognition event. These covalent complexes can be made via the monomer, polymer and linking chemistries described herein. In use, the embodiments shown in FIG. 6 can be a conjugated polymer complex for identifying a target biomolecule wherein the complex includes a conjugated polymer, a signaling chromophore covalently linked to the conjugated polymer and a sensor biomolecule covalently linked to the conjugated polymer. The signaling chromophore of the complex is capable of receiving energy from the conjugated polymer upon excitation of the conjugated polymer and the sensor biomolecule is capable of interacting with the target biomolecule. It is envisioned that the biomolecules can include but are not limited to an antibody, protein, affinity ligand, peptide, or nucleic acid. In one embodiment shown in FIG. 7A, a polymer is conjugated to both a bioconjugate, for example, an antibody (1° or 2°) and a dye. Covalent linkage between the donor conjugated polymer and acceptor dye ensures close proximity. Excitation of the donor conjugated polymer results in energy transfer, e.g., FRET, to the acceptor dye. Where the bioconjugate is an antibody, if the antibody binds to its target (e.g., antigen), this will be indicated by dye emission upon donor polymer excitation. In an alternative embodiment, as shown in FIG. 7B, a polymer can be conjugated to both a SA and a dye. Again, covalent linkage between the donor conjugated polymer and acceptor dye ensure close proximity, and excitation of the donor conjugated polymer results in energy transfer to the acceptor dye. The SA complex can be used to label or detect a biotin-labeled biomolecule such as a biotinylated antibody or nucleic acid. Polymer excitation followed by energy transfer to the dye label will result in greatly enhanced detection signals (i.e., greater sensitivity). The example exemplified in FIG. 7A is a conjugated polymer labeled with a dye acceptor and further conjugated to an antibody. This Tandem configuration can be used in similar fashion as those described for the structure in FIG. 3A but are useful in generating a secondary signal for detection, often in multiplex formats. The conjugated polymer complexes in FIG. 7 can have multiple dye attachments which can be positioned internally or at the terminus of the polymer structure (single dye shown for illustrative purposes only). In other embodiments as shown in FIGS. 3A and 7A, a sensor biomolecule for example a 1° antibody (Y shape) is conjugated covalently linked to the conjugated polymer (encircled hexagons) or conjugated polymer-dye tandem complex (hexagons with pendant encircled star). Upon conjugated polymer excitation, emission from the conjugated polymer (FIG. 3A) or dye (FIG. 7A) will indicate presence of the biocomplex and by extension with appropriate assay design that of the target recognized by the sensor molecule allowing use as a reporter, for example in an assay. FIGS. 29A and 29B represent comparable examples with covalent linkage of the conjugated polymer to a 2° antibody. As an alternative embodiment, the conjugated polymer may be associated indirectly with the sensor biomolecule or target associated biomolecule. FIGS. 8C and 8D illustrate a sequence specific oligonucleotide probe (wavy line) covalently conjugated to a biotin moiety (drop shape). Here the conjugated polymer (encircled hexagons) or conjugated polymer-dye tandem complex (hexagons with pendant encircled star) is covalently bound or conjugated to a biotin recognizing protein (for example, avidin, streptavidin or similar with high specific affinity for the ligand biotin). FIGS. 8A and 8B illustrate comparable examples with a biotinylated antibody interacting with a covalent conjugate of the conjugated polymer (FIG. 8A) and conjugated polymer-dye tandem complex (FIG. 8B) to the biotin recognizing protein. Indirect association of the target associated biomolecule with the conjugated polymer is not limited to biotin mediated interactions. FIGS. 8E and F represent sequence specific oligonucleotides (wavy line) which have been covalently labeled with a digoxygenin moiety (7 pointed star). In turn the digoxygenin moiety has been recognized by a primary antibody covalently linked to the conjugated polymer (FIG. 8E) and the conjugated polymer-dye tandem complex (FIG. 8F). Although not shown pictorially, further embodiments employing indirect detection of digoxygenin using biotinylated antibodies and biotin recognizing proteins covalently linked to conjugated polymers (or conjugated polymer-dye tandem complexes) or unlabelled primary antibodies recognizing digoxygenin and appropriate secondary antibodies covalently linked to the conjugated polymer (or conjugated polymer-dye tandem complexes) are intended. A number of further embodiments are also predicated on energy transfer (for example but not limited to FRET) between the conjugated polymer and an acceptor dye. Given the potential for multiplexing analysis, it is envisioned that the conjugated polymer can be linked to a number of dyes or signaling chromophores, including, but not limited to, fluorescein, 6-FAM, rhodamine, Texas Red, California Red, iFluor594, tetramethylrhodamine, a carboxyrhodamine, carboxyrhodamine 6G, carboxyrhodol, carboxyrhodamine 110, Cascade Blue, Cascade Yellow, coumarin, Cy2®, Cy3®, Cy3.5®, Cy5®, Cy5.5®, Cy7®, Cy-Chrome, DyLight 350, DyLight 405, DyLight 488, DyLight 549, DyLight 594, DyLight 633, DyLight 649, DyLight 680, DyLight 750, DyLight 800, phycoerythrin, PerCP (peridinin chlorophyll-a Protein), PerCP-Cy5.5, JOE (6-carboxy-4′,5′-dichloro-2′,7′-dimethoxyfluorescein), NED, ROX (5-(and-6)-carboxy-X-rhodamine), HEX, Lucifer Yellow, Marina Blue, Oregon Green 488, Oregon Green 500, Oregon Green 514, Alexa Fluor® 350, Alexa Fluor® 430, Alexa Fluor® 488, Alexa Fluor® 532, Alexa Fluor® 546, Alexa Fluor® 568, Alexa Fluor® 594, Alexa Fluor® 633, Alexa Fluor® 647, Alexa Fluor® 660, Alexa Fluor® 680, 7-amino-4-methylcoumarin-3-acetic acid, BODIPY® FL, BODIPY® FL-Br2, BODIPY® 530/550, BODIPY® 558/568, BODIPY® 564/570, BODIPY® 576/589, BODIPY® 581/591, BODIPY® 630/650, BODIPY® 650/665, BODIPY® R6G, BODIPY® TMR, BODIPY® TR, conjugates thereof, and combinations thereof. These embodiments include modifications of the above examples where the acceptor dye serves as the assay reporter (as exemplified in FIGS. 3D, 4D, 7, 8B, 8D, 8E, 29B, wherein the encircled ten pointed star represents the dye). In certain embodiments the conjugated polymer conjugates provided in FIGS. 2-10, 29 and 30 are intended for but not limited to use in flow cytometry, cell sorting, molecular diagnostics, fluorescence in situ hybridization (FISH), immunohistochemistry (IHC), polymerase chain reaction, microscopy (fluorescent, confocal, 2 photon, etc.), blotting (e.g. northern, southern, western), cytomic bead arrays (Luminex formats, etc.), fluorescent immune assay (FIA or ELISA), nucleic acid sequencing and microarrays. Embodiments are also envisaged where conjugated polymers are used to enhance the detection and quantification of nucleic acids using sequence specific fluorescent probes combined with nucleic acid amplification techniques such as but not limited to polymerase chain reaction, transcription mediated amplification, rolling circle amplification, recombinase polymerase amplification, helicase dependent amplification and Linear-After-The-Exponential polymerase chain reaction. FIG. 32 represents modifications of the HybProbe detection technique. In FIG. 32A, the dye conventionally used as an energy transfer donor is replaced by the conjugated polymer (hexagon chain) which is covalently linked to the donor probe (wavy helical structure represented as right hand helical duplex due to association with nucleic acid target depicted a longer helical wavy line). Upon sequence specific hybridization the donor and acceptor (represented similarly to donor probe but on left hand side of nucleic acid target) probes are spatially juxtaposed on the target nucleic acid strand of interest in sufficiently close proximity to allow energy transfer to take place between the fluors. Excitation energy is transduced through the conjugated polymer and emitted as a readable signal by the dye (encircled ten pointed star) to allow nucleic acid quantification, detection and/or characterization. Presence of increased template allows increased numbers of probe co-hybridisation events and thus correlates to increased specific signal from the acceptor dye. In combination with the melt curve technique commonly employed in HybProbe experiments it is envisaged that sequence specific information corresponding to sequence variations will be collectable in appropriately designed experiments. FIG. 32B represents a “signal off” modification of the HybProbe approach where the conjugated polymer is quenched by an acceptor probe consisting of a small molecule fluorescence quencher (for example but not limited to Black Hole Quenchers™ Iowa Black® or Dabsyl). In another embodiment, conjugated polymer and conjugated polymer-dye tandem complexes similar to those described in FIGS. 4C and 4D are used in the detection, quantification and/or characterization of nucleic acid targets. Nucleic acid probe sequences labeled with a quencher molecule (black circle, for example but not limited to Black Hole Quenchers™, Iowa Black® or Dabsyl) are also conjugated to a conjugated polymer (FIGS. 4C and 31A) and a conjugated polymer-dye tandem complex (FIGS. 4D and 31B). In FIGS. 4C and D the recognition of the target sequence leads to a hybridization and separation of the quencher from the conjugated polymer or conjugated polymer-dye tandem complex and upon polymer excitation produces an increase in fluorescent signal. In FIGS. 31A and 31B the nucleic acid probe conjugate will hybridize to a complementary target sequence and by treatment with specific enzymes the probe sequence is cleaved or hydrolyzed freeing the conjugated polymer or conjugated conjugated polymer-dye tandem complex from the quencher and upon polymer excitation produces an increase in fluorescent signal. The most common example of the methods described in FIG. 31 is the use of DNA polymerase enzymes which contain nuclease activity (e.g. TaqMan PCR assays). FIG. 9 shows examples of conjugated polymer (hexagons) conjugated to secondary antibodies (FIG. 9A) and primary antibodies (FIG. 9B) (antibodies shown as Y-shaped structures). In an assay, an unlabeled 1° antibody can bind to an antigen, for example, a target protein (shown as a black triangle). Addition of the 2° antibody, which is conjugated to a polymer, can bind specifically to the 1° antibody. After washing to remove unbound 2° antibody and upon application of light of suitable excitation wavelength, observance of polymer emission is indicative of specific binding (FIG. 9A). In other assay embodiments, a polymer-labeled 1° antibody can directly bind a target protein, shown as a black triangle, and after washing to remove unbound 1° antibody and upon application of light of suitable excitation wavelength, observance of polymer emission is indicative of specific binding (FIG. 9B). Optionally, whether conjugated to the 1° or 2° antibody, the polymer may be further conjugated to a dye. In such a case, optical excitation of the conjugated polymer can result in energy transfer to the dye, and amplified dye emission, in comparison to direct dye excitation results. Observance of dye emission is indicative of specific binding. FIG. 10 shows an example of a sandwich-type complex of one embodiment of the invention. In the assay shown in FIG. 10A the conjugated polymer complex is composed of a polymer (shown as hexagons) that is bioconjugated a biomolecule, for example, streptavidin (X shape). After an unlabeled 1° antibody binds the target (e.g. protein), shown as a black triangle, a biotin-labeled 2° antibody binds specifically to the 1° antibody. In a separate step, addition of the conjugated polymer complex will result in specific binding between the biotin and streptavidin. Excitation of the conjugated polymer will result in polymer emission, indicating the presence of the target protein. Additionally in another embodiment, a biotin-labeled 1° antibody may be used to probe the target protein directly (FIG. 10B). After this binding event takes place, addition of a streptavidin-polymer complex will result in specific binding between the biotin and streptavidin, and excitation of the conjugated polymer will result in polymer emission, indicating the presence of the target protein. Optionally, the polymer may be further conjugated to a dye. In such a case, optical excitation of the polymer will result in amplified dye emission, as compared to direct excitation of the dye. Signals arising from dye emission will indicate the presence of the target protein. FIG. 30 depicts example embodiments around the use of conjugated polymers in Fluorescent Immuno Assay (FIA). In FIG. 30 panels A-C analyte antigen is immobilised on a surface which can include but is not limited to a microtitre plate well, bead particle, glass slide, plastic slide, lateral flow strip, laminar flow device, microfluidic device, virus, phage, tissue or cell surface. Analyte molecules are then detected by use of labelled detection conjugates or sensor biomolecules. In FIG. 30A, a conjugated polymer covalently linked to a detection antibody is utilized for detection. In FIG. 30B, a biotin binding protein (for example but not limited to avidin, streptavidin or other high affinity biotin specific derivatives) covalently bound to the conjugated polymer and interacting with a biotinylated detection antibody is utilized for detection. In FIG. 30C, a secondary antibody covalently linked to the conjugated polymer and interacting with a detection antibody is utilized for detection. In FIG. 5B, a homogenous, solution based example is also embodied where two separate antibodies each bind to the antigen of interest. One antibody is covalently linked to the conjugated polymer, the other to a dye. When bound to the antigen, the respective fluorophores are brought into sufficient spatial proximity for energy transfer to occur. In assays predicated on the designs in FIG. 30 and FIG. 5B, the sample is interrogated with light matched to the excitation of the conjugated polymer and signal reported at the emission wavelength of the dye. In the examples embodied in FIG. 30 A-C the use of a polymer-dye tandem complex is further disclosed. In such cases, optical excitation of the polymer will result in amplified dye emission, as compared to direct excitation of the dye. Signals arising from dye emission will indicate the presence of the target. In a further aspect, the invention provides for the multiplexing of donor energy transfer to multiple acceptors. By using a conjugated polymer as a donor in an energy transfer system, benefits also include the ability to multiplex. A single donor can transfer energy to several dyes; thus with a single excitation source, the intensity of multiple dyes can be monitored. This is useful for applications including but not limited to cell imaging (i.e. immunohistochemistry), flow cytometry and cell sorting, where the different types of cells can be monitored by protein-antibody recognition events. In one embodiment, two dye-labeled antibodies can be incubated with a biological material, for example, a cultured cell line, tissue section or blood sample. Antibodies are able to recognize cells with a target protein expressed on its surface and specifically bind only to those proteins. By labeling the two antibodies with different dyes, it is possible to monitor for the expression of two different proteins or different cell types simultaneously. Typically, this would require two scans, excitations or images, once each with the correct excitation wavelength. As a final step prior to analysis, these two images or data sets would have to be overlaid or combined. By using antibodies conjugated with both a dye and a conjugated polymer, one excitation wavelength can be used for the conjugated polymer to excite both dyes, and a single image or scan will include data sets from each of the two antibodies. This can be done with any number of antibody combinations provided there is sufficient ability to resolve the resulting signals. It is envisioned that the invention described herein can be used to increase the sensitivity of any of a number of commercially available tests including but not limited to the OraQuick Rapid HIV-1/2 Antibody Test, manufactured by OraSure Technologies, Inc. (Bethlehem, Pa.), which is a FDA-approved HIV diagnostic test for oral fluid samples. This test can provide screening results with over 99 percent accuracy in as little as 20 minutes. Conjugated Polymers Light harvesting conjugated polymer systems can efficiently transfer energy to nearby luminescent species. Mechanisms for energy transfer include, for example, resonant energy transfer (Forster (or fluorescence) resonance energy transfer, FRET), quantum charge exchange (Dexter energy transfer) and the like. Typically, however, these energy transfer mechanisms are relatively short range, and close proximity of the light harvesting conjugated polymer system to the signaling chromophore is required for efficient energy transfer. Amplification of the emission can occur when the number of individual chromophores in the light harvesting conjugated polymer system is large; emission from a fluorophore can be more intense when the incident light (the “pump light”) is at a wavelength which is absorbed by the light harvesting conjugated polymer system and transferred to the fluorophore than when the fluorophore is directly excited by the pump light. The conjugated polymers used in the present invention can be charge neutral, cationic or anionic. In some embodiments, the conjugated polymers are polycationic conjugated polymers. In other embodiments, the conjugated polymers are polyanionic conjugated polymers. In further embodiments, the conjugated polymers can include cationic, anionic, and/or neutral groups in various repeating subunits. In yet other embodiments, the conjugated polymers are neutral conjugated polymers. In some instances, conjugated polymers contain groups such as ethylene glycol oligomers, ethylene glycol polymers, co-ammonium alkoxy salts, and/or w-sulfonate alkoxy salts that impart solubility in aqueous solutions. In some instances the neutral conjugated polymers with non-ionic side chains are soluble in greater than 10 mg/mL in water or phosphate buffered saline solutions and in certains cases the solubility is greater than 50 mg/mL. In some embodiments the conjugated polymers contain either a terminal linking site (e.g., capping unit), internal linking site or both. In some embodiments, a conjugated polymer is one that comprises “low bandgap repeat units” of a type and in an amount that contribute an absorption to the polymer in the range of about 450 nm to about 1000 nm. The low bandgap repeat units may or may not exhibit such an absorption prior to polymerization, but does introduce that absorption when incorporated into the conjugated polymer. Such absorption characteristics allow the polymer to be excited at wavelengths that produce less background fluorescence in a variety of settings, including in analyzing biological samples and imaging and/or detecting molecules. Shifting the absorbance of the conjugated polymer to a lower energy and longer wavelength thus allows for more sensitive and robust methods. Additionally, many commercially available instruments incorporate imaging components that operate at such wavelengths at least in part to avoid such issues. For example, thermal cyclers that perform real-time detection during amplification reactions and microarray readers are available which operate in this region. Providing polymers that absorb in this region allows for the adaptation of detection methods to such formats, and also allows entirely new methods to be performed. Incorporation of repeat units that decrease the band gap can produce conjugated polymers with such characteristics. Exemplary optionally substituted species which result in polymers that absorb light at such wavelengths include 2,1,3-benzothiadiazole, benzoxidazole, benzoselenadiazole, benzotellurodiazole, naphthoselenadiazole, 4,7-di(thien-2-yl)-2,1,3-benzothiadiazole, squaraine dyes, quinoxalines, perylene, perylene diimides, diketopyrrolopyrrole, thienopyrazine low bandgap commercial dyes, olefins, and cyano-substituted olefins and isomers thereof. Further details relating to the composition, structure, properties and synthesis of suitable conjugated polymers can be found in U.S. patent application Ser. No. 11/329,495, filed Jan. 10, 2006, now published as US 2006-0183140 A1, which is incorporated herein by reference in the entirety. In one aspect, provided herein are conjugated polymers of Formula (I): wherein: each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x′(OCH2CH2)y′OCH3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C2-C18(hetero)aryl group; each optional linker L1 and L2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another substrate, molecule or biomolecule selected from amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G1 and G2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, optionally substituted fluorine and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, and thiols within G1, G2, L1 or L2 that allows, for functional conjugation to another molecule, substrate or biomolecule; each dashed bond, - - - - - - , is independently a single bond, triple bond or optionally substituted vinylene (—CR5═CR5—) wherein each R5 is independently hydrogen, cyano, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. Non-ionic side groups capable of imparting solubility in water as used herein refer to side groups which are not charged and allow the resulting polymer to be soluble in water or aqueous solutions with no visible particulates. In some embodiments, each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL, in excess of 15 mg/mL, in excess of 20 mg/mL, in excess of 25 mg/mL, in excess of 30 mg/mL, in excess of 35 mg/mL, in excess of 40 mg/mL, in excess of 45 mg/mL, in excess of 50 mg/mL, in excess of 60 mg/mL, in excess of 70 mg/mL, in excess of 80 mg/mL, in excess of 90 mg/mL or in excess of 100 mg/mL. In some embodiments, conjugated polymers described herein comprises a minimum number average molecular weight of greater than 5,000 g/mol, greater than 10,000 g/mol, greater than 15,000 g/mol, greater than 20,000 g/mol, greater than 25,000 g/mol, greater than 30,000 g/mol, greater than 40,000 g/mol, greater than 50,000 g/mol, greater than 60,000 g/mol, greater than 70,000 g/mol, greater than 80,000 g/mol, greater than 90,000 g/mol, or greater than 100,000 g/mol. In some embodiments, each R is independently (CH2)x(OCH2CH2)yOCH3 where each x is independently an integer from 0-20, each y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)zOCH3 where each z is independently an integer from 0 to 50. In some instances, each R is (CH2)3(OCH2CH2)11OCH3. In other embodiments, each R is independently a benzyl substituted with at least one (OCH2CH2)zOCH3 group where each z is independently an integer from 0 to 50. In some instances, each R is a benzyl substituted with at least one (OCH2CH2)10OCH3 group. In other instances, each R is a benzyl substituted with at least two (OCH2CH2)10OCH3 groups. In further instances, each R is a benzyl substituted with at least three (OCH2CH2)10OCH3 groups. In further embodiments, each R is independently where k and l are independent integers from 0 to 25; *=site for covalent attachment. In yet further embodiments, each R is independently is a dendrimer of PAMAM, PEA, PEHAM, PPI, tri-branched benzoate, or glycerol with a generation of 1 to 4 and optionally terminal substitutions, said optionally terminal substitutions are (- - - - -)CH2CH2O)jCH3 or (- - - - -)(OCH2CH2)jCH3 and j is an integer from 0 to 25 and the dotted lines (- - - - -) are each independently selected from any one or a combination of, C1-C12 alkyl, C1-C12 alkoxy, C2-C12 alkene, amido, amino, aryl, (CH2)r(OCH2CH2)s(CH2)r where each r is independently an integer from 0-20, s is independently an integer from 0 to 50, carbamate, carboxylate, C3-C12 cycloalkyl, imido, phenoxy, or C4-C18(hetero)aryl groups. In alternative embodiments, each R is independently, Where k and l are independent integers from 0 to 25 and the dotted lines (- - - - -) are each independently selected from any one or a combination of, C1-C12 alkyl, C1-C12 alkoxy, C2-C12 alkene, amido, amino, aryl, (CH2)r(OCH2CH2)s(CH2)r where each r is independently an integer from 0-20, s is independently an integer from 0 to 50, carbamate, carboxylate, C3-C12 cycloalkyl, imido, phenoxy, or C4-C18(hetero)aryl groups; *=site for covalent attachment. In alternative embodiments, each R is independently, Where k and l are independent integers from 0 to 25 and the dotted lines (- - - - -) are each independently selected from any one or a combination of, C1-C12 alkyl, C1-C12 alkoxy, C2-C12 alkene, amido, amino, aryl, (CH2)r(OCH2CH2)s(CH2)r where each r is independently an integer from 0-20, s is independently an integer from 0 to 50, carbamate, carboxylate, C3-C12 cycloalkyl, imido, phenoxy, or C4-C18(hetero)aryl groups; *=site for covalent attachment. In some embodiments, conjugated polymers described herein contain no optional linkers, L1 and/or L2. In other embodiments, conjugated polymers contain at least about 0.01 mol %, at least about 0.02 mol %, at least about 0.05 mol %, at least about 0.1 mol %, at least about 0.2 mol %, at least about 0.5 mol %, at least about 1 mol %, at least about 2 mol %, at least about 5 mol %, at least about 10 mol %, at least about 20 mol %, or about 25 mol % of optional linkers, L1 and/or L2. In some embodiments, conjugated polymers contain up to 50 mol % total of optional linkers, L1 and L2, and may contain about 40 mol % or less, about 30 mol % or less, about 25 mol % or less, about 20 mol % or less, about 15 mol % or less, about 10 mol % or less, or about 5 mol % or less. Linkers can be evenly or randomly distributed along the polymer main chain. In some embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to unsaturated backbone wherein R3 is independently hydrogen, halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and q is an integer from 0 to 4. In some embodiments, optional linkers L1 or L2 have the structure represented by: *=site for covalent attachment to unsaturated backbone wherein A is a site for conjugation, chain extension or crosslinking and is —[O—CH2—CH2]t—W, or (C1-C12)alkoxy-X; W is —OH or —COOH; X is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]uNH2; t is an integer from 1 to 20; and u is an integer from 1 to 8. In other embodiments, optional linkers L1 or L2 are selected from the group consisting of a-h having the structure: *=site for covalent attachment to unsaturated backbone wherein R′ is independently H, halogen, C1-C12 alkyl, (C1-C12 alkyl)NH2, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C2-C18(hetero)aryl, C2-C18(hetero)arylamino, —[CH2—CH2]r′—Z1, or (C1-C12)alkoxy-X1; and wherein Z1 is —OH or —COOH; X1 is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]s′(CH2)s′NH2; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH2)3(OCH2CH2)x″OCH3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)y″OCH3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein R15 is selected from the group consisting of 1-t having the structure: and k is 2, 4, 8, 12 or 24; *=site for covalent attachment to backbone. In certain embodiments, optional linkers L1 or L2 are In some embodiments, G1 and G2 are optionally substituted aryl wherein the optional substituent is selected from halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, boronic acid, boronate radical, boronic esters and optionally substituted fluorene. In other embodiments, G1 and G2 are the same. In further embodiments, G1 and G2 are different. G1 and G2 can be activated units that allow further conjugation, crosslinking, or polymer chain extension, or they may be nonactivated termination units. In some embodiments, G1 and G2 are independently selected from structures represented by: *=site for covalent attachment to backbone wherein R11 is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In other embodiments, G1 and G2 are independently selected from the group consisting of 1-18 having the structure: *=site for covalent attachment to backbone wherein R15 is selected from the group consisting of 1-t having the structure: and k is 2, 4, 8, 12 or 24. In further embodiments, G1 and G2 is In some embodiments, optional linkers, L1 and/or L2, G1, and/or G2 can be further conjugated to an organic dye, a biomolecule or a substrate. Covalent linkage can be introduced by any known method and can include, but is not limited to, chemistry involving maleimide/thiol; thiol/thiol; pyridyldithiol/thiol; succinimidyl iodoacetate/thiol; N-succinimidylester (NHS ester), sulfodicholorphenol ester (SDP ester), or pentafluorophenyl-ester (PFP ester)/amine; bissuccinimidylester/amine; imidoesters/amines; hydrazine or amine/aldehyde, dialdehyde or benzaldehyde; isocyanate/hydroxyl or amine; carbohydrate-periodate/hydrazine or amine; diazirine/aryl azide chemistry; pyridyldithiol/aryl azide chemistry; alkyne/azide; carboxy-carbodiimide/amine; amine/Sulfo-SMCC (Sulfosuccinimidyl 4-[N-maleimidomethyl]cyclohexane-1-carboxylate)/thiol; and amine/BMPH (N-[β-Maleimidopropionic acid]hydrazide.TFA)/thiol. In some embodiments, MU is selected from the group consisting of a′-k′ having the structure: =site for covalent attachment to unsaturated backbone wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL. Non-ionic side groups include those previously described for polymers of Formula (I). As used herein, in some embodiments, a pendant chain is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups which connects a polymer with a functional group for conjugation to another substrate, molecule, or biomolecule. In some embodiments, conjugated polymers of Formula (I) have the structure of Formula (Ia): wherein R, L1, L2, G1, G2, MU, a, b, c, d and n are described previously for formula (I). In a further aspect, conjugated polymers of Formula I have the structure of Formula (Ib): wherein at least one of G1 or G2 comprises a functional conjugation cite. In a further aspect, conjugated polymers of Formula I have the structure of Formula (Ic): wherein L1 comprises a functional conjugation cite. In a further aspect, conjugated polymers of Formula I have the structure of Formula (Id): wherein at least one of G1 or G2 comprises a functional conjugation cite. In a further aspect, conjugated polymers of Formula I have the structure of Formula (II): wherein L1, G1, G2, a, c, n and dashed bonds are described previously for formula (I). In some embodiments, conjugated polymers of Formula (II) have the structure of Formula (IIa): wherein L1, G1, G2, a, c, and n are described previously for formula (I). In a further aspect, conjugated polymers of Formula I have the structure of Formula (III): wherein L1, G1, G2, a, c, n and dashed bonds are described previously for formula (I). In some embodiments, conjugated polymers of Formula (III) have the structure of Formula (IIIa): wherein L1, G1, G2, a, c, and n are described previously for formula (I). In a further aspect, conjugated polymers of Formula I have the structure of Formula (IV): wherein each R5 is independently hydrogen, cyano, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and L1, G1, G2, a, c, n and dashed bonds are described previously for formula (I). In a further aspect, conjugated polymers of Formula I have the structure of Formula (V): wherein each R5 is independently hydrogen, cyano, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and L1, G1, G2, a, c, n and dashed bonds are described previously for formula (I). Also provided herein are polymers having the structure of the following formula: wherein: G1 and G2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, optionally substituted aryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters and optionally substituted fluorene; L is a bond or an aryl or heteroaryl group that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x(OCH2CH2)pOCH3 where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, or a C2-C18(hetero)aryl group; L1, L1′, L2 and L2′ are each independently a covalent bond, a C1-C12 alkylene, a C3-C12 cycloalkylene, a C2-C12 alkenylene, a C2-C12 alkynylene, a (C6-C18)aryl(C1-C12)alkylene, a (C6-C18)aryl(C2-C12)alkenylene, a (C6-C18)aryl(C1-C12)alkynylene, a C6-C18 arylene group, —Y1—[O—Y2]p—, —O—Y1—[O—Y2]p— wherein each C1-C12 alkylene, C3-C12 cycloalkylene, (C6-C18)aryl(C1-C12)alkylene, or C6-C18 arylene group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, C1-C12 haloalkyl, —Y1—[O—Y2]p— or —O—Y1—[O—Y2]p—; q is 0 or an integer from 1 to 8; p is 0 or an integer from 1 to 24; Y1 and Y2 are each independently a covalent bond, or a C1-12 alkylene group, a C3-C12 cycloalkylene, a C2-C18(hetero)arylene, a (C6-C18)aryl(C1-C12)alkylene, wherein each C1-12 alkylene group, a C3-C12 cycloalkylene, a C2-C18(hetero)arylene, a (C6-C18)aryl(C1-C12)alkylene is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; E1 and E1′ are each independently, hydrogen, C1-C6 alkyl, —OH, —COOH, —SH, —SR, —SHR+, SR2+, —SO3−, —PO4−, Br, —NH2, —NHR, —NR2, —NH3+, —NH2R+, —NHR2+or —NR3, wherein and each R is independently a C1-C6 alkyl and —SHR+, SR2+, —SO3−, —PO4−, —NH3+, —NH2R+, —NHR2+or —NR3+each optionally has an associated counterion; and n is an integer from 1 to about 1,000. Also provided herein are polymers having the structure of the following formula: wherein each R is independently O(CHx), or (CH2)3(OCH2CH2)pOCH3 where each x is independently an integer from 0-20, each p is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)mOCH3 where each m is independently an integer from 0 to 50; G1 is selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, optionally substituted aryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters and optionally substituted fluorene; and n is an integer from 1 to about 10,000. Additional embodiments of conjugated polymers are described in the following Examples. Preparation of Conjugated Polymers The synthesis of conjugated polymers described herein may be accomplished using means described in the chemical literature, using the methods described herein, or a combination thereof. Conjugated polymers described herein may be synthesized using standard synthetic techniques known to those of skill in the art or using methods known in the art in combination with methods described herein. In additions, solvents, temperatures and other reaction conditions presented herein may vary according to the practice and knowledge of those of skill in the art. The starting material used for the synthesis of the conjugated polymers of Formula (1) and polymers having the structures described in the prior section as described herein can be obtained from commercial sources, such as Aldrich Chemical Co. (Milwaukee, Wis.), Sigma Chemical Co. (St. Louis, Mo.), or the starting materials can be synthesized. The polymers described herein, and other related polymers having different substituents can be synthesized using techniques and materials known to those of skill in the art, such as described, for example, in March, ADVANCED ORGANIC CHEMISTRY 4th Ed., (Wiley 1992); Carey and Sundberg, ADVANCED ORGANIC CHEMISTRY 4th Ed., Vols. A and B (Plenum 2000, 2001), and Green and Wuts, PROTECTIVE GROUPS IN ORGANIC SYNTHESIS 3rd Ed., (Wiley 1999) (all of which are incorporated by reference in their entirety). General methods for the preparation of polymers as disclosed herein may be derived from known reactions in the field, and the reactions may be modified by the use of appropriate reagents and conditions, as would be recognized by the skilled person, for the introduction of the various moieties found in the formulae as provided herein. As a guide the following synthetic methods may be utilized. Generally, polymerization of fluorene polymeric structures may be accomplished using polymerization techniques known to those of skill in the art or using methods known in the art in combination with methods described herein. For example, polymerization can be achieved via Suzuki coupling with a commercially available fluorene-dihalide monomer, e.g., 2,7-dibromofluorene, and its diboronic acid or ester derivative: Structures A-1 and A-2 are catalyzed by a metal catalyst to form exemplary polymer A-3 with termination points, labeled Y. Each Y is independently —H, —Br, —B(OH)2, or boronic ester, e.g., 4,4,5,5,-tetramethyl- 1,3,2-dioxaborolanyl. Synthesis of diboronic ester derivatives from a fluorene-dihalide monomer can also be accomplished via Suzuki coupling with bis(pinacolato)diboron: Substituents such as ethylene glycol oligomers or ethylene glycol polymers may be attached to monomers prior to polymerization or to the polymer itself after polymerization. An exemplary scheme of synthesizing substituted fluorene monomers with mPEGylated groups is as follows: 2,7-dibromofluorene (B-1) and 3-bromopropanol in the presence of a strong base such as sodium hydroxide, potassium hydroxide, or the like and a phase transfer catalyst, e.g. tetrabutylammonium bromide, is heated and reacted to completion to form 2,7-dibromo-9,9-di(3′-hydroxypropanyl)fluorene (B-2). —OH groups of B-2 are tosylated with tosyl chloride in the presence of pyridine and allowed to react to completion to form 2,7-dibromo-9,9-di(3′-methylbenzenesulfonatopropanyl)fluorene (B-3). B-3 is then reacted with a mPEG(x) alcohol in the presence of potassium tert-butoxide to form B-4 with attached mPEG chains. mPEG alcohols can have 1-50 mPEG chains. Typical sizes include but are not limited to mPEG5, mPEG8, mPEG11, mPEG24. In an alternative scheme, mPEG alcohols can be tosylated first via tosyl chloride and then reacted to B-2 to form B-4. Substituted monomers, such as exemplary structure B-4, can be further derivatized to diboronic esters in the schemes disclosed herein and subsequently be used for polymerization such as via Suzuki coupling. Polymeric fluorenes may also be obtained through the use of other reaction schemes involving organometallic catalysis. For example, the Yamamoto reaction uses a nickel(0)-based catalyst for the homo-coupling of aryl halide monomers like exemplary structure B-4. Additionally, conjugated polymers can be synthesized using Stille, Heck, and Sonogashira coupling reactions. See, e.g., Yamamoto et al., Macromolecules 25: 1214-1223, 1992; Kreyenschmidt et al., Macromolecules 28: 4577-4582, 1995; and Pei et al., J. Am. Chem. Soc. 118: 7416-7417, 1996 regarding Yamamoto reaction schemes. See, also, Leclerc, Polym. Sci. Part A: Polym. Chem. 39: 2867-2873, 2001 for Stille reaction schemes; Mikroyannidis et al., J. Polym. Sci. Part A: Polym. Chem. 45: 4661-4670, 2007 for Heck reaction schemes; and Sonogashira et al., Tetrahedron Lett. 16: 4467-4470, 1975 and Lee et al., Org. Lett. 3: 2005-2007, 2001 for Sonogashira reaction schemes. Linkers and capping units can be conjugated to a fluorene polymer backbone via similar mechanisms as described previously. For example, bromo- and boronic esters of capping units can be used to append one or both ends of a polymer. Utilizing both bromo- and boronic esters of capping units will append both ends of polymer. Utilizing only one form, either a bromo- or boronic ester of a capping unit, will append only those ends terminated with its repective complement and for symmetric A-A+B-B polymerizations can be used to statistically modify only one end of a polymer. For asymmetric polymers this approach is used to chemically ensure the polymers are only modified at a single chain terminus. FIG. 11 depicts appending an exemplary fluorene polymer with Y ends with one or more phenyl groups with bromobenzene, phenyl boronic acid or both using Suzuki coupling. Capping units can also be appended asymmetrically by first reacting a bromo-capping unit with a polymer with Y ends and subsequently reacting the polymer with a boronic ester capping unit. Exemplary bromo- and boronic ester capping units include but are not limited to the following structures: Further capping units can be found in structures 1-31 described herein or in the following Examples and methods for their attachment. The incorporation of optional linkers into conjugated polymer backbones further described in U.S. application Ser. No. 11/868,870, filed Oct. 8, 2007 and published as U.S. Application No. 2008/0293164, which application is herein incorporated by reference in its entirety. A desired optional linker incorporation can be achieved by varying the molar ratio of optional linker to bi-functional monomer. For example, an optional linker can be incorporated by substituting a percentage of one of the bi-functional monomers with a similar bi-functional optional linker which comprises the conjugation site of interest. The number and type of linking site included in the polymer is controlled by the feed ratio of the monomers to optional linker in the polymerization reaction. By varying the feed ratio, conjugated polymers can contain at least about 0.01 mol % of linker, L, and may contain at least about 0.02 mol %, at least about 0.05 mol %, at least about 0.1 mol %, at least about 0.2 mol %, at least about 0.5 mol %, at least about 1 mol %, at least about 2 mol %, at least about 5 mol %, at least about 10 mol %, at least about 20 mol %, or at least about 30 mol %. The conjugated polymers may contain up to 100 mol % of linker, L, and may contain about 99 mol % or less, about 90 mol % or less, about 80 mol % or less, about 70 mol % or less, about 60 mol % or less, about 50 mol % or less, or about 40 mol % or less. Linkers can be evenly or randomly distributed along the polymer main chain. In further embodiments, an optional linker can further allow covalent attachment of the resulting polymer to biomolecules, secondary reporters or other assay components. In alternative embodiments, the methods described herein to incorporate optional linkers may be used in combination with methods of introducing capping units with linking sites to produce polymers with both internal and terminal linking sites for conjugation. A non-limiting application of a polymer with both optional linkers and terminal capping units with linking sites for conjugation are polymer-dye-biomolecule tandem conjugates where the polymer is used as an energy transfer donor, such as in FRET, to a secondary dye acceptor thus shifting the emission wavelength to that of the corresponding dye. The person skilled in the art may further appreciate various syntheses and polymerization methods and embodiments of the present disclosure upon review of the following illustrative and non-limiting Examples. Antigen-Antibody Interactions The interactions between antigens and antibodies are the same as for other non-covalent protein-protein interactions. In general, four types of binding interactions exist between antigens and antibodies: (i) hydrogen bonds, (ii) dispersion forces, (iii) electrostatic forces between Lewis acids and Lewis bases, and (iv) hydrophobic interactions. Certain physical forces contribute to antigen-antibody binding, for example, the fit or complimentary of epitope shapes with different antibody binding sites. Moreover, other materials and antigens may cross-react with an antibody, thereby competing for available free antibody. Measurement of the affinity constant and specificity of binding between antigen and antibody is a pivotal element in determining the efficacy of an immunoassay, not only for assessing the best antigen and antibody preparations to use but also for maintaining quality control once the basic immunoassay design is in place. Antibodies Antibody molecules belong to a family of plasma proteins called immunoglobulins, whose basic building block, the immunoglobulin fold or domain, is used in various forms in many molecules of the immune system and other biological recognition systems. A typical immunoglobulin has four polypeptide chains, containing an antigen binding region known as a variable region and a non-varying region known as the constant region. Native antibodies and immunoglobulins are usually heterotetrameric glycoproteins of about 150,000 Daltons, composed of two identical light (L) chains and two identical heavy (H) chains. Each light chain is linked to a heavy chain by one covalent disulfide bond, while the number of disulfide linkages varies between the heavy chains of different immunoglobulin isotypes. Each heavy and light chain also has regularly spaced intrachain disulfide bridges. Each heavy chain has at one end a variable domain (VH) followed by a number of constant domains. Each light chain has a variable domain at one end (VL) and a constant domain at its other end. The constant domain of the light chain is aligned with the first constant domain of the heavy chain, and the light chain variable domain is aligned with the variable domain of the heavy chain. Depending on the amino acid sequences of the constant domain of their heavy chains, immunoglobulins can be assigned to different classes. There are at least five (5) major classes of immunoglobulins: IgA, IgD, IgE, IgG and IgM, and several of these may be further divided into subclasses (isotypes), e.g. IgG-1, IgG-2, IgG-3 and IgG-4; IgA-1 and IgA-2. The subunit structures and three-dimensional configurations of different classes of immunoglobulins are well known. Further details regarding antibody structure, function, use and preparation are discussed in U.S. Pat. No. 6,998,241, issued Feb. 14, 2006, the entire contents of which are incorporated herein by reference. Sandwich Assays Antibody or multiple antibody sandwich assays are well known to those skilled in the art including a disclosed in U.S. Pat. No. 4,486,530, issued Dec. 4, 1984, and references noted therein. The structures described in FIGS. 6, 7, 8, 9, 10 and 14 can be used directly as described or in various sandwich configurations including those described in Example 37. A sandwich configuration or a sandwich assay refers to the use of successive recognition events to build up layers of various biomolecules and reporting elements to signal the presence of a particular biomolecule, for example a target biomolecule or a target-associated biomolecule. A standard example of this would be the successive use of antibodies. In these assays, a primary antibody binds the target, the secondary antibody binds the primary, a third antibody can bind the secondary and so on. With each successive layer additional reporting groups can be added. Another strategy is using a repetitive addition of alternating layers of two (or more) mutually-recognizable components, or more than two components in a chain-recognition relationship, which comprise one or both of the components in a form of multimeric structure. In such a setup, one or more of the functional group(s) in each of the multimeric structure can be labeled with reporting group(s) and the unoccupied functional group(s) can serve as the recognition site for the other component(s), and this system will subsequently provide a platform for signal amplification. A typical example of this approach is the use of streptavidin-reporter conjugate and biotinylated anti-streptavidin antibody. In such assays, a biotinylated sensor molecule (nucleic acid or antibody) can be used to bind a target biomolecule, which is subsequently recognized by a detection system containing a streptavidin-reporter conjugate and biotinylated anti-streptavidin antibody. The sandwich structure in this case can be built up by successive rounds of biotinylated antibodies and labeled streptavidin complexes interaction to achieve the signal amplification. With an additional conjugation of a conjugated polymer to either the biotinylated antibody or the streptavidin-reporter complex, it is possible to further increase the signal output. In essence, the integration of a conjugated polymer in this type of signal amplification system can further amplify signals to a higher level. The bioconjugated polymer complexes described in FIGS. 6, 7, 8, 9, 10, 14, 15, 16 and 17 can be used to create optically enhanced sandwich assays by directly integrating a light harvesting conjugated polymer into commonly utilized recognition elements. The benefits of the conjugated polymer conjugated structures can also be applied directly to the primary target recognition elements without the need for successive recognition elements. For example, a primary antibody can be directly conjugated to polymer-dye complex such as shown in FIG. 14. Such a complex can be used to directly probe the presence of a target biomolecule. Polynucleotides Amplified target polynucleotides may be subjected to post amplification treatments. For example, in some cases, it may be desirable to fragment the target polynucleotide prior to hybridization in order to provide segments which are more readily accessible. Fragmentation of the nucleic acids can be carried out by any method producing fragments of a size useful in the assay being performed; suitable physical, chemical and enzymatic methods are known in the art. An amplification reaction can be performed under conditions which allow the sensor polynucleotide to hybridize to the amplification product during at least part of an amplification cycle. When the assay is performed in this manner, real-time detection of this hybridization event can take place by monitoring for light emission during amplification. Real time PCR product analysis (and related real time reverse-transcription PCR) provides a well-known technique for real time PCR monitoring that has been used in a variety of contexts, which can be adapted for use with the methods described herein (see, Laurendeau et al. (1999) “TaqMan PCR-based gene dosage assay for predictive testing in individuals from a cancer family with INK4 locus haploinsufficiency” Clin Chem 45(7):982-6; Laurendeau et al. (1999) “Quantitation of MYC gene expression in sporadic breast tumors with a real-time reverse transcription-PCR assay” Clin Chem 59(12):2759-65; and Kreuzer et al. (1999) “LightCycler technology for the quantitation of bcr/abl fusion transcripts” Cancer Research 59(13):3171-4, all of which are incorporated by reference). Samples In principle, a sample can be any material suspected of containing a target biomolecule (e.g., antibody, protein, affinity ligand, peptide, nucleic acid and the like) capable of causing excitation of a conjugated polymer complex. In some embodiments, the sample can be any source of biological material which comprises biomolecules that can be obtained from a living organism directly or indirectly, including cells, tissue or fluid, and the deposits left by that organism, including viruses, mycoplasma, and fossils. The sample may comprise a target biomolecule prepared through synthetic means, in whole or in part. Typically, the sample is obtained as or dispersed in a predominantly aqueous medium. Nonlimiting examples of the sample include blood, urine, semen, milk, sputum, mucus, a buccal swab, a vaginal swab, a rectal swab, an aspirate, a needle biopsy, a section of tissue obtained for example by surgery or autopsy, plasma, serum, spinal fluid, lymph fluid, the external secretions of the skin, respiratory, intestinal, and genitourinary tracts, tears, saliva, tumors, organs, samples of in vitro cell culture constituents (including but not limited to conditioned medium resulting from the growth of cells in cell culture medium, putatively virally infected cells, recombinant cells, and cell components), and a recombinant library comprising polynucleotide sequences. The sample can be a positive control sample which is known to contain the target biomolecule or a surrogate therefore. A negative control sample can also be used which, although not expected to contain the target biomolecule, is suspected of containing it (via contamination of one or more of the reagents) or another component capable of producing a false positive, and is tested in order to confirm the lack of contamination by the target biomolecule of the reagents used in a given assay, as well as to determine whether a given set of assay conditions produces false positives (a positive signal even in the absence of target biomolecule in the sample). The sample can be diluted, dissolved, suspended, extracted or otherwise treated to solubilize and/or purify any target polynucleotide present or to render it accessible to reagents which are used in an amplification scheme or to detection reagents. Where the sample contains cells, the cells can be lysed or permeabilized to release the polynucleotides within the cells. One step permeabilization buffers can be used to lyse cells which allow further steps to be performed directly after lysis, for example a polymerase chain reaction. Organic Dyes Organic dyes include signaling chromophores and fluorophores. In some embodiments, a signaling chromophore or fluorophore may be employed, for example to receive energy transferred from an excited state of an optically active unit, or to exchange energy with a labeled probe, or in multiple energy transfer schemes. Fluorophores useful in the inventions described herein include any substance which can absorb energy of an appropriate wavelength and emit or transfer energy. For multiplexed assays, a plurality of different fluorophores can be used with detectably different emission spectra. Typical fluorophores include fluorescent dyes, semiconductor nanocrystals, lanthanide chelates, and fluorescent proteins. Exemplary fluorescent dyes include fluorescein, 6-FAM, rhodamine, Texas Red, tetramethylrhodamine, a carboxyrhodamine, carboxyrhodamine 6G, carboxyrhodol, carboxyrhodamine 110, Cascade Blue, Cascade Yellow, coumarin, Cy2 ®, Cy3 ®, Cy3.5 ®, Cy5 ®, Cy5.5®, Cy-Chrome, DyLight 350, DyLight 405, DyLight 488, DyLight 549, DyLight 594, DyLight 633, DyLight 649, DyLight 680, DyLight 750, DyLight 800, phycoerythrin, PerCP (peridinin chlorophyll-a Protein), PerCP-Cy5.5, JOE (6-carboxy-4′,5′-dichloro-2′,7′-dime1hoxyfluorescein), NED, ROX (5-(and-6)-carboxy-X-rhodamine), HEX, Lucifer Yellow, Marina Blue, Oregon Green 488, Oregon Green 500, Oregon Green 514, Alexa Fluor® 350, Alexa Fluor® 430, Alexa Fluor® 488, Alexa Fluor® 532, Alexa Fluor® 546, Alexa Fluor® 568, Alexa Fluor® 594, Alexa Fluor® 633, Alexa Fluor® 647, Alexa Fluor® 660, Alexa Fluor® 680, 7-amino-4-methylcoumarin-3-acetic acid, BODIPY® FL, BODIPY® FL-Br2, BODIPY® 530/550, BODIPY® 558/568, BODIPY® 564/570, BODIPY® 576/589, BODIPY® 581/591, BODIPY® 630/650, BODIPY® 650/665, BODIPY® R6G, BODIPY® TMR, BODIPY® TR, conjugates thereof, and combinations thereof. Exemplary lanthanide chelates include europium chelates, terbium chelates and samarium chelates. A wide variety of fluorescent semiconductor nanocrystals (“SCNCs”) are known in the art; methods of producing and utilizing semiconductor nanocrystals are described in: PCT Publ. No. WO 99/26299 published May 27, 1999, inventors Bawendi et al.; U.S. Pat. No. 5,990,479 issued Nov. 23, 1999 to Weiss et al.; and Bruchez et al., Science 281:2013, 1998. Semiconductor nanocrystals can be obtained with very narrow emission bands with well-defined peak emission wavelengths, allowing for a large number of different SCNCs to be used as signaling chromophores in the same assay, optionally in combination with other non-SCNC types of signaling chromophores. Exemplary polynucleotide-specific dyes include acridine orange, acridine homodimer, actinomycin D, 7-aminoactmomycin D (7-AAD), 9-amino-6-chlor-2-methoxyacridine (ACMA), BOBO™-1 iodide (462/481), BOBO™-3 iodide (570/602), BO-PRO™-1 iodide (462/481), BO-PRO™-3 iodide (575/599), 4′,6-diamidino-2- phenylindole, dihydrochloride (DAPI), 4′,6-diamidino-2-phenylindole, dihydrochloride (DAPI), 4′,6-diamidino-2-phenylindole, dilactate (DAPI, dilactate), dihydroethidium (hydroethidine), dihydroethidium (hydroethidine), dihydroethidium (hydroethidine), ethidium bromide, ethidium diazide chloride, ethidium homodimer-1 (EthD-1), ethidium homodimer-2 (EthD-2), ethidium monoazide bromide (EMA), hexidium iodide, Hoechst 33258, Hoechst 33342, Hoechst 34580, Hoechst S769121, hydroxystilbamidine, methanesulfonate, JOJO™-1 iodide (529/545), JO-PRO™-1 iodide (530/546), LOLO™-1 iodide (565/579), LO-PRO™-1 iodide (567/580), NeuroTrace™ 435/455, NeuroTrace™ 500/525, NeuroTrace™ 515/535, NeuroTrace™ 530/615, NeuroTrace™ 640/660, OliGreen, PicoGreen® ssDNA, PicoGreen® dsDNA, POPO™-1 iodide (434/456), POPO™-3 iodide (534/570), PO-PRO™-1 iodide (435/455), PO-PRO™-3 iodide (539/567), propidium iodide, RiboGreen®, SlowFade®, SlowFade® Light, SYBR® Green I, SYBR® Green II, SYBR® Gold, SYBR® 101, SYBR® 102, SYBR® 103, SYBR® DX, TO-PRO®-1, TO-PRO®-3, TO-PRO®-5, TOTO®-1, TOTO®-3, YO-PRO®-1 (oxazole yellow), YO-PRO®-3, YOYO®-1, YOYO®-3, TO, SYTOX® Blue, SYTOX® Green, SYTOX® Orange, SYTO® 9, SYTO® BC, SYTO® 40, SYTO® 41, SYTO® 42, SYTO® 43, SYTO® 44, SYTO® 45, SYTO® Blue, SYTO® 11, SYTO® 12, SYTO® 13, SYTO® 14, SYTO® 15, SYTO® 16, SYTO® 20, SYTO® 21, SYTO® 22, SYTO® 23, SYTO® 24, SYTO® 25, SYTO® Green, SYTO® 80, SYTO® 81, SYTO® 82, SYTO® 83, SYTO® 84, SYTO® 85, SYTO® Orange, SYTO® 17, SYTO® 59, SYTO® 60, SYTO® 61, SYTO® 62, SYTO® 63, SYTO® 64, SYTO® Red, netropsin, distamycin, acridine orange, 3,4-benzopyrene, thiazole orange, TOMEHE, daunomycin, acridine, pentyl-TOTAB, and butyl-TOTIN. Asymmetric cyanine dyes may be used as the polynucleotide-specific dye. Other dyes of interest include those described by Geierstanger, B. H. and Wemmer, D. E., Annu. Rev. Vioshys. Biomol. Struct. 1995, 24, 463-493, by Larson, C. J. and Verdine, G. L., Bioorganic Chemistry: Nucleic Acids, Hecht, S. M., Ed., Oxford University Press: New York, 1996; pp 324-346, and by Glumoff, T. and Goldman, A. Nucleic Acids in Chemistry and Biology, 2nd ed., Blackburn, G. M. and Gait, M. J., Eds., Oxford University Press: Oxford, 1996, pp 375-441. The polynucleotide-specific dye may be an intercalating dye, and may be specific for double-stranded polynucleotides. The term “fluorescent protein” includes types of protein known to absorb and emit light. One of the more commonly used classes of such materials are phycobiliproteins. Examples include but are not limited to phycoerythrin (PE and R-PE), allophycocyanin (APC) and PerCP. Other classes include green fluorescent protein and related versions. The term “green fluorescent protein” refers to both native Aequorea green fluorescent protein and mutated versions that have been identified as exhibiting altered fluorescence characteristics, including altered excitation and emission maxima, as well as excitation and emission spectra of different shapes (Delagrave, S. et al. (1995) Bio/Technology 13:151-154; Heim, R. et al. (1994) Proc. Natl. Acad. Sci. USA 91:12501-12504; Heim, R. et al. (1995) Nature 373:663-664). Delgrave et al. isolated mutants of cloned Aequorea victoria GFP that had red-shifted excitation spectra. Bio/Technology 13:151-154 (1995). Heim, R. et al. reported a mutant (Tyr66 to His) having a blue fluorescence (Proc. Natl. Acad. Sci. (1994) USA 91:12501-12504). Substrates In some embodiments, an assay component can be located upon a substrate. The substrate can comprise a wide range of material, either biological, nonbiological, organic, inorganic, or a combination of any of these. For example, the substrate may be a polymerized Langmuir Blodgett film, functionalized glass, Si, Ge, GaAs, GaP, SiO2, SiN4, modified silicon, or any one of a wide variety of gels or polymers such as (poly)tetrafluoroethylene, (poly)vinylidenedifluoride, polystyrene, cross-linked polystyrene, polyacrylic, polylactic acid, polyglycolic acid, poly(lactide coglycolide), polyanhydrides, poly(methyl methacrylate), poly(ethylene-co-vinyl acetate), polysiloxanes, polymeric silica, latexes, dextran polymers, epoxies, polycarbonates, or combinations thereof. Conducting polymers and photoconductive materials can be used. Substrates can be planar crystalline substrates such as silica based substrates (e.g. glass, quartz, or the like), or crystalline substrates used in, e.g., the semiconductor and microprocessor industries, such as silicon, gallium arsenide, indium doped GaN and the like, and includes semiconductor nanocrystals. The substrate can take the form of a photodiode, an optoelectronic sensor such as an optoelectronic semiconductor chip or optoelectronic thin-film semiconductor, or a biochip. The location(s) of probe(s) on the substrate can be addressable; this can be done in highly dense formats, and the location(s) can be microaddressable or nanoaddressable. Silica aerogels can also be used as substrates, and can be prepared by methods known in the art. Aerogel substrates may be used as free standing substrates or as a surface coating for another substrate material. The substrate can take any form and typically is a plate, slide, bead, pellet, disk, particle, microparticle, nanoparticle, strand, precipitate, optionally porous gel, sheets, tube, sphere, container, capillary, pad, slice, film, chip, multiwell plate or dish, optical fiber, etc. The substrate can be any form that is rigid or semi-rigid. The substrate may contain raised or depressed regions on which an assay component is located. The surface of the substrate can be etched using well known techniques to provide for desired surface features, for example trenches, v-grooves, mesa structures, or the like. Surfaces on the substrate can be composed of the same material as the substrate or can be made from a different material, and can be coupled to the substrate by chemical or physical means. Such coupled surfaces may be composed of any of a wide variety of materials, for example, polymers, plastics, resins, polysaccharides, silica or silica-based materials, carbon, metals, inorganic glasses, membranes, or any of the above-listed substrate materials. The surface can be optically transparent and can have surface Si—OH functionalities, such as those found on silica surfaces. The substrate and/or its optional surface can be chosen to provide appropriate characteristics for the synthetic and/or detection methods used. The substrate and/or surface can be transparent to allow the exposure of the substrate by light applied from multiple directions. The substrate and/or surface may be provided with reflective “mirror” structures to increase the recovery of light. The substrate and/or its surface is generally resistant to, or is treated to resist, the conditions to which it is to be exposed in use, and can be optionally treated to remove any resistant material after exposure to such conditions. Polynucleotide or polypeptide probes can be fabricated on or attached to the substrate by any suitable method, for example the methods described in U.S. Pat. No. 5,143,854, PCT Publ. No. WO 92/10092, U.S. patent application Ser. No. 07/624,120, filed Dec. 6, 1990 (now abandoned), Fodor et al., Science, 251: 767-777 (1991), and PCT Publ. No. WO 90/15070). Techniques for the synthesis of these arrays using mechanical synthesis strategies are described in, e.g., PCT Publication No. WO 93/09668 and U.S. Pat. No. 5,384,261. Still further techniques include bead based techniques such as those described in PCT Appl. No. PCT/US93/04145 and pin based methods such as those described in U.S. Pat. No. 5,288,514. Additional flow channel or spotting methods applicable to attachment of sensor polynucleotides or polypeptides to the substrate are described in U.S. patent application Ser. No. 07/980,523, filed Nov. 20, 1992, and U.S. Pat. No. 5,384,261. Reagents are delivered to the substrate by either (1) flowing within a channel defined on predefined regions or (2) “spotting” on predefined regions. A protective coating such as a hydrophilic or hydrophobic coating (depending upon the nature of the solvent) can be used over portions of the substrate to be protected, sometimes in combination with materials that facilitate wetting by the reactant solution in other regions. In this manner, the flowing solutions are further prevented from passing outside of their designated flow paths. Typical dispensers include a micropipette optionally robotically controlled, an ink-jet printer, a series of tubes, a manifold, an array of pipettes, or the like so that various reagents can be delivered to the reaction regions sequentially or simultaneously. The substrate or a region thereof may be encoded so that the identity of the sensor located in the substrate or region being queried may be determined. Any suitable coding scheme can be used, for example optical codes, RFID tags, magnetic codes, physical codes, fluorescent codes, and combinations of codes. Excitation and Detection Any instrument that provides a wavelength that can excite the conjugated polymer complex and is shorter than the emission wavelength(s) to be detected can be used for excitation. Commercially available devices can provide suitable excitation wavelengths as well as suitable detection components. Exemplary excitation sources include a broadband UV light source such as a deuterium lamp with an appropriate filter, the output of a white light source such as a xenon lamp or a deuterium lamp after passing through a monochromator to extract out the desired wavelengths, a continuous wave (cw) gas laser, a solid state diode laser, or any of the pulsed lasers. Emitted light can be detected through any suitable device or technique; many suitable approaches are known in the art. For example, a fluorimeter or spectrophotometer may be used to detect whether the test sample emits light of a wavelength characteristic of the signaling chromophore upon excitation of the conjugated polymer. Compositions of Matter Also provided are compositions of matter of any of the molecules described herein in any of various forms. The conjugated polymers and complexes including conjugated polymers as described herein may be provided in purified and/or isolated form. The conjugated polymers and complexes including conjugated polymers may be provided in either crystalline or amorphous form. The conjugated polymers and complexes including conjugated polymers may be provided in solution, which may be a predominantly aqueous solution, which may comprise one or more of the additional solution components described herein, including without limitation additional solvents, buffers, biomolecules, polynucleotides, fluorophores, etc. In addition, a mixture of CPs in solution is also able to provide improved detection sensitivity as compared to that for a single CP/dye system. The conjugated polymers and complexes including conjugated polymers can be present in solution at a concentration at which a first emission from the first optically active units can be detected in the absence of biomolecule target or a biomolecule associated therewith. The solution may comprise additional components as described herein, including labeled probes such as fluorescently labeled antibodies or polynucleotides, specific for a species or a class of biomolecule target or a biomolecule associated therewith for the conjugated polymers and complexes including conjugated polymers. The conjugated polymers and complexes including conjugated polymers may be provided in the form of a film. The compositions of matter may be claimed by any property described herein, including by proposed structure, by method of synthesis, by absorption and/or emission spectrum, by elemental analysis, by NMR spectra, or by any other property or characteristic. In some embodiments expression of a gene is detected in a sample. In a further embodiment identification of a cell marker or cell type is detected in a sample either in a flow cytometer, cell sorter, microscope, plate reader or fluorescence imager. In a further embodiment the identification of cell type or marker is used in the diagnosis of lymphoma or other circulating cancers. In a further embodiment the identification of cell type or marker is used in the diagnosis and monitoring of HIV infection. In a further embodiment the identification of cell type or marker is used to sort cells for therapeutic application. In a further embodiment, a measured result of detecting a biomolecule target or a biomolecule associated therewith can be used to diagnose a disease state of a patient. In yet another embodiment the detection method of the invention can further include a method of diagnosing a disease state. In a related embodiment, the method of diagnosing a disease can include reviewing or analyzing data relating to the presence of a biomolecule target or a biomolecule associated therewith and providing a conclusion to a patient, a health care provider or a health care manager, the conclusion being based on the review or analysis of data regarding a disease diagnosis. Reviewing or analyzing such data can be facilitated using a computer or other digital device and a network as described herein. It is envisioned that information relating to such data can be transmitted over the network. In practicing the methods of the present invention, many conventional techniques in molecular biology are optionally utilized. These techniques are well known and are explained in, for example, Ausubel et al. (Eds.) Current Protocols in Molecular Biology, Volumes I, II, and III, (1997), Ausubel et al. (Eds.), Short Protocols in Molecular Biology: A Compendium of Methods from Current Protocols in Molecular Biology, 5th Ed., John Wiley & Sons, Inc. (2002), Sambrook et al., Molecular Cloning: A Laboratory Manual, 3rd Ed., Cold Spring Harbor Laboratory Press (2000), Innis et al. (Eds.) PCR Protocols: A Guide to Methods and Applications, Elsevier Science & Technology Books (1990), and Greg T. Hermanson, Bioconjugate Techniques, 2nd Ed., Academic Press, Inc. (2008) all of which are incorporated herein by reference. FIG. 12 is a block diagram showing a representative example logic device through which reviewing or analyzing data relating to the present invention can be achieved. Such data can be in relation to a disease, disorder or condition in a subject. FIG. 12 shows a computer system (or digital device) 800 connected to an apparatus 820 for use with the conjugated polymers or conjugated polymers complexes 824 to, for example, produce a result. The computer system 800 may be understood as a logical apparatus that can read instructions from media 811 and/or network port 805, which can optionally be connected to server 809 having fixed media 812. The system shown in FIG. 12 includes CPU 801, disk drives 803, optional input devices such as keyboard 815 and/or mouse 816 and optional monitor 807. Data communication can be achieved through the indicated communication medium to a server 809 at a local or a remote location. The communication medium can include any means of transmitting and/or receiving data. For example, the communication medium can be a network connection, a wireless connection or an internet connection. It is envisioned that data relating to the present invention can be transmitted over such networks or connections. In one embodiment, a computer-readable medium includes a medium suitable for transmission of a result of an analysis of a biological sample. The medium can include a result regarding a disease condition or state of a subject, wherein such a result is derived using the methods described herein. Kits Kits comprising reagents useful for performing described methods are also provided. In some embodiments, a kit comprises reagents including conjugated polymers or conjugated polymers complexes, bioconjugates, for example, antibodies, nucleic acids, and other components as described herein. The kit may optionally contain one or more of the following: one or more labels that can be incorporated into conjugated polymers or conjugated polymers complexes; and one or more substrates which may or may not contain an array, etc. The components of a kit can be retained by a housing. Instructions for using the kit to perform a described method can be provided with the housing, and can be provided in any fixed medium. The instructions may be located inside the housing or outside the housing, and may be printed on the interior or exterior of any surface forming the housing that renders the instructions legible. A kit may be in multiplex form for detection of one or more different target biomolecules or biomolecules associated therewith. As described herein and shown in FIG. 13, in certain embodiments a kit 903 can include a container or housing 902 for housing various components. As shown in FIG. 13, and described herein, in one embodiment a kit 903 comprising one or more conjugated polymers or conjugated polymers complexes reagents 905, and optionally a substrate 900 is provided. As shown in FIG. 13, and described herein, the kit 903 can optionally include instructions 901. Other embodiments of the kit 903 are envisioned wherein the components include various additional features described herein. EXAMPLES The following examples provide illustrative methods for making and testing the effectiveness of the conjugated polymers described herein. These examples are provided for illustrative purposes only and not to limit the scope of the claims provided herein. All of the methods disclosed and claimed herein can be made and executed without undue experimentation in light of the present disclosure. It will be apparent to those of skill in the art that variations may be applied to the methods and in the steps or in the sequence of steps of the method described herein without departing from the concept, spirit and scope of the claims. All such similar substitutes and modifications apparent to those skilled in the art are deemed to be within the spirit, scope and concept of the appended claims. Example 1: Synthesis of a Polymer of Formula (I) Example 1a: Synthesis of monomers, 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) and 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (B) for subsequent polymerization Step 1: 2,7-dibromo-9,9-di(3′-hydroxypropanyl)fluorene 2,7-dibromofluorene (9.72 g, 30 mmol), tetrabutylammonium bromide (300 mg, 0.93 mmol), and DMSO (100 mL) were added to a 3-neck flask under nitrogen(g), followed by the addition of 50% NaOH (15 mL, 188 mmol) via syringe. The mixture was heated to 80° C., and 3-bromopropanol (6.70 mL, 77 mmol) was added dropwise via addition funnel, and the reaction mixture was stirred at 80° C. for another 2 hours. Upon completion, the mixture was cooled to room temperature and quenched with water (250 mL). The aqueous layer was extracted with ethyl acetate (3 150 mL portions). The organic layers were combined, washed with water, then dried over MgSO4, and filtered. The solvent was removed and the residual was recrystallized in chloroform to yield pale yellow needle crystals (9.20 g, 70%). Step 2: 2,7-dibromo-9,9-di(3′-methylbenzenesulfonatopropanyl)fluorene 2,7-dibromo-9,9-di(3′-hydroxypropanyl)fluorene (500 mg, 1.14 mmol) was dissolved in dichloromethane (5 mL) at 0° C. under nitrogen(g). To the mixture, added p-toluenesulfonyl chloride (650 mg, 3.40 mmol), followed by pyridine (0.39 mL, 4.77 mmol). Allowed reaction to stir at 0° C. and naturally rise to room temperature over night. The reaction was quenched with water (15 mL). Removal of solvent by vacuo resulted solids formation. Filtered off solids to yield white solids (758 mg, 89%). Step 3: 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) mPEG11 alcohol (770 mg, 1.49 mmol) was dissolved in anhydrous THF (2 mL) at 0° C. under nitrogen. To the mixture, was added potassium tert-butoxide (1.63 mmol, 1.63 mL, 1M in THF). After 10 min stirring, 2,7-dibromo-9,9-di(3′-methylbenzenesulfonatopropanyl)fluorene (504 mg, 0.673 mmol) in 10 mL of THF was added via a syringe. The mixture was allowed to room temperature and stirred overnight. The reaction mixture was diluted with THF. The insoluble inorganic salt was removed by filtration. Concentration of the filtrate yielded crude product, which was purified by column chromatography (DCM-MeOH) to yield a colorless oil (605 mg, 62.5%). Step 4: 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (B) 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (1.510 g, 1.501 mmol), bis(pinacolato)diboron (800 mg, 3.15 mmol), potassium acetate (619 mg, 6.31 mmol), Pd(dppf)Cl2 [1,1′-Bis(diphenylphosphino)ferrocene]dichloropalladium(II)] (51.5 mg, 0.063 mmol) and DMSO (30 mL) were mixed under N2. The mixture was heated at 80° C. for 5.5 hour. Upon completion, the DMF was distilled and water (50 mL) was added. The product was extracted with DCM (3×40 mL). The organic layers were combined and concentrated. The crude product was purified by column chromatography (DCM-MeOH) to give colorless oil (1.015 g, 63%). Example 1b: Polymerization of Monomers (A) and (B) 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) (0.084 mmol, 120 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (B) (0.088 mmol, 135 mg), and palladium tetra(triphenylphosphine) (0.0035 mmol, 4 mg) were combined in a round bottom flask equipped with a stirbar. Next, 0.35 mL of 2M potassium carbonate (aq) and 1.9 mL of tetrahydrofuran were added and the flask is fitted with a vacuum adaptor and put on a Schlenk line. The mixture was degassed using 3 freeze-pump-thaw cycles. The degassed mixture was heated to 80° C. under nitrogen with vigorous stirring for 18 hours. The reaction mixture was then cooled and the solvent removed with rotary evaporation. The resulting semisolid was diluted with ca. 50 mL water and filtered through glass fiber filter paper. Ethanol was added to adjust the solvent to 20% ethanol in water. Preparative gel permeation chromatography was performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions was removed with rotary evaporation and 100 mg of poly [2,7{9,9-bis (2, 5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene] was collected as an amber oil. Example 2: Synthesis of Asymmetric Polymers of Formula (I) Via Suzuki Coupling Example 2a: Synthesis of Asymmetric Monomer, 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (C) for Subsequent Polymerization Step 1: 2-dibromo-7-iodofluorene 2-bromofluorene (10.01 g, 40.84 mmol), acetic acid (170 mL), water (8 mL), iodine (4.34 g, 17.20 mmol), potassium iodate (2.18 g, 10.19 mmol) and sulfuric acid (4 mL) were mixed under nitrogen. The resulting mixture was heated at 80° C. for 2 h and cooled to room temperature. The formed precipitate which is the desired product was collected after filtration and acetic acid wash (13.68 g, 90%). Step 2: 2-dibromo-9,9-di(3′hydroxypropanyl)-7-iodofluorene 2-dibromo-7-iodofluorene (2.186 g, 5.892 mmol), tetrabutylammonium bromide (60 mg, 0.186 mmol), and DMSO (25 mL) were added to a 3-neck flask under nitrogen(g), followed by the addition of 50% NaOH (4 mL, 50 mmol) via syringe. The mixture was heated to 80° C., and 3-bromopropanol (1.33 mL, 14.7 mmol) was added slowly, and the reaction was stirred at 80° C. for another 1 hour. Upon completion, the mixture was cooled to room temperature and quenched with water. The precipitate as crude product was collected after filtration. The crude product was purified by column chromatography (eluant: hexane-ethylacetate) to give pale yellow solid (2.15 g, 75%). Step 3: 2-bromo-9,9-di(3′-hydroxypropanyl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene 2-dibromo-9,9-di(3′hydroxypropanyl)-7-iodofluorene (2.454 g, 5.037 mmol), bis(pinacolato)diboron (1.407 g, 5.541 mmol), potassium acetate (1.483 g, 15.11 mmol), Pd(dppf)Cl2 (123 mg, 0.15 mmol) and DMSO (25 mL) were mixed under N2. The mixture was heated at 80° C. for 1.5 hour. Upon completion, the mixture was cooled to room temperature and quenched with water (50 mL). The product was extracted with DCM (3×40 mL). The organic layers were combined and concentrated. The crude product was purified by column chromatography (eluant: hexane-ethylacetate) to give pale solid (2.09 g, 85%). Step 4: 2-bromo-9,9-di(3′-methanesulfanotopropanyl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene 2-bromo-9,9-di(3′-hydroxypropanyl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (2.280 g, 4.694 mmol) and p-toluenesulfonyl chloride (2.684 g, 14.08 mmol) were dissolved in dichloromethane at room temperature under N2. Triethylamine (3.95 mL, 28.2 mmol) was added slowly via syringe. The mixture was stirred at room temperature over night. The mixture was then concentrated and purified by column chromatography (Hexane-EtOAc) to yield pale solid (2.66 g, 72%). Step 5: 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorine (C) mPEG11 alcohol (3.331 g, 6.448 mmol) was dissolved in anhydrous THF (20 mL) at 0° C. under nitrogen. To the mixture, was added potassium tert-butoxide (7.74 mmol, 7.74 mL, 1M in THF). After 10 min stirring, 2-bromo-9,9-di(3′-methanesulfanotopropanyl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorine (2.052 g, 2.579 mmol) in 20 mL of anhydrous THF was added via a syringe. The mixture was allowed to room temperature and stirred overnight. After evaporation of THF, brine (50 mL) was added and crude product was extracted with dichloromethane (3×40 mL). The combined organic layers were concentrated and purified by column chromatography (DCM-isopropanol) to give colorless gel-like product (2.164 g, 57%). Example 2b: Synthesis of an Asymmetric Polymer Via Suzuki Coupling Polymerization Asymmetric polymers are synthesized using conditions similar to polymerization conditions as described in Example 1b. Example 3: Synthesis of a Linker or Capping Unit Example 3a: Synthesis of Linker or Capping Unit, Tert-Butyl 4-(3,5-Dibromophenoxy)Butylcarbamate Step 1: 4-(3,5-dibromophenoxy)butan-1-amine 1-(4′-phthalimidobutoxy)3,5-dibromobenzene (1.0 g, 2.20 mmol) was dissolved in ethanol (45 mL) for 5 minutes under nitrogen. Hydrazine monohydrate (610 mg, 12.1 mmol) was added and the reaction was refluxed at 80° C. for 2 hours. To the reaction aqueous 1M HCl (17.7 mL, 17.7 mmol) was added and refluxed at 105° C. for another 2 hours. The aqueous layer was extracted with dichloromethane (2×150 mL). The organic layers were combined, washed with saturated NaHCO3 (3×), water, and brine, then dried over MgSO4, and filtered. Removal of solvent yielded a yellow oil (560 mg, 78%). Step 2: Tert-butyl 4-(3,5-dibromophenoxy)butylcarbamate 4-(3,5-dibromophenoxy)butan-1-amine (397 mg, 1.23 mmol) was dissolved in anhydrous THF (24.6 mL) under nitrogen. Di-tert-butyl dicarbonate (423 mL, 1.84 mmol) was added to the mixture and refluxed reaction at 40° C. for 2 hours. After extraction of the reaction with dichloromethane (2×50 mL), the organic layers were combined, washed with saturated NaHCO3, water, and brine, then dried over MgSO4, and filtered. The solvent is removed and the residue is purified by column chromatography (9:1, hexanes: EtOAc) to give a white solid (306 mg, 59%). Example 3b: Synthesis of Linker or Capping Unit, Tert-butyl-4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butylcarbamate Step 1: 2,7-dibromo-9-methyl-9H-fluorene 2,7-dibromofluorene (30 g, 92.59 mmol) was dissolved in anhydrous THF (300 mL) under nitrogen and cooled to −78° C. To solution at −78° C., added n-butyllithium (40.36 mL, 100.9 mmol) over 5 minutes and allowed reaction stir for another 10 minutes. To reaction, then add methyl iodide (6.29 mL, 100.9 mmol) and allowed reaction to stir at −78° C. for 2.0 hours. The reaction was poured into a mixture of dichloromethane and water. The organic layer was collected, and the water layer was further extracted with dichloromethane. Combined all organic layers and removed solvent via vacuo. The crude material was triturated with hexanes and filtered using Buchner funnel to give white solids (22 g, 70%). 1H NMR (500 MHz, CDCl3): δ=7.62 (s, 2H), 7.56-7.58 (d, 2H), 7.48-7.50 (dd, 2H), 3.90-3.94 (q, 1H), 1.49-1.51 (d, 3H). Step 2: 2-(4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butyl)isoindoline-1,3-dione 2,7-dibromo-9-methyl-9H-fluorene (10.0 g, 29.58 mmol) was dissolved in 50 mL DMSO under nitrogen. To mixture was added KOH (2.01 g, 35.79 mmol), water (1.5 mL), N-(4-bromobutyl)phthalimide (9.93 g, 35.2 mmol), and stirred reaction at room temperature for 2.0 hours, then at 50° C. for 3.0 hours. The reaction was cooled to room temperature and diluted with dichloromethane. The organic layer was washed with brine (2λ), and water. Removal of solvent yield a solid, which was purified by column chromatography (7:3, hexanes:EtOAc) to yield white solids (3.08 g, 20%). 1H NMR (500 MHz, CDCl3): δ=7.81-7.83 (m, 2H), 7.68-7.71 (m, 2H), 7.48-7.51 (m, 4H), 7.41-7.44 (dd, 2H), 3.46-3.49 (t, 2H), 2.00-2.04 (p, 2H), 1.47-1.49 (m, 2H), 1.45 (s, 3H), 0.65-0.68 (m, 2H). Step 3: 4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butan-1-amine 2-(4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butyl)isoindoline-1,3-dione (3.08, 5.71 mmol) was dissolved in ethanol (250 mL) under nitrogen. To the mixture was added hydrazine monohydrate (2.77 mL, 57.1 mmol), and the reaction was refluxed at 80° C. for 3.0 hours. The reaction was cooled to room temperature, and added 1M HCl (˜100 mL). The mixture was stirred for 30 minutes or until all solids were dissolved. Dichloromethane was added to the solution and the organic layer was extracted with saturated NaHCO3 three times, and washed with water. The organic layers were collected and removed solvent by vacuo to give an yellow oil (2.33 g, 100%). 1H NMR (500 MHz, CD2Cl2): δ=7.57 (d, 2H), 7.52 (d, 2H), 7.46-7.48 (dd, 2H), 2.39-2.42 (t, 2H), 1.95-1.98 (t, 2H), 1.44 (s, 3H), 1.17-1.23 (m, 2H), 0.59-0.65 (m, 2H). Step 4: tert-butyl-4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butylcarbamate 4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butan-1-amine (2.39 g, 5.84 mmol) was dissolved in anhydrous THF (20 mL) under nitrogen. To solution, was added di-tert-butyl-dicarbonate (2.01 mL, 8.76 mmol), and the reaction was stirred at 40° C. for 3 hours. The reaction was cooled to room temperature and concentrated via vacuo. Crude solids were triturated with hexanes and filtered using buchner funnel to yield the desired white solids (2.34 g, 79%). 1H NMR (500 MHz, CDCl3): δ=7.53 (d, 2H), 7.45-7.47 (d, 4H), 4.30 (s, 1H), 2.88-2.90 (q, 2H), 1.93-1.96 (t, 2H), 1.43 (s, 3H), 1.41 (s, 9H), 1.25-1.28 (m, 2H), 0.59-0.66 (m, 2H). Example 4: Synthesis of a Linker or Capping Unit Example 4a: Synthesis of Tert-butyl 4-(4-bromophenoxy)butylcarbamate Step 1: N(4-(4-bromophenoxy)butyl)phthalimide Combined 4-bromophenol (4.64 g, 26.8 mmol), N-(4-bromobutylphthalimide) (6.30 g, 22.33 mmol), K2CO3 (11.09 g, 80.38 mmol), 18-crown-6 (265 mg, 1.00 mmol), and acetone (100 mL), and refluxed reaction under nitrogen at 70° C. over night. The reaction was cooled to room temperature and removed solvent by vacuum. The crude mixture was diluted with dichloromethane (200 mL) and washed with water (3×), then dried over MgSO4, and filtered. Removal of solvent, followed by trituration with hexanes, and filtered using Buchner funnel to yield a white solid (6.03 g, 71%). Step 2: 4-(4-bromophenoxy)butan-1-amine N(4-(4-bromophenoxy)butyl)phthalimide (6.01 g, 16.1 mmol) is dissolved in ethanol (200 mL) under nitrogen, followed by the addition of hydrazine monohydrate (7.8 mL, 161 mmol). The reaction was refluxed at 80° C. for 2 hours. Once reaction completed (solids formed at the top layer), cooled reaction to room temperature and neutralized with 1M HCl (50 mL). The mixture is allowed to stir until all solids are completely dissolved and diluted with dichloromethane (150 mL). The solution was extracted with two portions of saturated NaHCO3 (2×). The organic layers were combined, washed with brine and water, then dried over MgSO4, and filtered. Removal of solvent yields a yellow oil (2.93 g, 75%). Step 3: Tert-butyl 4-(4-bromophenoxy)butylcarbamate 4-(4-bromophenoxy)butan-1-amine (1.0 g, 4.09 mmol) was dissolved in anhydrous THF (20 mL) under nitrogen and stirred until solution is homogenous. Di-tert-butyl-dicarbonate (1.34 g, 6.14 mmol) was added and the reaction was stirred at 40° C. for 2 hours. The reaction was quenched with water (30 mL) and stirred at room temperature for 1.0 hour. The aqueous layer was extracted with ethyl acetate (50 mL×2). The organic layers were combined, washed with saturated NaHCO3, water, and brine, then dried over MgSO4, and filtered. Removal of solvent yield a solid, which was purified by column chromatography (9:1, hexanes:EtOAc) to yield white solids (1.0 g, 71%). Example 4b: Synthesis of tert-butyl 4-(4-bromophenyl)butanoate Allowed tert-butanol to melt and added 20 mL to round bottom flask. To the solution, added di-tert-butyl-dicarbonate (1.79 g, 8.22 mmol) and 4-(4-bromophenyl)butyric acid (1.0 g, 4.11 mmol). To reaction, then added DMAP (150.7 mg, 1.23 mmol) and stirred reaction at room temperature over night. The reaction was concentrated via vacuo, and re-diluted in ethyl acetate. The organic layer was washed with 1M HCl, brine, and water. After removal of solvent, the crude solids were purified via column chromatography (20:1, hexanes:EtOAc) to give the desired product (570 mg, 46%), which is a clear oil. 1H NMR (500 MHz, CD2Cl2): 5=7.39-7.41 (d, 2H), 7.03-7.09 (d, 2H), 2.57-2.60 (t, 2H), 2.18-2.21 (t, 2H), 1.83-1.186 (p, 2H), 1.42 (s, 9H). Example 4c: Synthesis of 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid Combined 4-(4-bromophenyl)butyric acid (10 g, 41.13 mmol), bis(pinacolato)diboron (15.67 g, 61.70 mmol), potassium acetate (12.11 g, 123.4 mmol), and DMSO (100 mL), and purged mixture with nitrogen for 10 minutes at room temperature. To reaction under nitrogen, added Pd(dppf)Cl2 and purged reaction again with nitrogen for another 20 minutes at room temperature. The reaction was then refluxed at 80° C. over night. After cooling to room temperature, the reaction was quenched with water and stirred for 1.0 hour. The solids formed were filtered using Buchner funnel. The crude solids were purified via column chromatography (8.5:1.5, hexanes:EtOAc). The desired fractions were collected and concentrated via vacuo, and triturated with hexanes and filtered to give the desired white solids (6.7 g, 56%). Example 5: Synthesis of Linker or Capping Unit, Tert-butyl 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenoxy)butylcarbamate Combined tert-butyl 4-(4-bromophenoxy)butylcarbamate from Example 4a (500 mg, 1.45 mmmol), potassium acetate (428 mg, 4.36 mmol), bis(pinacolato)diboron (737 mg, 2.90 mmol) and DMSO (12 mL), and purged mixture with nitrogen for 10 minutes at room temperature. To mixture was added Pd(dppf)Cl2 (59.3 mg, 0.07 mmol) and continued to stir solution at room temperature under nitrogen for another 20 minutes. After refluxing at 80° C. for 3 hours, the reaction was cooled to room temperature and quenched with water (30 mL). The aqueous layer was extracted with dichloromethane (50 mL×2). The organic layers were combined, washed with brine, then dried over MgSO4, and filtered. Removal of solvent yield a dark brown oil, which was purified by column chromatography (9:1, hexanes:EtOAc) to yield a light yellow oil (539 mg, 95%). Example 6: Synthesis of Linker or Capping Unit with Long Oligoether Spacer Between Arylhalide Phenyl and FMOC Protected Primary Amine 4-(4-bromophenoxy)butan-1-amine+oligoether-FMOC+N,N′-dicyclohexylcarbodiimide (DCC) (9H-fluoren-9-yl)methyl 80-(4-bromophenoxy)-75-oxo-3,6,9,12,15,18,21,24,27,30,33,36,39,42,45,48,51,54,57,60,63,66,69,72-tetracosaoxa-76-azaoctacontylcarbamate. 4-(4-bromophenoxy)butan-1-amine (21.5 mg, 0.09 mmol), 1-(9H-fluoren-9-yl)-3-oxo-2,7,10,13,16,19,22,25,28,31,34,37,40,43,46,49,52,55,58,61,64,67,70,73,76-pentacosaoxa-4-azanonaheptacontan-79-oic acid (100 mg, 0.073 mmol), and N,N′-dimethylaminopyridine (5.4 mg, 0.044 mmol) were combined in a round bottom flask flushed with nitrogen and charged with a Teflon stirbar. Next 5 mL of anhydrous dichloromethane was added via syringe. N,N-Dicyclohexylcarbodiimide (23 mg, 0.11 mmol) is transferred to a second flask flushed with nitrogen and charged with a stirbar and 5 mL of anhydrous dichloromethane is added via syringe. While stirring the first solution, add the dicyclohexylcarbodiimide solution slowly, dropwise. The reaction is then allowed to proceed overnight. The following day solids from the reaction were filtered off and the filtrate was concentrated onto silica. Column chromatography in methanol and dichloromethane gave a clear thick oil (83.3 mg, 71% yield). Example 7: Synthesis of Polymer, Poly[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene}-co-3,5-phenylbut-V-oxy-4″-amine], with an Internal Linking Site The incorporation of internal conjugation sites into conjugated polymer backbones is described in U.S. application Ser. No. 11/868,870, filed Oct. 8, 2007 and published as U.S. Application No. 2008/0293164, which application is herein incorporated by reference in its entirety. Provided is a modified synthesis based on the protocol. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.084 mmol, 120 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (0.088 mmol, 135 mg), tert-butyl-4-(3,5-dibromophenoxy)butylcarbamate (0.0044 mmol, 2.0 mg), and palladium tetra(triphenylphosphine) (0.0035 mmol, 4 mg) are combined in a round bottom flask equipped with a stirbar. Next, 0.35 mL of 2M potassium carbonate (aq) and 1.9 mL of tetrahydrofuran are added and the flask is fitted with a vacuum adaptor and put on a Schlenk line. The mixture is degassed using 3 freeze-pump-thaw cycles. The degassed mixture is heated to 80 C under nitrogen with vigorous stirring for 18 hours. The reaction mixture is then cooled and the solvent is removed with rotary evaporation. Next, 4 mL of 4 M HCl in dioxane is added and the mixture is stirred for no less than 4 hours. The solution is neutralized with 2M potassium carbonate solution. The bulk of the solvent is again removed with rotary evaporation. The resulting semisolid is diluted with ca. 50 mL water and filtered through glass fiber filter paper. Ethanol is added to adjust the solvent to 20% ethanol in water. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and 100 mg of poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene}-co-3,5-tert-butyl-4-(4-bromophenoxy)amine] is collected as an amber oil. Example 8: Synthesis of Phenylene Vinylene Co-Polymer with an Internal Linking Site A modified synthesis similar to that described in Examples 7 and 15. Example 9: Synthesis of Polymer with Exclusively Terminal Amine Capping Units 2,7-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene])-diphen-4-oxybutyl-4′-amine 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.163 mmol, 235 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (0.163 mmol, 250 mg), and palladium tetra(triphenylphoshine) (0.0065, 7.5 mg) are combined in a round bottom flask equipped with a stirbar. Next, 0.75 mL of 2M potassium carbonate (aq) and 3 mL of tetrahydrofuran are added and the flask is fitted with a vacuum adaptor. The reaction mixture is put on a Schenk line and is degassed with three freeze-pump-thaw cycles and then heated to 80 C under nitrogen with vigorous stirring for 18 hours. A solution of tert-butyl 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenoxy)butylcarbamate (0.064 mmol, 25 mg) in 0.5 mL tetrahydrofuran is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction is allowed to continue for an additional 4 hours at 80 C with stirring. Next, a solution of tert-butyl 4-(4-bromophenoxy)butylcarbamate (0.192 mmol, 66 mg) in 0.5 mL of THF is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction was allowed to proceed overnight. The reaction mixture was allowed to cool and solvent was removed with rotary evaporation. A 4 mL portion of 4M HCl in dioxane was added to the residue and stirred for a minimum of 4 hours. The solution was neutralized with 2 M potassium carbonate (aq) and then the solvent was removed under vacuum. The resulting residue was diluted to −30 mL with 20% ethanol in water and filtered. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and 337 mg of polymer is collected as an amber oil. The order of end linker addition (aryl hylide or boronic ester/acid) can be reversed. Similar processes can be used to add alternative linkers or end capping units. Example 10: Synthesis of Polymer, 2-(Poly [2,7{9,9-Bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene])-phen-4-oxybutyl-4′-amine, Statistically Enriched in Chains with a Single Terminal Amine Capping Unit 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.163 mmol, 235 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (0.163 mmol, 250 mg), and palladium tetra(triphenylphoshine) (0.0065, 7.5 mg) are combined in a round bottom flask equipped with a stirbar. Next, 0.75 mL of 2M potassium carbonate (aq) and 3 mL of tetrahydrofuran are added and the flask is fitted with a vacuum adaptor. The reaction mixture is put on a Schenk line and is degassed with three freeze-pump-thaw cycles and then heated to 80 C under nitrogen with vigorous stirring for 18 hours. A solution of tert-butyl 4-(4-bromophenoxy)butylcarbamate (0.049 mmol, 17 mg) in 0.5 mL tetrahydrofuran is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction is allowed to continue for an additional 4 hours at 80 C with stirring. Next, a solution of phenylboronic acid (0.150 mmol, 18 mg) in 0.5 mL of THF is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction was allowed to proceed overnight. The reaction mixture was allowed to cool and solvent was removed with rotary evaporation. A 4 mL portion of 4M HCl in dioxane was added to the residue and stirred for a at least 4 hours. The solution was neutralized with 2 M potassium carbonate (aq) and then the solvent was removed under vacuum. The resulting residue was diluted to −30 mL with 20% ethanol in water and filtered. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and 315 mg of polymer is collected as an amber oil. Resulting polymers contain chains with an enriched fraction of chains with one amine linker plus chains with 2 linkers and no linkers. Example 11: Synthesis of Polymer Statistically Enriched in Chains with a Single Terminal Capping Unit with a Long Oligoether Spacer (24 Repeats) Between the Polymer Chain and the Primary Amine Linking Group 2-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene])-phen-4-oxybutyl-4′-amine. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.163 mmol, 235 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (0.163 mmol, 250 mg), and palladium tetra(triphenylphoshine) (0.0065, 7.5 mg) are combined in a round bottom flask equipped with a stirbar. Next, 0.75 mL of 2M potassium carbonate (aq) and 3 mL of tetrahydrofuran are added and the flask is fitted with a vacuum adaptor. The reaction mixture is put on a Schenk line and is degassed with three freeze-pump-thaw cycles and then heated to 80 C under nitrogen with vigorous stirring for 18 hours. A solution of tert-butyl 4-(4-bromophenoxy)butylcarbamate (0.049 mmol, 17 mg) in 0.5 mL tetrahydrofuran is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction is allowed to continue for an additional 4 hours at 80 C with stirring. Next, a solution of phenylboronic acid (0.150 mmol, 18 mg) in 0.5 mL of THF is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction was allowed to proceed overnight. The reaction mixture was allowed to cool and solvent was removed with rotary evaporation. A 4 mL portion of 4M HCl in dioxane was added to the residue and stirred for a minimum of 4 hours. The solution was neutralized with 2 M potassium carbonate (aq) and then the solvent was removed under vacuum. The resulting residue was diluted to −30 mL with 20% ethanol in water and filtered. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and 315 mg of polymer is collected as an amber oil. Example 12: Synthesis of an Asymmetric Polymer with a Terminal Carboxylic Capping Unit Added During Polymerization Reaction The linking monomer is added during the polymerization reaction as described in Examples 9, 10 and 11. The carboxylic acid group can later be converted to an activated ester such as N-hydroxysuccinimidyl as is described in Example 29. Example 13: Synthesis of an Asymmetric Polymer with a Terminal Carboxylic Acid Capping Unit Added Post Polymerization The linking monomer is added after the polymerization reaction is completed and polymer purified. Linker addition is done under similar reaction conditions as those described in Examples 9, 10 and 11. The carboxylic acid group can later be converted to an activated ester such as N-hydroxysuccinimidyl as is described in Example 29. Example 14: Synthesis of an Polymer with Branched PEG Groups Example 14a: Synthesis of Monomers, (D) and (E) for Subsequent Polymerization Step 1: 2,7-dibromo-9,9-bis(3,5-dimethoxybenzyl)fluorene 2,7-dibromofluorene (4.16 g, 12.8 mmol) and tetrabutylammonium bromide (362 mg, 1.12 mmol) were added to a round bottom flask charged with a Teflon stirbar. Next, 60 mL of dimethylsulfoxide was added to the flask and the mixture was stirred for 5 minutes. A portion of 50% NaOH aqueous solution (5.2 mL) was added followed immediately by 3,5-dimethoxybenzyl bromide (7.14 g, 31 mmol). Over the course of 2 hours the solution changes color from orange to blue. The reaction is stirred overnight. The resulting mixture is slowly poured into 200 mL of water and then extracted with three 100 mL portions of dichloromethane. The organic layers are combined and dried over magnesium sulfate and then filtered. The crude product is purified by column chromatography using hexanes and dichloromethane as eluent to give a pale yellow solid (6.63 g, 79% yield). Step 2: 2,7-Dibromo-9,9-Bis(3,5-Dihydroxybenzyl)-9H-Fluorene 2,7-dibromo-9,9-bis(3,5-dimethoxybenzyl)-9H-fluorene (1.3 g, 2.08 mmol) was added to a round bottom flask charged with a stirbar and equipped with a rubber septum. The flask is purged with nitrogen for 10 min. Anhydrous dichloromethane (20 mL) is transferred to the flask via cannula and the mixture is stirred until the solids are completely dissolved. The solution is then cooled with a dry ice/acetone bath for 10 minutes. BBr3 (6.1 mL, 63.3 mmol) is added dropwise via cannula with constant stirring. The bath is allowed to warm to room temperature and the mixture is stirred overnight. The reaction is quenched with the slow addition of 125 mL of water. The solution is then extracted with 3 portions of ethyl acetate (50 mL). The organic layer is dried over MgSO3, filtered, and dried onto silica. Flash chromatography of the crude using ethyl acetate in dichloromethane gives an off-white crystalline solid (800 mg, 68% yield). Step 3: 2,7-dibromo-9,9-bis(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl) benzyl)-9H-fluorene (D) 2,7-dibromo-9,9-bis(3,5-dihydroxybenzyl)-9H-fluorene (537 mg, 0.945 mmol), 2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 4-methylbenzenesulfonate (2.788 g, 4.156 mmol), potassium carbonate (1.57 g, 11.34 mmol) and acetone (80 mL) are transferred to a round bottom flask charged with a Teflon stirbar and equipped with a reflux condenser. The mixture is refluxed with constant stirring overnight. The mixture is then allowed to cool to room temperature and the acetone is removed under vacuum. After extracting with 3 portions of dichloromethane, the organic layer is dried over MgSO4, filtered, and the filtrate is concentrated onto silica. Column chromatography using methanol and dichloromethane affords the product as a slightly colored thick oil (1.69 g, 70% yield). Step 4: 2,7- di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)-9,9-bis(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl) benzyl)-9H-fluorene (E) Monomer (E) is synthesized using conditions similar to conditions as described in Example 1. Example 14b: Polymerization of (D) and (E) Polymerization of (D) and (E) are polymerized using conditions similar to polymerization conditions as described in Example 1b. Example 15: Synthesis of a Neutral Base Phenylene Vinylene Co-Polymer 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.25 mmol), 1,4-divinylbenzene (32.3 mg, 0.25 mmol), palladium acetate (3 mg, 0.013 mmol), tri-ortho-tolylphosphine, (10 mg, 0.033 mmol), and potassium carbonate (162 mg, 1.2 mmol) are combined with 5 mL of DMF in a small round bottom flask charged with a Teflon coated stirbar. The flask is fitted with a needle valve and put in a Schlenk line. The solution is degassed by three cycles of freezing, pumping, and thawing. The mixture is then heated to 100° C. overnight. The polymer can be subsequently reacted with terminal linkers or capping units using similar (in situ) protocols to those provided in the previous examples (9, 10 and 11) or by modifying them post polymerization work up as a separate set of reactions. Example 16: Synthesis of a Branched Phenylene Vinylene Co-Polymer 2,7-dibromo-9,9-bis(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl) benzyl)-9H-fluorene (636 mg, 0.25 mmol), 1,4-divinylbenzene (32.3 mg, 0.25 mmol), palladium acetate (3 mg, 0.013 mmol), tri-ortho-tolylphosphine, (10 mg, 0.033 mmol), and potassium carbonate (162 mg, 1.2 mmol) were combined with 5 mL of DMF in a small round bottom flask charged with a Teflon coated stirbar. The flask was fitted with a needle valve and put in a Schlenk line. The solution was degassed by three cycles of freezing, pumping, and thawing. The mixture was then heated to 100° C. overnight. The polymer can be subsequently reacted with terminal linkers or capping units using similar (in situ) protocols to those provided in Example 5 or by modifying them post polymerization work up as a separate set of reactions. Example 17: Synthesis of a Branched Phenylene Vinylene Co-Polymer with Functional Amines for Covalent Conjugation. Poly [2,7-divinyl{9,9-bis(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl)benzyl)-9H-fluorene}-alt-1,4-benzene-co-4-phenoxybutyl-N-t-butylcarbamate] Step 1: Polymerization 2,7-dibromo-9,9-bis(3,5-(2,5, 8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl) benzyl)-9H-fluorene (636 mg, 0.25 mmol), 1,4-divinylbenzene (32.3 mg, 0.25 mmol), palladium acetate (3 mg, 0.013 mmol), tri-ortho-tolylphosphine, (10 mg, 0.033 mmol), and potassium carbonate (162 mg, 1.2 mmol) were combined with 5 mL of DMF in a small round bottom flask charged with a Teflon coated stirbar. The flask was fitted with a needle valve and put in a Schlenk line. The solution was degassed by three cycles of freezing, pumping, and thawing. The mixture was then heated to 100° C. overnight. Step 2: Linker Addition The next morning divinylbenzene (10 mg, 0.077 mmol) was transferred to a small round bottom flask with 1 mL of DMF. The flask was fitted with a needle valve and put in a Schlenk line. The solution was degassed by three cycles of freezing, pumping, and thawing. The solution was transferred via cannula through the needle valves and into the polymerization reaction. After this addition the reaction was allowed to continue at 100° C. overnight. The next day tert-butyl 4-(4-bromophenoxy)butylcarbamate (53 mg, 0.15 mmol) and 1 mL of DMF were transferred to a small round bottom flask. The flask was fitted with a needle valve and put in a Schlenk line. The solution was degassed by three cycles of freezing, pumping, and thawing. The solution was transferred via cannula through the needle valves and into the polymerization reaction. After this addition the reaction was allowed to continue at 100° C. overnight. Step 3: Work up The reaction is then cooled and diluted with 100 mL of water. The aqueous solution was filtered twice through G-6 glass fiber filter paper. The filtrate was evaporated to dryness and re-diluted with dichloromethane. The organic layer was dried over MgSO4 and filtered. The filtrate was evaporated to yield an amber colored oil (342 mg, 56% yield). A 4 mL portion of 4M HCl in dioxane was added to the polymer residue and stirred for a minimum of 4 hours. The solution was neutralized with 2 M potassium carbonate (aq) and then the solvent was removed under vacuum. The resulting residue was diluted to −30 mL with 20% ethanol in water and filtered. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and the polymer is collected as an amber oil. The linker or capping unit addition steps can be performed in the polymerization reaction as presented above or alternatively, in some embodiments, can be performed in a separate set of reactions after the polymerization work up. In the latter case, the polymer is reacted under the analogous conditions as those provided in the example. In other embodiments, it is also possible to react with a combination of terminal monomers to introduce polymers with bi-functionality, allowing the polymer to be conjugated to more than one entity. Example 18: Synthesis of a Fluorene Monomer with Glycerol-Based Dendrimers Step 1 Dimethyl 3,3′-(2,7-dibromo-9H-fluorene-9,9-diyl)dipropanoate. 2,7-Dibromofluorene (1 g, 3.1 mmol), methyl acrylate (861 mg, 10 mmol) tetrabutylammonium bromide (100 mg, 0.3 mmol) and toluene (5 mL) were added to a small round bottom flask with a Teflon-coated stirbar. Next 2 mL of 50% NaOH (aq) is added while stirring. The reaction is allowed to proceed overnight. The next day the toluene layer is transferred to a flask and the aqueous layer extracted with two portions of toluene. The organic layers are combined, dried with Mg2SO4, and filtered. Silica (2 g) is added to the filtrate and the solution is evaporated. The product is obtained as a white solid (1.23 g, 80% yield) after purification by column chromatography. Step 2 3,3′-(2,7-dibromo-9H-fluorene-9,9-diyl)dipropanoic acid. Dimethyl 3,3′-(2,7-dibromo-9H-fluorene-9,9-diyl)dipropanoate (1.23 g, 2.5 mmol) is transferred to a small round bottom flask equipped with a Teflon-coated stirbar. A mixture of THF:MeOH:H2O, 3:2:1, (10 mL) is added and the mixture is stirred for 1 hr. Then a 1 mL portion of 1M NaOH (aq) is added and the mixture is stirred overnight. The next day the water layer is isolated and extracted with 20 mL portions diethyl ether three times. Next the water layer is acidified to ˜pH 2. The water layer is extracted three times with 20 mL portions of dichloromethane. The organic layers are combined and dried with Mg2SO4. The organic solution is filtered and the solvent evaporated to obtain the product as an off-white solid (948 mg, 90% yield). Step 3 3,3′-(2,7-Dibromo-9H-fluorene-9,9-diyl)bis(N-(7,15-bis((2,3-dihydroxypropoxy)methyl)-1,3,19,21-tetrahydroxy-5,9,13,17-tetraoxahenicosan-11-yl)propanamide). 3,3′-(2,7-Dibromo-9H-fluorene-9,9-diyl)dipropanoic acid (500 mg, 1.1 mmol), 11-amino-7,15-bis((2,3-dihydroxypropoxy)methyl)-5,9,13,17-tetraoxahenicosane-1,3,19,21-tetraol (1.954, 3.3 mmol) (prepared as per ref. Heek, T.; Fasting, C.; Rest, C.; Zhang, X.; Wurthner, F.; Haag, R. Chem. Commun., 2010, 46, 1884-1886), and N,N′-dimethylaminopyridine (61 mg, 0.5 mmol) are combined in a round bottom flask equipped with a Teflon-coated stirbar and sealed with a rubber septum. The flask was flushed with N2 and 10 mL of anhydrous dichloromethane was added via syringe. The mixture is stirred to dissolve the solids. In another round bottom flask equipped with a Teflon-coated stirbar, dicyclohexylcarbodiimide (DCC, 910 mg 4.4 mmol) transferred and the flask is sealed with a rubber septum. Next, 5 mL of anhydrous dichloromethane is transferred to the flask via syringe. The DCC solution is transferred to the fluorene reaction mixture via a syringe dropwise. The reaction is allowed to react overnight. The next day the reaction mixture is filtered. The filtrate is purified by column chromatography to afford a clear oil (1.24 g, 70% yield). Example 19: Synthesis of a Fluorene Monomer PAMAM-Based Dendritic Side Chain Capped with methylPEG Chains Step 1: 9,9′-(3,3′-Diamido(tetramethyl PAMAM G[2])-2,7-dibromofluorene (i) Dimethyl 3,3′-(2,7-dibromo-9H-fluorene-9,9-diyl)dipropanoate (1 g, 2.0 mmol) is transferred to a round bottom flask equipped with a stirbar and sealed with a rubber septum. The flask is flushed with nitrogen and 10 mL of dry methanol is transferred to the flask via syringe and the solid is dissolved by stirring. Ethylenediamine (5.5 mL, 82 mmol) is added via syringe slowly and the mixture is allowed to stir for 2 hours. The septum is removed and the methanol and unreacted ethylenediamine is removed under vacuum. Another 10 mL portion of methanol is added and stirred and then was evaporated to remove any remaining ethylenediamine. The residue remaining in the flask was then sealed again with a septum, flushed with nitrogen, and dry methanol (10 mL) was added and stirred. Methyl acrylate (7.2 mL, 80 mmol) is added slowly via syringe and the mixture is allowed to stir for 2 hours. The septum is again removed and the methanol and methyl acrylate are removed under vacuum. A 10 mL portion of toluene is added, the mixture stirred, and the solvent removed under vacuum affording an off-white solid (1.79 g, quantitative yield). Step 2: 9,9′-(3,3′-Diamido(PAMAM G[2] tetraacid)-2,7-dibromofluorene (ii) 9,9′-(3,3′-Diamido(tetramethyl PAMAM G[2])-2,7-dibromofluorene (i) (1.79 g, 2 mmol) is transferred to a small round bottom flask equipped with a Teflon-coated stirbar. A mixture of THF:MeOH:H2O, 3:2:1, (10 mL) is added and the mixture is stirred for 1 hr. Then a 1 mL portion of 1M NaOH (aq) is added and the mixture is stirred overnight. The next day the water layer is isolated and extracted with 20 mL portions diethyl ether three times. Next the water layer is acidified to ˜pH 2. The water layer is extracted three times with 20 mL portions of dichloromethane. The organic layers are combined and dried with Mg2SO4. The organic solution is filtered and the solvent evaporated to obtain the product as an off-white solid (1.51 g, 90% yield). Step 3: 9,9′-(3,3′-Diamido(PAMAM G[2] N-(2,5,8,11,14,17,20,23-octaoxapentacosan-25-yl)propionamidyl)-2,7-dibromofluorene (iii) 9,9′-(3,3′-Diamido(PAMAM G[2] tetraacid)-2,7-dibromofluorene (ii) (500 mg, 0.6 mmol), 2,5,8,11,14,17,20,23-octaoxapentacosan-25-amine (1.15 g, 3 mmol)), and N,N′-dimethylaminopyridine (12 mg, 0.1 mmol) are combined in a round bottom flask equipped with a Teflon-coated stirbar and sealed with a rubber septum. The flask was flushed with N2 and 10 mL of anhydrous dichloromethane was added via syringe. The mixture is stirred to dissolve the solids. In another round bottom flask equipped with a Teflon-coated stirbar, dicyclohexylcarbodiimide (DCC, 825 mg 4.0 mmol) transferred and the flask is sealed with a rubber septum. Next, 5 mL of anhydrous dichloromethane is transferred to the flask via syringe. The DCC solution is transferred to the fluorene reaction mixture via a syringe dropwise. The reaction is allowed to react overnight. The next day the reaction mixture is filtered. The filtrate is purified by column chromatography to afford a clear oil (967 g, 70% yield). Example 20: Synthesis of a Fluorene Monomer with Highly Branched PEGylated Side Chains Based on a Trihydroxybenzene Linkage Step 1: Methyl 3,4,5-tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)benzoate (iv) Methyl 3,4,5-trihydroxybenzoate (200 mg, 1.1 mmol), 2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 4-methylbenzenesulfonate (2.58 g, 3.85 mmol), and 18-crown-6 (100 mg, 0.38 mmol) are transferred to a round bottom flask equipped with a Teflon-coated stirbar. Acetone (10 mL) is added and the flask is equipped with a reflux condenser. The mixture is refluxed with constant stirring overnight. The next day silica (4 g) is added and the solvent evaporated. After purification by column chromatography, a clear oil is obtained (887 mg, 48% yield). Step 2: 3,4,5-Tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)-N-(2-aminoethyl)benzamide (v) Methyl 3,4,5-tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)benzoate (iv) (887 mg, 0.52 mmol) flask is transferred to a round bottom flask equipped with a stirbar and sealed with a rubber septum. The flask is flushed with nitrogen and 10 mL of dry methanol is transferred to the flask via syringe and the solid is dissolved by stirring. Ethylenediamine (0.7 mL, 10.4 mmol) is added via syringe slowly and the mixture is allowed to stir for 2 hours. The septum is removed and the methanol and unreacted ethylenediamine is removed under vacuum. The product is obtained as an oil (886 mg, quanitative yield). Step 3:]3,3′-(2,7-Dibromo-9H-fluorene-9,9-diyl)bis(N-(2-3,4,5-tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)-benzamidyl-N amidoethyl)propanamide) (vi) 3,4,5-Tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)-N-(2-aminoethyl)benzamide (v) (886 mg, 0.52 mmol), 3,3′-(2,7-Dibromo-9H-fluorene-9,9-diyl)dipropanoic acid (112 mg, 0.24 mmol), and N,N′-dimethylaminopyridine (12 mg, 0.1 mmol) are combined in a round bottom flask equipped with a Teflon-coated stirbar and sealed with a rubber septum. The flask was flushed with N2 and 10 mL of anhydrous dichloromethane was added via syringe. The mixture is stirred to dissolve the solids. In another round bottom flask equipped with a Teflon-coated stirbar, dicyclohexylcarbodiimide (DCC, 148 mg 0.72 mmol) transferred and the flask is sealed with a rubber septum. Next, 5 mL of anhydrous dichloromethane is transferred to the flask via syringe. The DCC solution is transferred to the fluorene reaction mixture via a syringe dropwise. The reaction is allowed to react overnight. The next day the reaction mixture is filtered. The filtrate is purified by column chromatography to afford a clear oil (924 mg, 70% yield). Example 21. Dual End Capped Polymer Used to Create a Polymer-Dye Label for Biomolecule or Substrate Conjugation Step 1: Synthesis of an Asymmetric Neutral Water-Soluble Polymer with a t-BOC Protected Amine Pendant Group at One Terminus of the Polymer 2-bromo-7-(4″-phenoxybutyl-1-tert-butyl carbamate)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (1.0 g, 0.674 mmol), 3 mL of tetrahydrofuran, and 2 mL of 2M potassium carbonate (aqueous) were transferred to a small round bottom flask charged with a Teflon stirbar. The flask was fitted with a septum and the solution is degassed by sparging with Ar for 15 minutes. Palladium tetra(triphenylphoshine) (15.6 mg, 0.013 mmol) was added through the neck of the flask and the flask was transferred to a reflux condenser equipped with a needle valve and fixed to a Schlenk line. The solution was quickly frozen solid with liquid nitrogen and was further degassed using freeze-pump-thaw technique. Once degassed the reaction was heated to 80° C. with constant stirring. The reaction was allowed to proceed overnight. The next day tert-butyl 4-(4-bromophenoxy)butylcarbamate (35 mg, 0.10 mmol) in 1 mL of THF was degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction continued overnight at 80° C. The next day the reaction mixture was cooled and the bulk of the solvent was removed under vacuum. The remaining material was transferred to a small Erlenmeyer flask with a total of −50 mL of dichloromethane. The solution was stirred for 30 minutes. Approximately 1 g of MgSO4(anhydrous) was added to the solution and the mixture was filtered through a fluted paper filter. The filtrate was evaporated and 410 mg (47% yield) of an amber oil was collected. Step 2: Synthesis to Append a Terminal Linking Monomer with a t-Butyl Ester at the Terminus Opposite the Protected Amine Pendant 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-tert-butyl carbamate)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene 2-Bromo-7-(4″-phenoxybutyl-1-tert-butyl carbamate)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene (410 mg, 0.32 mmol of repeat unit), tert-butyl 1-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenoxy)-3,6,9,12,15,18,21-heptaoxatetracosan-24-oate (33 mg, 0.048 mmol), 2 mL of tetrahydrofuran, and 1.5 mL of 2M potassium carbonate (aqueous) were transferred to a small round bottom flask charged with a Teflon stirbar. The flask was fitted with a septum and the solution is degassed by sparging with Ar for 15 minutes. Palladium tetra(triphenylphoshine) (15 mg, 0.013 mmol) was added through the neck of the flask and the flask was transferred to a reflux condenser equipped with a needle valve and fixed to a Schlenk line. The solution was quickly frozen solid with liquid nitrogen and was further degassed using freeze-pump-thaw technique. Once degassed the reaction was heated to 80° C. with constant stirring. The reaction was allowed to proceed overnight. The remaining material was transferred to a small Erlenmeyer flask with a total of −50 mL of dichloromethane. The solution was stirred for 30 minutes. Approximately 1 g of MgSO4(anhydrous) was added to the solution and the mixture was filtered through a fluted paper filter. The filtrate was evaporated and 351 mg (78% yield) of an amber oil was collected. Step 3: Synthesis of a Neutral Water-Soluble Polymer with Primary Amine at One Terminus and a t-Butyl Ester Pendant on the Other 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-amino)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-tert-butyl carbamate)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene (23 mg, 0.018 mmol) and 0.5 mL of 4M HCl in dioxane were combined in a 1 dram vial with a Teflon-coated stirbar. The mixture was stirred for 4 hours. The mixture was neutralized with 2M potassium carbonate (aqueous). The solution was then diluted to 50 mL of roughly 20% ethanol in water and filtered through G-6 glass fiber filter paper. The filtrate was desalted by centrifugation in a 4 mL 10 KDa cutoff centrifuge filter. The retentate was evaporated under vacuum and two 1 mL portions of toluene were added and removed under vacuum to remove any remaining water. A thick amber liquid was recovered from the desalting (21 mg, 85% yield). Step 4 Attachment of an NHS-functionalized dye to a primary amine pendant on a neutral water-soluble polymer. 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-amido-DYE)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-amino)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene (518 ug, 0.4 μM) was dissolved in 100 μL of dry dichloromethane in a glass vial. A small crystal of 4-N,N′-dimethylaminopyridine was added. In another vial 65 μg (0.06 □uM) of NHS-functionalized DyLight 594 (Pierce) was dissolved in 50 of dry dichloromethane. The two solutions were combined and allowed to stir in a sealed vial for 4 hours covered in foil. The solvent was then evaporated and the remaining material was dissolved in 95% ethanol and injected onto a Sepharose 6 column. The remaining dye was separated from the polymer. A solution of dye-labeled polymer was obtained from combining fractions (˜100 μg, 20% yield). Step 5 Hydrolysis of the t-butyl ester pendant on the dye-labeled neutral water-soluble polymer to form the carboxylic acid pendant on one of the termini. 2-(4-(1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosane-27-acid))-7-(4″-phenoxybutyl-1-amido-DYE)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene The polymer was combined with ZnBr2 in dichloromethane and stirred overnight. The next day a portion of water was added and the mixture was stirred for 1 hour. The solvent was evaporated and the residue was dissolved in 20% ethanol in water. The filtrate was then desalted by centrifugation in a 4 mL 10 KDa cutoff centrifuge filter. The retentate was evaporated under vacuum and two 1 mL portions of toluene were added and removed under vacuum to remove any remaining water. Activation (for subsequent conjugation) of the second functional group in this example (carboxylic acid) can be achieved using a number of different methods including those described in Examples 29 and other examples with carboxylic acid to amine to maleimide. One such method is given below in Step 6, by way of example only. Step 6: NHS Activation of the Carboxylic Acid Penant of a Dye-Labeled Neutral Water-Soluble Polymer 2-(4-(1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosane-27-N-hydroxysuccinimidyl ester))-7-(4″-phenoxybutyl-1-amido-DYE)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene. 2-(4-(1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosane-27-acid))-7-(4″-phenoxybutyl-1-amido-DYE)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene and O—(N-Succinimidyl)-1,1,3,3-tetramethyluronium tetrafluoroborate and DIPEA are combined in dry acetonitrile and allowed to react under nitrogen for 30 min. The solution is evaporated and the solid is resuspended in dry dichloromethane. Solids are filtered off and the filtrate is evaporated to afford the NHS ester. In further embodiments, various commonly used protecting groups can be used with those functional groups provided (amine and carboxylic acid). Additionally different capping monomers and protecting group combinations can be used to produce polymers with different functional groups for conjugation. Eliminating or substituting the dye labeling step for another entity will result in a polymer with two different functional groups for conjugation. The dye attachment via NHS/amine chemistry can be performed under a variety of commonly used conditions. Dye attachment can also be performed with other functional chemistries. Example 22. Asymmetric Polyfluorene Synthesis Using Non-Regulated Suzuki Conditions Step 1: Polymerization Method A: A solution of K2CO3 in water (2M, 4 mL) was added to a stirred mixture of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (A) (2.3 g, 1.5 mmol) and THF (6 mL) in a round bottom flask. This mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (38.5 mg, 0.03 mmol) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. The reaction mixture was cooled to 23° C. and solvent removed by rotary evaporation. The resulting residue was transferred to an Erlenmeyer flask and diluted with 20% EtOH/H2O (75 mL). EDTA (300 mg, 1.0 mmol) was added to the mixture and stirred at 23° C. for 1 h. The mixture was filtered through a glass fiber filter paper and the filter paper rinsed with 20% EtOH/H2O. The resulting filtrate was then filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (regenerated cellulose Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until conductivity of the filtrate measured less than 0.01 mS/cm. The solvent was then removed under vacuum to give poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene] (B) as a gel-like product (1.41 g, 71%) Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=51,000, Mw=108,000, Mp=90,000, D=2.1). The extent of end linker incorporation was determined by first converting the acid to an NHS ester (similar protocol to that provided in Example 29) then reacting with an amine functional dye. After purification of free dye the ratio of dye to polymer was determined from absorbance measurements, factoring in the difference in extinction coefficients and polymer molecular weight. Method B: A solution of K2CO3 in water (2M, 4 mL) was added to a stirred mixture of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (A) (2.3 g, 1.5 mmol) and DMF (6 mL) in a round bottom flask. This mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (38.5 mg, 0.03 mmol) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. Work-up and purification was performed in a manner similar to previously described Method A. Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=96,000, Mw=231,000, Mp=185,000, D=2.4). Method C: Cs2CO3 (2.08 g, 6.4 mmol) was added to a stirred mixture of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (A) (200 mg, 0.135 mmol) and DMF (7 mL) in a round bottom flask. This mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (15.6 mg, 10 mol %) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. Work-up and purification was performed in a manner similar to previously described Method A. Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=95,000, Mw=218,000, Mp=206,000, D=2.3). Step 2: End Capping -(4-iodophenyl)butanoic acid (227 mg, 0.783 mmol) was washed into a flask containing poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene] (B) (1.00 g, 0.783 mmol) using THF (3.5 mL). A solution of K2CO3 in water (2M, 2.3 mL) was added to the flask and this mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (36 mg, 4 mol %) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. The reaction mixture was cooled to 23° C. and the solvent removed with rotary evaoporation. The resulting residue was transferred to an Erlenmeyer flask and diluted with 20% EtOH/H2O (150 mL). EDTA (500 mg) was added to the mixture and stirred at 23° C. for 1 h. The mixture was filtered through a glass fiber filter paper and the filter paper rinsed with 20% EtOH/H2O. The resulting filtrate was then filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (regenerated cellulose Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until conductivity of the filtrate measured less than 0.01 mS/cm. The solvent was then removed under vacuum to give 4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)phenyl)butanoic acid (C) as a gel-like product (388 mg, 39%) Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=89,000, Mw=196,000, Mp=124,000, D=2.2). The extent of end linker incorporation was determined by first converting the acid to an NHS ester (similar protocol to that provided in Example 29) then reacting with an amine functional dye. After purification of free dye the ratio of dye to polymer was determined from absorbance measurements, factoring in the difference in extinction coefficients and polymer molecular weight. Step 3: Amine Activation 4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)phenyl)butanoic acid (C) (200 mg, 0.156 mmol) was dissolved in 2 mL ethanol, then added drop-wise to 23 mL of MES buffer (50 mM, pH 5) at 4° C. while stirring. N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride (576 mg, 3.00 mmol) was added in portions, followed by N-hydroxy succinimide (115 mg, 1.00 mmol) in one portion. The solution was stirred for 30 minutes, ethylene diamine (0.501 mL, 7.50 mmol) was added drop-wise and the reaction mixture was stirred overnight at room temperature. The reaction mixture was then desalted over a G25 desalting column and the solvent removed via rotary evaporation to give N-(2-aminoethyl)-4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)butanamide as a clear yellow oil (190 mg, 95%). Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=89,000, Mw=196,000, Mp=124,000, D=2.2). Extent of amine conversion was determined by reacting the amine polymer with an NHS active dye in similar fashion as that described in Example 38. Example 23. Asymmetric Polyfluorene Synthesis Using Linker Modified End Caps to Regulate the Suzuki Polymerization Step 1: Polymerization/End Capping/Work-up A solution of K2CO3 in water (2M, 4 mL) was added to a stirred mixture of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (A) (2.3 g, 1.55 mmol), 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid (B) (6.7 mg, 2 mol %), and DMF (6 mL) in a round bottom flask equipped with a side-arm stopcock. This mixture was degassed with argon for 25 min. Palladium tetrakis(triphenylphosphine) (38.5 mg, 2 mol %) was then added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was further degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. Separately, 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid (B) (230 mg, 0.793 mmol) was dissolved in DMF (3 mL) in a found bottom flask equipped with a side arm stopcock. This solution was sparged with argon for 15 minutes, attached to a reflux condenser, and degassed via three freeze-pump thaw cycles. Upon thawing the solution was added to the reaction mixture after two hours of reaction time using an argon flushed syringe. The reaction mixture was stirred for an additional 12 h at 80° C. The reaction mixture was cooled to 23° C. and solvent removed with rotary evaporation. The resulting residue was transferred to an Erlenmeyer flask and diluted with 20% EtOH/H2O (75 mL). EDTA (300 mg, 1.00 mmol) was added to the mixture and stirred at 23° C. for 1 h. The mixture was filtered through a glass fiber filter paper and the filter paper rinsed with 20% EtOH/H2O. The resulting filtrate was then filtered through a 0.45 um cup filter. The filtered reaction mixture was purified and size fractionated using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 30,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until conductivity of the filtrate measured less than 0.01 mS/cm and Mn of the retentate measured more than 70,000 by GPC. The solvent was then removed under vacuum to give 4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)phenyl)butanoic acid as a gel-like product (1.41 g, 71%). Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=68,000, Mw=134,000, Mp=122,000, D=1.9). The extent of end linker incorporation was determined by first converting the acid to an NHS ester (similar protocol to that provided in Example 29) then reacting with an amine functional dye. After purification of free dye the ratio of dye to polymer was determined from absorbance measurements, factoring in the difference in extinction coefficients and polymer molecular weight. Despite having a molecular weight in excess of 50,000 g/mole the polymer is soluble in both water and phosphate buffered saline solutions at concentrations easily greater than 10 mg/mL. In many conjugation experiments the polymer provided (and other described herein with similar structure) was concentrated to 50 mg/mL or higher which is remarkable for a neutral conjugated polymer. The moderate molecular weight also provides extinction coefficients greater than 2,500,000 M−1 cm−1. The large extinction coefficient and quantum yield of 60% (PBS) provide for exceptionally bright fluorescent reporters for use in biological assays including their use in flow cytometry. Step 2: Amine Activation 4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)phenyl)butanoic acid (C) (500 mg, 0.13 mmol) was dissolved in 2 mL ethanol, then added drop-wise to 23 mL of MES buffer (50 mM, pH 5) at 4° C. while stirring. N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride was added in portions, followed by N-hydroxy succinimide (0.52 g) in one portion. The solution was stirred for 30 minutes, ethylene diamine (2.8 mL) was added drop-wise and the reaction mixture was stirred overnight at room temperature. The reaction mixture was then desalted over a G25 desalting column and the solvent removed via rotary evaporation to give N-(2-aminoethyl)-4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)butanamide as a yellow oil (450 mg, 90%). Extent of amine conversion was determined by reacting the amine polymer with an NHS active dye in similar fashion as that described in Example 38. Example 24. Yamamoto Polymerization of PEG Modified Polyfluorene Step 1 Yamamoto Polymerization/Work-up In a dry box, Ni(COD)2(0.387 g, 1.41 mmol), 2,2′-bipyridyl (0.220 g, 1.41 mmol), COD (0.152 g, 1.41 mmol) and anhydrous DMF (16 ml) were added to a long-neck round bottom flask. [00251] 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) (1.00, 0.696) was weighed into a 40 ml vial and dissolved in anhydrous DMF (8 ml). The flask was sealed with a septum and the vial was closed with a septum screw cap. The catalyst mixture and the monomer solution were transferred out of the dry box and were placed under static argon. The reaction flask was heated to 70° C. for 45 min. The monomer solution was then was quickly transferred from the vial to the catalyst mixture flask with an argon flushed syringe. The reaction mixture was then heated to 70° C. for 6 h. The reaction mixture was cooled and solvent removed by rotary evaporation. The resultant black residue was re-dissolved in 20% EtOH (80 mL) and centrifuged at 2400 rpm for 12 hours. The supernatant was then decanted and filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until GPC analysis of retentate indicated the absence of low molecular weight material. The solvent was then removed under vacuum to give poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene] (B) as a viscous oil (0.700 g, 79%) Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=62,000, Mw=127,000, Mp=93,000, D=2.0). Step 2 End Capping: End capping is performed in a manner similar to Example 22, Step 2. Step 3 Amine Activation: Amine activation is performed in a manner similar to Example 22, Step 3. Example 25. Synthesis of a Tandem Polymer with Two Different Linkers Step 1: Polymerization In a dry box, Ni(COD)2 (0.765 g, 2.78 mmol), 2,2′-bipyridyl (0.435 g, 2.78 mmol), COD (0.301 g, 2.78 mmol) and anhydrous DMF (20 ml) were added to a long-neck round bottom flask. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) (1.80, 1.26 mmol) and tert-butyl 4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butylcarbamate (B) (0.071 g, 0.126 mmol) were added to a 40 ml vial and dissolved in anhydrous DMF (30 ml). The flask was sealed with a septum and the vial was closed with a septum screw cap. The catalyst mixture and the monomer solution were transferred out of the dry box and were placed under static argon. The reaction flask was heated to 70° C. for 45 min. The monomer solution was then was quickly transferred from the vial to the catalyst mixture flask with an argon flushed syringe. The reaction mixture was then heated to 70° C. for 6 h. The reaction mixture was cooled and solvent removed by rotary evaporation. The resultant black residue was re-dissolved in 20% EtOH (80 mL) and centrifuged at 2400 rpm for 12 hours. The supernatant was then decanted and filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until GPC analysis of retentate indicated the absence of low molecular weight material. The solvent was then removed under vacuum to give 2,7-dibromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)] (C) as a viscous oil (1.3 g, 45%) Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=72,000, Mw=156,000, Mp=138,000, D=2.1). Step 2: End Capping A solution of K2CO3 in water (2M, 4 mL) was added to a stirred mixture of 2,7-dibromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)] (C) (800 mg, 0.67 mmol), 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid (D) (120 mg, 0.41 mmol), and DMF (6 mL) in a round bottom flask. This mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (50 mg, 6 mol %) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. The reaction mixture was cooled to 23° C. and concentrated in vacuo to a volume of 2 mL. The crude reaction mixture was transferred to an Erlenmeyer flask and diluted with 20% EtOH/H2O (75 mL). EDTA (300 mg, 2.00 mmol) was added to the mixture and stirred at 23° C. for 1 h. The mixture was filtered through a glass fiber filter paper and the filter paper rinsed with 20% EtOH/H2O. The resulting filtrate was then filtered through a 0.45 um cup filter. The filtered reaction mixture was purified and size fractionated using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until conductivity of the filtrate measured less than 0.01 mS/cm. The solvent was then removed under vacuum to give 4-(4-(2-bromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)])phenyl)butanoic acid (E) as a yellow oil (660 mg, 82%). Step 3: Linker Deprotection Trifluoroacetic acid (4 mL) was added dropwise to a stirred solution of 4-(4-(2-bromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)])phenyl)butanoic acid (E) (200 mg, 0.169 mmol) and dichloromethane (16 mL) in a round bottom flask. The reaction mixture was stirred at room temperature for 2 hours and then concentrated in vacuo. The residue was redissolved in minimal 20% EtOH and 1M HCl was added to the solution until pH=7. The neutralized solution was then desalted over G25 gel and the resultant material was concentrated to dryness to yield a clear pale yellow oil (F). Examples of dye incorporation, linker activation and bioconjugation are contained in further Example 38 and related examples. Example 26: Synthesis of a Tandem Polymer with Two Different Linkers Using End Capping Units to Regulate the Polymerization Reaction Step 1: Yamamoto Polymerization In a dry box, Ni(COD)2 (0.433 g, 8.40 mmol), 2,2′-bipyridyl (0.246 g, 8.40 mmol), COD (0.170 g, 8.40 mmol) and anhydrous DMF (15 ml) were added to a long-neck round bottom flask. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) (1.00, 0.696 mmol), tert-butyl 4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butylcarbamate (B) (0.037 g, 0.069 mmol), and tert-butyl 4-(4-bromophenyl)butanoate (C) (0.004 g, 0.007 mmol) were added to a 40 ml vial and dissolved in anhydrous DMF (10 ml). The flask was sealed with a septum and the vial was closed with a septum screw cap. The catalyst mixture and the monomer solution were transferred out of the dry box and were placed under static argon. The reaction flask was heated to 70° C. for 45 min. The monomer solution was then was quickly transferred from the vial to the catalyst mixture flask with an argon flushed syringe. The reaction mixture was then heated to 70° C. for 6 h. The reaction mixture was cooled and solvent removed by rotary evaporation. The resultant black residue was re-dissolved in 20% EtOH (80 mL) and centrifuged at 2400 rpm for 12 hours. The supernatant was then decanted and filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until GPC analysis of retentate indicated the absence of low molecular weight material. The solvent was then removed under vacuum to give tert-butyl 4-(4-(2-bromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)])phenyl)butanoate (D) as a viscous oil (664 g, 80%). Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=50,000, Mw=88,000, Mp=174,000, D=1.8). Step 2: Linker Deprotection Trifluoroacetic acid (6 mL) was added dropwise to a stirred solution of Polymer (300 mg, X mmol) and dichloromethane (24 mL) in a round bottom flask. The reaction mixture was stirred at room temperature for 2 hours and then concentrated in vacuo. The residue was redissolved in minimal 20% EtOH and 1M HCl was added to the solution until pH=7. The neutralized solution was then desalted over G25 gel and the resultant material was concentrated to dryness to yield a clear pale orange oil (261 mg, 87%). Examples of dye incorporation, linker activation and bioconjugation are contained in further Example 38 and related examples. Example 27. Dual Functional Asymmetric Polymer with Both Internal and Terminal Conjugation Sites Used to Create a Polymer-Dye Label for Biomolecule or Substrate Conjugation Suzuki polymerization of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-′7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene is performed under those conditions described in Example 23 where y % is the mol % of the end linker used to regulate the polymerization and ensure high incorporation of linker. The linker in this example is 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid. In this example, x mol % of the internal linker is also added to the polymerization to incorporate the second linking site into the polymer. This method for incorporating the internal linker is generally described in Examples 21, 25 and 26. The internal linker must be incorporated during the polymerization as indicated, however, it is expected that it would be possible to add the terminal linker as a separate step as described in Examples 9, 10, 11 and 21. Example 28: Enrichment of Linker-Functionalized Polymers The synthesis of linker-functionalized polymers can yield a mixture of chains with and without linker functionalities. Because conjugation efficiency is expected to improve with higher purity polymers for conjugation, the methods described in this example address this by enriching for chains containing linker. For a polymer batch containing a mixture of a COOH-modified and unmodified polymer: Dissolve polymer in 95% EtOH, then dilute with water to a final EtOH concentration of 20%. Desalt the polymer using 10 kDa MWCO filter until conductance is <0.1 mS/cm. Inject onto Q-Sepharose column, ensuring that the polymer load is suitable for the column capacity. Pass 20% EtOH in water over column to wash out unbound polymer. Release bound material by changing the eluting buffer to 1M NaCl in 20% EtOH in water for two column volumes to trigger the release of the bound polymeric material. Collect enriched material. The polymer is passed over a strong anion exchanger such as a Q-Sepharose column. Polymer chains bearing a functional carboxylic acid group will bind the strong anion exchanger, and polymer that is not functionalized will not bind and instead will wash through. After the non-functionalized polymer has passed through the column, the column is washed with 1M NaCl, which triggers the release of the acid-functionalized polymer by screening the acid group from the media. By using this method, the percent functional polymer has been shown to increase from 25% of polymer chains bearing a carboxylic acid group to >80% of polymer chains bearing a carboxylic acid group. This increase in functional chains has been shown by analyzing the absorbance ratios of polymer-dye conjugates pre- and post-enrichment. This procedure is also described in Example 38. A similar process has been validated for the enrichment of amine containing polymers. In that case an anionic exchange resin, SP Sephrose (or similar), is loaded at reduced conductivity (below 0.01 mS/cm). Example 29: Preparation of Polymer-Streptavidin Conjugates Via NHS/Amine Coupling Example 29a: Polymer Modifications Polymer Modification—Carboxylic Acid to Amine Conversion 1.35 g of a carboxylic acid terminated polymer was dissolved at in 9 mL ethanol, then added dropwise to 80 mL of 4° C. 50 mM IVIES, pH 5 while stirring. 0.52 g N-hydroxy succinimide was added in one portion. Once the N-hydroxy succinimide had dissolved, 2.3 g N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride was added in portions. After stirring the solution for 30 minutes, 2.8 mL of ethylene diamine was added dropwise. The solution was stirred overnight at room temperature and purified by tangential flow filtration (MWCO=10 kDa). 1.22 g yield (90%). Polymer Modification—Amine to Carboxylic Acid Conversion 70 mg of an amine-terminated polymer was dissolved in 7 mL DMSO. 2.3 mg DIPEA was added to the polymer solution. 2.2 mg DMAP was dissolved in 220 μL DMSO and added to the resulting polymer solution. 5.5 mg succinic anhydride was dissolved in 550 μL DMSO and added to the resulting polymer solution. The solution was agitated at room temperature overnight. The reaction was then purified over Amicon Ultra centrifugal filtration units (MWCO=10 kDa) with 25 mM IVIES pH 5 buffer. 62 mg yield (89%). Polymer Modification—Carboxylic Acid to NETS-Ester Conversion 60 mg of a carboxylic acid-terminated polymer was dissolved in 600 μL acetonitrile. 1.2 μg DIPEA was added to the polymer solution. 2.8 mg N,N,N′,N′-Tetramethyl-O—(N-succinimidyl)uronium was dissolved in 370 μL acetonitrile and added to the polymer solution. The solution was agitated at room temperature for 15 minutes. After the reaction is complete, the solvent was evaporated under reduced pressure. 50 mg yield (83%). Example 29b: Protein-Polymer Conjugation Streptavidin protein is dissolved in 50 mM NaHCO3 pH 8.2 buffer to make a 1 mg/mL solution. Crude activated polymer (10-15 eq or as required) solution from Step 2 is added to the aqueous streptavidin protein solution; the protein concentration is adjust with buffer to ensure that the volume of organic solvent added is <10% of the total volume, if necessary. The solution is agitated at room temperature for 3 hr and the reaction transferred to a Amicon Ultra filter (MWCO=10 kDa) to remove DMF. The protein is recovered into the initial volume with 25 mM PO4 pH 6.5 buffer. Purification of the Protein-Polymer Conjugate A 1 mL HiTrap SP Sepharose FF column is equilibrated with 20 mM Na Citrate pH 3 buffer. 1 mL (0.3-1 mg/mL) of Streptavidin-polymer conjugate is loaded in 25 mM NaHPO4 pH 6.5. The sample is wash through column with 20 mM Na Citrate pH 3 buffer until a stable baseline is obtained. Multiple 1 mL aliquots of sample may subsequently be loaded and washed. The column is washed with a minimum of 10 column volumes of 20 mM Na Citrate pH 3 buffer. The conjugate is eluted with 10 column volumes of 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer and the column is stripped with 10 column volumes of 20% ethanol in the elution buffer. The elution peak is concentrated with an Amicon Ultra filter (MWCO=10 kDa) to reduce the volume to ˜200 μl. A 10×300 mm Superose 12 column is equilibrated with 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer. 200 μL of concentrated Streptavidin-polymer conjugate is loaded and eluted with 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer. Fractions are pooled and buffer exchanged into PBS+0.05% NaN3 using Amicon Ultra Centrifugation filters (10 kD MWCO). Elutions are concentrated to desired concentration for testing; at around 2 μM Streptavidin. Characterization of a Purified Protein-Polymer Conjugate A 4-20% acrylamide Tris-HCl Ready Gel (BioRad) is prepared and the gel is loaded with the conjugate along with free streptavidin and free polymer in separate lanes. Gel electrophoresis is performed in 25 mM Tris 192 mM, Glycine pH 8.3 and stained with Coomassie to visualize the protein. The gel is stained for 30 minutes then destained with commercial destain overnight. Agarose gel conditions were also used to characterize polymer-streptavidin conjugates, an example which is shown in FIG. 29. In alternative embodiments, the above example can be adapted to allow for conjugation of the polymer to biomolecules or dyes, including but not limited to, antibodies and nucleic acids. The amine on the polymer is converted to a maleimide and a carboxylic acid (further activated to form the NHS ester) using alternative crosslinkers or modifiers. In certain embodiments, conjugation of the same polymer to other biomolecules (streptavidin, antibody fragments, nucleic acids) is facilitated using malimide-thiol chemistry (using SATA linkers to convert free amines on the biomolecule or TCEP (or DPP) reduction of an antibody to create free thiols). Example 30: Preparation of Polymer-Streptavidin Conjugates Via Hydrazide/Benzaldehyde Coupling Step 1: Streptavidin-4FB Modification Streptavidin protein is reconstituted at 1.7 mg/mL and exchange into reaction buffer, 50 mM NaHCO3, pH 8. 15 molar equivalents of bifunctional benzaldehyde/succinimidyl linker, S-4FB (Solulink, San Diego, Calif.) 20 mg/mL in anhydrous DMSO is added to streptavidin, ensuring that the organic phase is less than 10% of the total volume. Reaction is mixed on shaker for 4 hours at room temperature and unreacted linker is subsequently filtered away via Amicon Ultra filter, 10 kD MWCO with 50 mM IVIES buffer, pH 5; centrifuged at 2400 rpm and a repeated wash ×3. Streptavidin protein is recovered in its initial volume, targeting 1.7 mg/mL in conjugation buffer, 50 mM NaPO4, pH 6.5. Step 2: Polymer Modification Polymer with terminal amine group (1 molar eq) is dissolved with DMF to make a 10 mg/mL solution. 20 molar equivalents of a bifunctional hydrazine/succinimidyl linker, SHTH (Solulink, San Diego, Calif.) at 80 mg/mL in anhydrous DMSO is added to the polymer solution. 1 drop of DIPEA is added to the reaction by a syringe and 22 g needle. The solution is agitated at room temperature for 4 hr and the reaction transferred to a Amicon Ultra filter (MWCO=10 kDa) filled with 25 mM MES pH 5 buffer. The solution is then centrifuged. The filter is refilled and washed with the following wash buffers: 1x DI H2O+1 drop 1 M HCl 1x DI H2O+1 drop 1M NaOH 3x 50 mM MES, pH 5 Step 3: Protein-Polymer Conjugation 15 equivalents of modified polymer from Step 2 are added with desired amount of modified protein from Step 1. Aniline is added to the reaction for a final concentration of 10 mM and allowed to mix for 12 hours. The reaction is purified with Amicon Ultra filter (MWCO=10 kDa) to remove DMF and recovered with 25 mM PO4 pH 6.5 buffer. Step 4: Purification of the Protein-Polymer Conjugate A 1 mL HiTrap SP Sepharose FF column is equilibrated with 20 mM Na Citrate pH 3 buffer. 1 mL (0.3-1 mg/mL) of Streptavidin-polymer conjugate is loaded in 25 mM NaHPO4 pH 6.5. The sample is wash through column with 20 mM Na Citrate pH 3 buffer until a stable baseline is obtained. Multiple 1 mL aliquots of sample may subsequently be loaded and washed. The column is washed with a minimum of 10 column volumes of 20 mM Na Citrate pH 3 buffer. The conjugate is eluted with 10 column volumes of 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer and the column is stripped with 10 column volumes of 20% ethanol in the elution buffer. The elution peak is concentrated with an Amicon Ultra filter (MWCO=10 kDa) to reduce the volume to ˜200 μl. A 10×300 mm Superose 12 column is equilibrated with 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer. 200 μL of concentrated Streptavidin-polymer conjugate is loaded and eluted with 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer. Fractions are pooled and buffer exchanged into PBS+0.05% NaN3 using Amicon Ultra Centrifugation filters (10 kD MWCO). Elutions are concentrated to desired concentration for testing; at around 2 μM Streptavidin. Step 5: Characterization of a Purified Protein-Polymer Conjugate A 4-20% acrylamide Tris-HCl Ready Gel (BioRad) is prepared and the gel is loaded with the conjugate along with free streptavidin and free polymer in separate lanes. Gel electrophoresis is performed in 25 mM Tris 192 mM, Glycine pH 8.3 and stained with Coomassie to visualize the protein. The gel is stained for 30 minutes then destained with commercial destain overnight. FIG. 14 top, depicts conjugation of streptavidin to a polymer of formula (Vb) in cartoon format. FIG. 14, bottom, is a Coomassie stain of acrylamide gel which depicts the mobility of the conjugate is retarded relative to the free protein indicating an increase in mass. A neutral polymer alone shows no evidence of staining and without a formal charge, the polymer is not mobile in the electrophoritic field. In alternative embodiments, the above example can be adapted to allow for conjugation of the polymer to biomolecules or dyes, including but not limited to, antibodies and nucleic acids. The amine on the polymer is converted to a maleimide and a carboxylic acid (further activated to form the NHS ester) using alternative crosslinkers or modifiers. In certain embodiments, conjugation of the same polymer to other biomolecules (streptavidin, antibody fragments, nucleic acids) is facilitated using malimide-thiol chemistry (using SATA linkers to convert free amines on the biomolecule or TCEP reduction of an antibody to create free thiols) and NETS-amine chemistry (reacting the NETS polymer directly with lysines on the protein or nucleic acid). Example 31: Preparation of Biotin-Labeled Polymers Amine functionalized polymer of formula (Vc) is dissolved at 10 mg/mL in anhydrous DMF and divided into two portions. NHS-biotin (0.9 mg in 90 μL, 88 equivalents) (Pierce, 20217) and NHS-LC-LC-biotin (Pierce, 21343) at 10 mg/mL (1.5 mg in 150 μL, 88 equivalents) are dissolved in anhydrous DMF. The NHS-biotin and NHS-LC-LC-biotin solutions are immediately added to the two portions of polymer solution and allowed to mix on a shaker overnight in the dark. Excess reactant is removed by washing the solution using Amicon Ultra-4 mL 10 kD MWCO filter cartridges in a series of wash steps: First, the cartridge is first filled approximately halfway with water, and the reaction solution (by pipet) subsequently added directly into the water. Next, the cartridge is filled with water until it is full. The solution is mixed by pipetting up and down. Then, the cartridge is centrifuged at 2400 rpm for 30 minutes, or until the volume is reduced to 250 μL. The cartridge is then refilled with water 1 drop of 1M HCl is added; the solution is mixed, and centrifuged at 2400 rpm for 30 minutes, or until the volume was reduced to 250 μL. Next, the cartridge is refilled with water, 1 drop of 1M NaOH is added; the solution is mixed, and centrifuged at 2400 rpm for 30 minutes, or until the volume is reduced to 250 μL. The cartridge is then refilled with water, mixed and centrifuged at 2400 rpm for 30 minutes, or until the volume is reduced to 250 μL. This final step is repeated for a total of 5 washes. Characterization of a Purified Biotin-Labeled Polymer Excess biotin-labeled polymer is incubated with a Cy5-labeled streptavidin in DPBS buffer plus 0.2% BSA and 0.05% NaN3. A 0.8% agarose gel is is prepared and the gel is loaded with the conjugate along with free Cy5-streptavidin and free biotinylated polymer in separate lanes. Gel electrophoresis is performed in 10 mM NaHCO3 pH10 and and visualized using a Typhoon gel imager with 457 nm and 635 nm laser excitation. FIG. 15 (bottom) depicts retardation of mobility of the polymer-streptavidin complex relative to the free protein indicating an increase in mass. The polymer alone shows little mobility on its own due to a lack of formal charge. This protocol is adapted to successfully biotin-modify a range of conjugated polymers containing both internal and terminal amine linkers. Example 32: Functional Testing of Covalent Polymer Streptavidin Conjugates by Selective Binding to Biotinylated Microspheres Materials Required: 1x TBST: 50 mM Tris-HCl, 150 mM NaCl, 0.1% Tween20, pH 7.5; Biotin microspheres (10 mg/mL in TBST); BSA (1 mg/mL); AvDN (220 μM); and Polymer-Strepavidin (SA) conjugate: (1 μM with regard to SA, provided at 5 μM). Preparation of Master Mixes: Prepare in Labelled 1.5 mL Microfuge Tubes: Experimental Negative control master mix master mix 14 μl TBST 9 μl TBST 6 μl BSA stock 6 μl BSA stock 5 μl bead stock 5 μl avidin stock 5 μl bead stock Briefly vortex both tubes and allow 20-30 minutes to pre-incubate the negative control beads with excess avidin before proceeding. A variable speed orbital mixer at 800 RPM for incubation is suggested to keep beads from settling. Bead Hybridization: Pipette 10 μL of each master mix into separate labelled 1.5 ml microfuge tubes. Add 2 μL of polymer-SA conjugate to each. Prepare additional tube containing 10 μL master mix and no polymer to be used as a blank. Briefly vortex and pulse spin all tubes. Transfer to variable speed orbital mixer and incubate for 30 mins at 800 RPM. Bead Processing/Washing: Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 480 μl supernatant being diligent not to disturb bead pellet. Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 500 μl supernatant being diligent not to disturb bead pellet. Repeat steps 3 and 4. Remove as much of remaining supernatant as possible using P200 pipette without disturbing bead pellet. Add 100 μL TBST and vortex briefly to re-suspend beads. Bead Measurement: Transfer 100 μL of positive, negative and blank beads to a BLACK 96 well plate. Excite wells at 430 nm and collect emission in the range 450-650 nm using required slit widths and/or sensitivity setting to achieve measurable signals above background. Compare emission of positive and negative control beads. FIG. 16 shows the polymer streptavidin conjugate was bound to a biotinylated microsphere. Excitation at 440 nm in a florometer resulted in emission from the polymer as indicated by the solid curve. The dashed curve represents the negative control where the biotin bead was first treated with excess avidin to block the biotin binding sites prior to treatment with the polymer streptavidin conjugate. Example 33: Functional Testing of Covalent Polymer Streptavidin Conjugates by Selective Binding to Biotinylated Microspheres and FRET to Dye Acceptors on Co-Localized Streptavidin-Dye Conjugates Materials Required: 1x TBST: 50 mM Tris-HCl, 150 mM NaCl, 0.1% Tween20, pH 7.5. Biotin microspheres (10 mg/mL in TBST). Cy3-SA (1 μM or 50 μg/mL). Polymer-Strepavidin (SA) conjugate: (1 μM with regard to SA, provided at 5 μM). Bead Preparation and Hybridization: Prepare in labelled 1.5 mL microfuge tubes: Blank control Cy3-SA control FRET-SA Control 16 μl TBST 14 μl TBST 14 μl TBST 4 μl bead stock 2 μl Cy3-SA stock 2 μl Cy3-SA stock 4 μl bead stock 2 μl polymer-SA stock 4 μl bead stock Briefly vortex all tubes and transfer to variable speed orbital mixer for incubation of at least 30 mins at 800 RPM. Bead Processing/Washing: Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 480 μl supernatant being diligent not to disturb bead pellet. Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 500 μl supernatant being diligent not to disturb bead pellet. Repeat steps 3 and 4. Remove as much of remaining supernatant as possible using P200 pipette without disturbing bead pellet. Add 100 μL TBST and vortex briefly to re-suspend beads. Bead Measurement: Transfer 100 μL of all samples to a BLACK 96 well plate. Excite wells at 430 nm and collect emission in the range 450-650 nm using required slit widths and/or sensitivity setting to achieve measurable signals above background. Detect and record polymer emission in the range of 480-500 nm and Cy3 emission at the expected 570 nm. FIG. 17 shows the polymer streptavidin conjugate was bound to a biotinylated microsphere. Excitation at 440 nm in a florometer resulted in energy transfer between the polymer and a Cy3 dye conjugated to a different streptavidin protein as indicated by the solid upper curve. The dashed curve shows beads alone and the lower solid curve direct excitation of the Cy3-streptavidin conjugate at 440 nm. Example 34: Functional Testing of Biotin-Labeled Polymers by Selective Binding to Avidin Coated Microspheres Materials Required: 1x TBST: 50 mM Tris-HCl, 150 mM NaCl, 0.1% Tween20, pH 7. SA microspheres (10 mg/mL in TBST). Biotin (1 mM). 440 nm biotin-polymer conjugate: (46 μM). Bead Preparation and Hybridization: Prepare in labelled 1.5 mL microfuge tubes: Blank control Negative control Positive Control 16 μl TBST 11 μl TBST 15 μl TBST 4 μl bead stock 4 μl biotin stock 4 μl bead stock 4 μl bead stock Briefly vortex all tubes and transfer to variable speed orbital mixer for incubation of 20-30 mins at 800 RPM to ensure biotin has blocked all SA sites on negative control beads. Add 1 uL of polymer-biotin stock to both positive and negative control tubes. Vortex briefly and transfer to variable speed orbital mixer and incubate for 30 mins at 800 RPM. Bead Processing/Washing: Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 480 μl supernatant being diligent not to disturb bead pellet. Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 500 μl supernatant being diligent not to disturb bead pellet. Repeat steps 3 and 4. Remove as much of remaining supernatant as possible using P200 pipette without disturbing bead pellet. Add 100 μL TBST and vortex briefly to re-suspend beads. Bead Measurement: Transfer 100 μL of all samples to a BLACK 96 well plate. Excite wells at 430 nm and collect emission in the range 450-650 nm using required slit widths and/or sensitivity setting to achieve measurable signals above background. Compare emission of positive and negative control beads. FIG. 18 shows the biotin modified polymer was bound to a streptavidin microsphere (top). In FIG. 18 (bottom), excitation at 440 nm in a florometer resulted in emission from the polymer as indicated by the solid upper curve. The lower solid curve represents the negative control where the streptavidin bead was first treated with excess biotin to block the binding sites prior to treatment with the biontinylated polymer. The lower solid curve represents beads alone. Example 35: Selective Binding of Biotin-Labeled Polymer to Dye-Labeled SA Conjugates to Validate FRET Properties and Functional Activity of the Polymer Modification Materials Required: Biotin-Polymer Conjugate: (46 μM). Cy3-SA conjugate (1 mg/mL or 18.9 μM). BLACK 96-well plate. Forming the Biotin-Streptavidin Complex: In a 1.5 mL microfuge tube, combine 9.4 μL of the biotin-polymer conjugate and 2.9 μL of the Cy3-SA. Vortex to mix, then incubate on a shaker (under foil) for 0.5 h. Longer incubation times are also suitable. Instrument Settings: Model experiments were conducted on a BioTek Synergy 4 in the Fluorescence mode with the following settings: Emission: 400-750 nm in 5 nm steps and Sensitivity level: 50. Plate Layout: Prepare solutions in a BLACK 96-well plate as in the below table. Take care to add the A+B solution last, after all other materials have been added: Material Well 1 Well 2 Well 3 Polymer-biotin 9.4 μL* 9.4 μL — Cy3-SA 2.9 μL* — 2.9 μL Buffer 100 μL 100 μL 100 μL *Pre-incubated in the first step, Forming the Biotin-Streptavidin Complex. FIG. 19 shows the biotin modified polymer was bound to a dye labeled streptavidin (Cy3 or Texas Red—top). Excitation at 440 nm in a florometer resulted in emission from the dye acceptors at their respective emission wavelength (approximately 570 nm and 620 nm respectively—bottom left) as well as some residual emission from the polymer (approximately 520 nm). A titration was also performed to saturate the binding of polymer to the streptavidin (bottom right). The solid curve indicates the emission from the Cy3 label on the streptavidin via energy transfer from the polymer at 440 nm excitation. The dotted curve represents the negative control where the streptavidin was first treated with excess biotin to block the binding sites prior to treatment with the biontinylated polymer. Example 36: Polymer-Streptavidin Conjugates for Use in Flow Cytometry Polymer bioconjugates are evaluated by Stain Index, as defined by Becton Dickinson (BD) Biosciences on a flow cytometer. See, e.g., H. Maeker and J. Trotter, BD Biosciences Application Note: “Selecting Reagents for Multicolour Flow Cytometry”, September 2009. The stain index reports a measure of the polymer's brightness, nonspecific binding and can also be related by the Resolution Index on a flow cytometer. Flow cytometry provides a method through which to measure cells of a specific phenotype or analytes of interest on specific microspheres. This can be done with direct labeling of a primary antibody or, if signal amplification is desired, through a secondary antibody or the avidin-biotin complexation with avidin-polymer conjugates. Procedure for Cell Staining Cells of interest are taken up in sufficient quantity, at least 105 per test condition. Cells are then spun down at 250 rcf for 3 minutes, washed in DPBS+0.2% BSA and 0.05% NaN3 (staining buffer), then resuspended in staining buffer at 1×107 cells/mL. For primary incubation, cells are incubated with a primary conjugate (reporter labeled antibody) specific to an antigen of interest, negative cells serve as a negative non-specific binding reference. A control population or an established commercial conjugate is used as a positive control. Primary polymer conjugates are incubated at 4° C. with 4×105 cell aliquots at concentrations with volume dilutions from 10-330 nM for 30 minutes. Following primary incubation, cells are rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse is repeated three times. Cells are resuspended for testing at 8×105 cells/mL in DPBS+0.2% BSA, 0.05% NaN3. For secondary antibody labeling, an unlabeled primary antibody to the antigen of interest is incubated at 0.4 ug/uL, or other titrated amount, at 4° C. with 4×105 cells per test condition for 30 min. Following primary incubation, cells are rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse is repeated three times. Species reactive secondary polymer conjugates are incubated at 4° C. with 4×105 cell aliquots at concentrations with volume dilutions from 10-330 nM for 30 minutes. Following secondary incubation, cells are rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse is repeated three times. Cells are resuspended for testing at 8×105 cells/mL in DPBS+0.2% BSA, 0.05% NaN3. For streptavidin-polymer conjugate labeling, cells are incubated with a biotinylated primary antibody to the marker of interest, as detailed above for the secondary antibody labeling, instead of an unlabeled primary. Following the primary washing, cells are resuspended and divided in 4×105 cell aliquots and incubated with streptavidin-polymer conjugates at 1-100 nM volume dilutions for 30 minutes at 4° C. Following secondary incubation, cells are rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse is repeated three times. Cells are resuspended for testing at 8×105 cells/mL in DPBS+0.2% BSA, 0.05% NaN3. If further signal amplification is desired, cells and be incubated with an unlabeled primary antibody and then subsequently follow with a species reactive biotinylated secondary antibody prior to incubation with streptavidin conjugates. The incubation steps, washing protocol and testing protocol should follow as previously detailed. These flow testing procedures have been developed specific to CD4 markers on Cyto-trol cells. Cell preparation and incubation protocols may vary with cell type and an optimal staining, washing and handling protocol should be developed specific to cell type. Working concentration ranges of antibodies have been identified as optimal for both CD4 (35-50% population) and CD45 (85% population) markers on Cyto-trol control lymphocytes as well as on Whole Lysed Blood (for primary antibody only). Markers which have populations significantly different than these ranges may fall outside of the suggested titration ranges. Testing was also done on a Jurkat cell line grown in culture following similar protocols. In these tests a CD45 marker was used. As there are no negative cell populations a different negative control procedure was used. In the negative control samples the primary antibody was omitted from the primary incubation step. This step and all subsequent steps were performed according to the standard protocol. Again a commercially dye-antibody or dye-strepatvidin conjugate were used as a positive control. Procedure for Flow Cytometry Analysis Flow testing was done in test tubes, at 0.5 mL volumes on a BD LSR II Flow Cytometer. Flow testing is performed using the voltage settings determined from daily calibration of the cytometer with calibration particles by flow facility staff. Lymphocyte specific gating by forward scatter vs. side scatter is performed on unstained cell samples as a background control. Standard doublet gating is performed for both forward scatter and side scatter area vs. width profiles. With only a single color, no compensation is required. Data are collected for all forward and side scatter parameters and fluorescence measurements are made using BD's standard Pacific Blue channel. Pacific Blue data utilizes excitation with the 408 nm Violet lasers and a 450/50 BP filter. Samples are collected for 30,000 events within the stated gating parameters. Representative Experiments: CD4 marking was measured on Cyto-trol cells, lyophilized human lymphocytes for analysis of polymer performance in flow. Cyto-trol cells (Beckman Coulter) were reconstituted in the provided reconstitution buffer and allowed to swell for 15 minutes at room temperature. Cells were then spun down at 250 rcf for 3 minutes, washed in DPBS+0.2% BSA and 0.05% NaN3 (staining/testing buffer), then resuspended in staining buffer at 1×107 cells/mL. Cell suspension was divided in two; half the cells were incubated with biotinylated anti-CD4 at 0.4 ug/uL, the other half of the cells were incubated with staining buffer as a negative control for 30 min. Following primary incubation, cells were rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse was repeated three times. Cells were resuspended at prior volume in staining buffer. 4×105 cells were measured per test and divided out accordingly, streptavidin-fluorophore conjugates prepared in Example 19 were incubated at 100 nM with each aliquot of cells for 30 min, allowing the avidin-biotin complex to form. Following the secondary incubation, cells were rinsed and detailed previously. Final cell suspensions were made for testing at 8×105 cells/mL. Flow analysis was performed on a BD LSR II flow cytometer at The Scripps Research Institute (TSRI), San Diego, Calif. Routine calibration with Rainbow fluorescent particles for aligning fluorescent channels on the cytometer was performed by staff at TSRI, all calibrated voltages were used, per staff recommendation. All samples were excited with a 408 nm Violet laser, the polymer conjugate was measured in the AmCyan channel with a 525/50 filter. All samples were initially referenced to unstained cells. The polymer streptavidin conjugate from FIG. 14 showed specific secondary labeling of the primary identified CD4 positive cells, with the positive cells as 44% of the population. The polymer streptavidin conjugate demonstrated a positive stain index showed low non-specific binding with reference to unstained cells and its respective negative control (FIG. 20. (A)). This provides evidence that the polymer, although its peak absorbance is a 440 nm, is a viable fluorescent material for use in flow cytometry with Violet laser excitation. Secondary Antibody Polymer Conjugate on Cyto-Trol Cells Amine-functionalized 405 polymer was conjugated to goat anti-mouse IgG κ1 purified antibody by route of maleimide-thiol conjugation and TCEP partial reduction of the antibody. The polymer and conjugation proceedure are provided specifically in Example 46. Conjugates were tested on Cyto-trol cells (Beckman Coulter), a fixed and lypholized lymphocyte cell population for control testing of specific human antigens. Cell staining followed secondary cell staining protocol. Cells were incubated with and without (negative control) unlabeled anti-CD4 (RPA-T4 clone, BD Biosciences) raised in mouse against the human antigen. After complete washing of primary antibody incubation, cells were incubated with polymer labeled goat anti-mouse conjugates for specific labeling of primary identified CD4 positive cells. Secondary labeling occurs by Fc recognition and binding of the mouse primary antibody by the secondary goat IgG, raised against murine species. A positive control was used by incubation with commercially available Pacific Blue goat anti-mouse IgG (Invitrogen) as the secondary labeling species. FIG. 20 (B) depicts the specific recognition of CD4 specific cells by the secondary fluorescent conjugates. Unstained cells show a negative control and natural autoflourescence of the cells, and incubation of polymer conjugate on cells with no primary labeling show minimal non-specific binding of the conjugate to unlabeled cells. Positive control, Pacific Blue goat anti-mouse shows the commercially available standard for CD4 labeling by secondary antibody with Violet excitation. 405 polymer-goat anti-mouse conjugate (red) shows positive identification of CD4 positive cells, a minimal shift in the negative cell population and great fluorescent signal and resolution that Pacific Blue standard. FIG. 20 (C) depicts Streptavidin polymer conjugates on Jurkat cells. Conjugates were produced with the polymer provided in Example 11 using the protocol defined in Example 29. The stain index for the polymer streptavidin conjugate was over 10 fold higher than that obtained for the commercially available Pacific Blue streptavidin control conjugate. FIG. 20 (D) depicts a primary monoclonal antibody polymer (antiCD4, RPA-T4) conjugate evaluated on Cyto-trol cells using the protocols defined above. The conjugate was prepared using the polymers and protocols defined in Example 46. Additional details on the conjugation can also be found in Example 39. Example 37: Preparation of Polymer Conjugated to —COOH Beads Via EDC Coupling Materials (per 100 μL of Beads): LodeStars —COOH functionalized magnetic beads (Varian, Inc. PL6727-0001) (100 μL of suspension at spec'd 30 mg/mL). Polymer with amine terminal ends from Example 17 (125 μL at 1.6 μM in 25 mM MES pH 5, for a 10-fold excess over theoretical bead capacity). 10 mM NaOH (2 mL). DI H2O (3 mL). 25 mM cold MES, pH 5. EDC at 50 mg/mL in 25 mM cold MES, pH 5 (100 μL). NHS at 50 mg/mL in 25 mM cold MES, pH 5 (100 μL). 100 mM Tris/HCl pH 7.4 (1 mL). Centrifuge and black flat-bottom 96-well plate. Antibody capacity was given at 10 ug/mg bead, giving an amine coupling capacity of 2 nmol polymer/mL bead (at 30 mg/mL). A 10 fold-excess of polymer over the suggested capacity was used to target the antibody concentration given in Varian's protocol. Bead Washing Beads were washed collectively as 600 μL and then split into 6×100 μL samples for coupling. Beads were washed 2× with 1 mL 10 mM NaOH, then 3× with 1 mL DI H2O; in between washes, the tube was centrifuged 1 min at 3000 rpm to recollect the beads as a pellet, supernatant was discarded and beads were resuspended in the next wash. After the final wash, beads were resuspended in 600 μL cold 25 mM MES, pH 5 and aliquoted into 6×100 μL volumes in microcentrifuge tubes. Beads were centrifuged again 1 min at 3000 rpm and supernatant was discarded. EDC Activation 100 μL of the EDC solution was added to each reaction set. 100 μL of the NHS solution was added to each reaction set. Beads were resuspended by vortexing and then allowed to mix on a rotator for 30 minutes. Beads were washed 2× in cold 25 mM MES pH 5, pelleted by centrifuging for 1 min at 3000 rpm and the supernatant was discarded. Beads were resuspended in 125 μL cold 25 mM MES, pH 5. Polymer Coupling 125 μL of polymer at 1.6 μM was added. Samples were vortexed to mix thoroughly and then reacted at RT on a mixer for 3 hours. Beads were pelleted by centrifuging for 1 min at 3000 rpm; supernatant was discarded. Beads were resuspended in 1 mL 100 mM Tris/HCl to block unreacted —COOH sites, vortexed and mixed for 1 hour. Beads were recollected by centrifugation and resuspended in 100 μL 25 mM MES. At this point, the supernatant of several tubes were yellow in color and had significant absorbance at 440 nm; the beads were washed 6 times until absorbance was at baseline. Beads sat for an additional 2 days prior to fluorescence measurement, after sitting in solution for 2 days, the supernatant was again yellow in color and had measureable absorbance. Beads were washed 3 more times with 30 minute mixes in between until no absorbance was measureable. At 2 days following fluorescence measurements, the supernatant remained clear and free of measureable absorbance. Example 38: Preparation of Polymer-Dye Conjugates Example 38a: Preparation of Polymer-Dye Conjugate at Polymer Terminal 0.5 mg amine-terminated polymer was dissolved in 15 μL DMSO. The polymer solution was then exchanged into 50 mM NaHCO3/Na2CO3, pH 8 buffer and recovered in buffer at −5 mg/mL as determined by UV-VIS absorbance. 50 μg NETS-ester dye (DyLight 594) was dissolved at 10 mg/mL in anhydrous DMSO, which was then immediately added to 120 μg of polymer. The tube was mixed on shaker (600-800 rpm) for 1 h and subsequently diluted to 100 with 20% EtOH in water. The mixture was added to a 30 cm Superdex 200 SEC column in 0.6M NaCl and 20% EtOH to separate polymer-dye conjugate from unreacted dye. The addition of dye can be used to estimate the incorporation of linker on the polymer structure by measuring an absorbance ratio based on the relative extinction coefficients of the polymer and dye. Using the molecular weight of the polymer it is possible to estimate the number of polymer chains which contain a linker. In additional embodiments, polymers with a carboxylic acid side chain are modified with amine functional dyes using standard EDC conjugation procedures or by first converting to the NETS ester using the protocol similar to that described in Example 29. Thiol dyes conjugated to maleimide terminated polymers have also been demonstrated. Any range of chemistry pairs would be expected to work in similar fashion to conjugate a polymer and dye. Example 38b: Preparation of Polymer-Dye Conjugate at Internal Position In a glovebox, 100 mg polymer with internal amine functionalities was dissolved in 10 mL anhydrous DMSO in a 20 mL amber scintillation vial. 0.32 mL DIPEA was added to the polymer solution. 24 mg of NETS-ester dye (Cy3) was dissolved in 2.4 mL in anhydrous DMSO and added to the polymer solution. The vial was tightly sealed, then removed from the glovebox and stirred at room temperature for 48 hours. The reaction was then purified over Amicon Ultra centrifugal filtration units (MWCO=30 kDa) with 20% ethanol in water until all free dye was removed. Purity was verified by running a 0.15 mg sample over a 30 cm Superdex 200 SEC column in 0.6M NaCl and 20% ethanol. 90 mg yield (90%). The addition of dye can be used to estimate the incorporation of linker monomers in the polymer structure by measuring an absorbance ratio based on the relative extinction coefficients of the polymer and dye. For polymers described above, the ratio of linker monomers (or dye attachments) per fluorene monomer in the final polymer are in general agreement with the molar feed ratio of monomers used in the polymerization reaction. Polymers with a carboxylic acid side chain can also be modified with amine functional dyes using standard EDC conjugation procedures or by first converting to the NHS ester using the protocol similar to that described in Example 29. Analogous procedures can be used to conjugate a range of dyes including Cy3, DyLight 549, DyLight 633, FAM, FITC, Alexa633, Alexa647 and several others. Polymers with a carboxylic acid side chain can also be modified with amine functional dyes using standard EDC conjugation procedures. FIG. 21 (A) shows the polymer structure above conjugated to (from left to right) FITC, Cy3, DyLight 594 and DyLight633. The polymer alone is show for reference (far left). Note in each case the amount of residual donor (polymer) emission is minimal. The data highlight the capablity of generating several diagnostic signals at different wavelenghts for multiplex applications. In this embodiment a single light source is capable of generating five distinct emission wavelengths. Example 38c: Energy Transfer Evaluation for Polymer-Dye Conjugates Based on Polymer Excitation for Use in Polymer Tandem Conjugates FIG. 21 (B) depicts a comparison of the fluorescence of the dye (DyLight594) excited near its absorbance maximum (lower curve) and polymer-dye conjugate excited at 405 nm (upper curve). Dye emission around 620 nm was over 5 fold brighter from the polymer-dye conjugate at the same molar concentration of dye versus direct dye excitation. Such embodiments highlight the signal amplification afforded by the disclosed polymer donors in energy transfer processes. The picture in the upper left corner highlights the visual color change in the emission of the complex based on dye conjugation. The polymer solution emits blue in the absence of dye and red upon dye conjugation (post purification). FIG. 21 (C) compares the fluorescent signal of the base polymer (no dye, peak emission near 420 nm) to that of the polymer-dye conjugate (peak emission near 620 nm). The DyLight594 dye quenches >98% of the polymer emission when conjugated to the polymer above (Example 38b). This is a feature of the polymer materials as any remaining donor emission could manfest as background signal in multilpex assay formats. The ability to conjugate the dye directly to the polymer structure and vary the number of attachement sites provides for efficent transfer that can be regulated by chemical design. Example 39: Flow Testing of Monoclonal Antibody (antiCD4) Conjugates on Whole Lysed Blood Samples Polymer conjugates of primary antiCD4 antibody (RPA-T4 clone) were produced using 3 different conjugation routes as provided in Examples 45, 46 and 49. 1) Amine modified polymer converted to a maleimide reactive group using SMCC (maleimide/NHS crosslinker) reacted with thiol groups on the antibody introduced by reacting SATA (thiol/NHS cross linker) with lysine (amine) groups (CJ11-2, FIG. 22). 2) Same polymer modified with SMCC (malemide) but with thiol groups introduced on antibody using TCEP to partially reduce the disulfide linkages in the antibody (CJ13-2, FIG. 22 and FIG. 20D). 3) A carboxylic acid terminated polymer activated with TSTU to form the NHS ester was reacted directly with the lysine (amine) groups on the antibody (CJ04-2 FIG. 22). All conjugates were made from the same polymer structure and batch. The polymer was synthesized using the protocol depicted in Example 12 with an amine end capping unit in place of the carboxylic acid capping unit shown. The NHS/amine conjugation was done with the protocol described in Example 45. The maleimide/thiol conjugation reactions were done in lines with those protocols described in Examples 46 and 49. FIG. 22 depicts the performance of these conjugates in flow cytometry conduced as follows. 100 μl whole human blood from a healthy volunteer was aliqoted into FACS tubes (duplicates for each sample). Antibody conjugates were diluted in wash buffer (PBS with 0.5% BSA and 0.1% Sodium Azide) and added to the blood at specified concentrations. Samples were vortexed vigorously then incubated for 15-30 mins in the dark at room temperature. 2 ml of 1x BD FACS Lyse solution was added to each sample and mixed in by vigorous vortexing prior to a further 10 mins incubation in the dark at room temperature. Samples were centrifuged for 5 min at 500 g and the supernatant tipped off and discarded. Samples were vortexed and 3 ml of wash buffer (PBS with 0.5% BSA and 0.1% Sodium Azide) added. Centrifugation was repeated at 500 g for a further 5 min. The resulting supernatant was tipped off and discarded and the remaining cell pellet vortexed. Samples were run on a BD LSRII flow cytometer acquiring all violet channels equipped with a violet laser and 450/50 nm filter that had been set up and precalibrated against BD CST beads. All polymer conjugate samples (CJ04-2, CJ11-2 and CJ13-1 lines) showed minimal non specific binding compared to unstained cells. Further, all polymer conjugates produced significantly higher positive signals than a commercially available Pacific Blue control conjugate of the same antibody clone which is commonly used for flow cytometry at compatible wavelengths. The best performing conjugates from this set provided over 6 fold high stain index than the commercially available Pacific Blue control antibody. Example 40: Preparation of Polymer-Dye Conjugate The polymer is conjugated to a dye, Dylight 594, and purified in a manner similar to the methods as described in Example 36. FIG. 23 depicts a comparison of the florescence of the dye (DyLight594) and polymer-dye conjugate. The dye was excited at 594 nm and the polymer-dye conjugate at 380 nm. Example 41: Fluorescent Immunoassay (ELISA) with Streptavidin-Conjugated Polymer An immunoassay for human IgG was developed as a demonstrative system in 96 well plate format. In further embodiments, similar functionality would be equally applicable in other formats including suspended microspheres and protein chip microarrays. Step 1: Preparation of Reagents Wash concentrate was prepared by dissolving 79.2 g Tris base pre-set crystals (pH 7.7), 225 g sodium chloride and 0.5 g Thimerosol in 1000 mL deionised water. Wash solution was prepared by adding 100 mL wash concentrate to 2400 mL deionised water. Subsequently, 10 mL 10% Triton X-100 was added. The basic assay buffer was prepared by dissolving 14.8 g Tris base pre-set crystals (pH 7.7), 18 g sodium chloride and 0.5 g Thimerosol in 2000 mL Milli-Q water (conductivity 18.2 mΩcm). Subsequently, 2 mL 10% Tween 20 and 10 g Bovine Serum Albumin Fraction V, essentially gamma globulin free were added. The solution was filtered and stored at 4° C. Step 2: Preparation of Capture Antibody Coated Plates Capture antibody was coated onto the surface of Nunc white Maxisorp 96 well plates at a concentration of approximately 1 microgramme per well. The plates were sealed and stored overnight at 4° C. Subsequently, the plates were washed once with wash solution and tapped dry on absorbent paper. Unless otherwise stated all plate washing in this example was performed on an automated microtitre plate washer. Two hundred and fifty (250) microlitres of blocking buffer (0.1M PBS containing 2% BSA) were added to each well, the plates re-sealed and stored at 4° C. until use. Step 3: Immunoassay Capture antibody-coated microtitre plates were washed twice with wash solution and tapped dry on absorbent paper. Two hundred (200) μL of either assay standard or experimental unknown sample were added in quadruplicate to appropriate wells of the coated plate. The plates were incubated on a shaker for 2 hours at 18° C. Subsequently, the plates were washed three times with wash solution, tapped dry on absorbent paper, and 200 μL of biotinylated detection antibody at a previously determined optimal concentration (diluted in assay buffer and filtered before use) were added to each well. The plates were incubated on an orbital shaker at ambient temperature for a further 60 minutes. The plates were then washed three times and tapped dry on absorbent paper. Two hundred (200) μL of 0.2 micron syringe filtered Streptavidin-polymer conjugate as prepared in Example 30 diluted to a concentration previously determined as suitable in assay buffer. The polymer was a fluorene polymer with neutral PEG11 side chains and an amine conjugation site. The plates were incubated on an orbital shaker at ambient temperature for a further 2 hours. The plates were then washed six times, tapped dry, turned around 180o, and re-washed a further six times. The plates were again tapped dry on absorbent paper. Two hundred (200) μL of filtered release reagent (0.1M sodium hydroxide, 2% Triton X-100) were added using a multi-channel pipette, the plates shaken for 60 minutes at ambient temperature and the fluorescence measured with a Victor Fluorometer. The plate was then sealed, stored overnight at 4° C. and re-read in the Victor Fluorimeter the following morning. Fluorescence counts were analysed using the Multicalc Software from Perkin Elmer to determine lower limit of assay detection and assorted similar parameters. Alternative conditions were also evaluated to release the conjugate from the well plate surface to improve the fluorescent readout. A representative data set is shown in FIG. 24. Comparisons were also made to commercially available SA-dye conjugates. The polymer conjugates demonstrated superior detection limits relative to the dye conjugates as was expected due to the collective optical properties. Example 42: Synthesis, Conjugation and Application of Para-Phenylene Vinylene Co-Polymer with Active Functional Linker for Bioconjugation Poly(1,4-(di2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 2,5-dibromoterephthalate)-vinyl-alt-para(2-methoxy-5-2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl benzene)-vinylene) with phenylbutoxyamino termini. Di-2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 2,5-dibromoterephthalate (2.0 g, 1.52 mmol),34-(4-methoxy-2,5-divinylphenoxy)-2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontane (1.11 g, 1.52 mmol), palladium acetate (13.6 mg, 0.061 mmol), tri-o-tolylphosphine (37 mg, 0.121 mmol), triethylamine (1 mL, 7.6 mmol) and 4 mL of DMF were combined in a small round bottom flask, equipped with a Teflon stribar, fitted with a needle valve and transferred to a Schlenk line. The solution was degassed via three freeze-pump-thaw cycles, put under nitrogen and heated to 100 C with constant stirring overnight. Next di-2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 2,5-dibromoterephthalate (2.0 g, 1.52 mmol) (100 mg, 5 mol %), palladium acetate (5 mg), and tri-o-tolylphosphine and 0.5 mL DMF were combined in a small round bottom flask which is fitted with a needle valve and transferred to the Schlenk line. The solution was degassed via three cycles of freeze-pump-thaw and once warmed to room temperature was transferred to the polymerization reaction via cannula to exclude air and moisture. Allowed the mixture to react overnight. Next 4-(4-bromophenoxy)butan-1-amine (43 mg, 15 mol %) and 0.5 mL of DMF were combined in a small round bottom flask, equipped with a Teflon stribar, fitted with a needle valve and transferred to a Schlenk line. Once warmed to room temperature the solution was transferred to the polymerization reaction via cannula to exclude air and moisture. Allowed the mixture to react overnight. The next day the reaction was cooled to room temperature and the bulk of triethylamine was removed under vacuum. The reaction mixture was diluted with ˜30 mL of water and filtered through G 6 glass fiber filter paper. The filtrate was transferred to several Amicon filters (10 kDa cutoff) to concentrate the polymer and remove DMF. The remaining water is removed under vacuum and the residue is extracted into methylene chloride. The methylene chloride solution is dried over magnesium sulfate and filtered. The solvent is removed leaving behind a dark red thick oil, approximately 900 mg. The polymer was found to have a Mn of 20,400 g/mol as determined by GPC analysis relative to polystyrene standards. Incorporation of the amine linker was verified by conjugating a dye to the final polymer as described in Example 38. The polymer was then conjugated to streptavidin protein as follows: Amine polymer was dissolved at 50 mg/ml and desalted and buffer exchanged into 100 mM phosphate buffer pH 7.5. Polymer concentration was assessed by absorbance and 25 molar equivalents of SMCC (10 mg/ml in anhydrous DMSO) added. The reaction was mixed for 60 mins at room temperature and then desalted and buffer exchanged into PBS pH7.0+5 mM EDTA prior to repeat polymer concentration determination and confirmation of malemide functionality by SAMSA-fluorescein dye test. Streptavidin (5 mg/ml in 100 mM phosphate buffer pH7.5) was activated by addition of 20 molar equivalents of SATA (5 mg/ml in anhydrous DMSO). The reaction was mixed at room temperature for 60 mins prior to quenching (>15 mins room temp) with 10% (v/v) 50 mM EDTA, 2.5M hydroxylamine pH7.0. The activated protein was desalted and buffer exchanged into the same buffer as the activated polymer prior to an performance of an Ellman's assay to confirm and quantify thiol incorporation. Both the activated polymer and streptavidin were used as follows without delay. A greater than order of magnitude molar excess of SMCC activated polymer was added to the SATA activated streptavidin and the two mixed for 2 hours at room temperature prior to quenching with 20 molar equivalents of N-ethylmaleimide which was mixed in for 15 minutes at room temperature. Ion exchange and size exclusion chromatography were used to purify the bioconjugate of unreacted polymer and streptavidin. Appropriate fractions were pooled to maximize yield and performance and then concentrated by ultrafiltration. The conjugate was tested and its performance compared to a commercially available streptavidin-phycoerythrin (SA-PE) conjugate designed for purpose in a model Luminex xMap assay (FIG. 27, left). Donkey anti-mouse IgG antibody was covalently conjugated to xMap beads. A standard curve titration of Mouse IgG was then performed under standard Luminex xMap assay conditions (FIG. 27, right). Replicate samples were detected using either 4 μg/mL streptavidin-phycoerythrin or streptavidin conjugated polymer conjugate prepared as above (concentration not rigorously controlled). Samples were then read on a Luminex instrument. Absolute signals were found to be lower using the conjugated polymer. This is partially attributed to a non-ideal match between the polymer spectra and the excitation and emission optics in the instrument as well as the putative lower concentration of detection reagent used compared with the commercially available phycoerythrin product. However, the proportional background (non specific signal) from the polymer was also markedly lower resulting in a very comparable lower limit of detection for both detection formats (Fluorescence highest point in standard curve/fluorescence zero concentration of analyte (MFI/zero): 21.8 PE, 26.6 Polymer). Example 43: Synthesis of a Fluorene Co-Polymer with a DPP Hand Gap Modifying Unit To a 25 mL round-bottomed flask were added: PEGylated dibromo-DPP monomer (110 mmol), PEGylated fluorene diboronicester (110 mmol), THF (2.4 mL) solvent, 2M K2CO3 (1.6 mL) and tetrakis(triphenylphosphine)palladium (3.3 mmol) catalyst. The mixture was degassed by three freeze-pump-thaw cycles and then stirred under argon at 80 C over night. The resulting mixture was allowed to r.t. and diluted with water. Polymer was collected after dichloromethane extraction. The resulting polymer was found to have an absorption maxima at 520 nm and emission maxima at 590 nm with quantum yield of 6% in water. The polymer had a MW estimated at 16,000 by GPC analysis relative to polystyrene standards and was soluble in water, methanol and dichloromethane. End linker incorporation can be performed using methods similar to those described above and including methods described in Examples 9, 10 and 11. Example 44: Synthesis of a Substituted Divinylbenzene Polymer Methods used to prepare the polymer above were similar to those provided in Example 38. General methods for the preparation of divinylbenzene polymers as disclosed herein may be derived from known reactions in the field as well as methods found herein, and the reactions may be modified by the use of appropriate reagents and conditions, as would be recognized by the skilled person, for the introduction of the various moieties found in the formulae as provided herein. Example 45: Conjugation of Polymer to an Amine on a Primary Antibody Procedure for Production of NHS Ester Polymer-Antibody Conjugate Primary monoclonal antibody, anti-CD4 (RPA-T4 clone) was desalted, and exchanged into 50 mM NaHCO3 buffer, pH 8.2 at 1 mg/mL. Enriched NHS functionalized polymer was dissolved into anhydrous dimethyl sulfoxide (DMSO) at 100 mg/mL. Polymer solution was added at 30 fold molar excess of antibody into the antibody solution and allowed to mix by agitation for 3 hours at RT. Protein concentration was adjusted with buffer prior to incubation to ensure the volume of organic solvent was <10% the total volume. Following ultrafiltration over a 10 KDa MWCO filter device, ion exchange and size exclusion chromatographic techniques were then used to purify the bioconjugate of unreacted polymer and antibody, respectively. Appropriate fractions were pooled to maximize yield and buffer exchanged into PBS+0.05% NaN3 and simultaneously concentrated by ultrafiltration as above. Degree of labeling (indicated as p above) was determined via absorbance at 405 nm and a corrected 280 nm value. The polymer conjugate (CJ04-02) provided in Example 39 (FIG. 22) had an F/P (# of polymers per antibody) of approximately 2.04. This conjugate demonstrated flow performance as determined by stain index measurements which were greater than 3 fold higher than a Pacific Blue control conjugate of the same antibody. Example 46: Conjugation of Polymer to an Antibody Using Malemide/Thiol Chemistry Malemide/Thiol Conjugation of Polymers to Partially Reduced Antibodies Secondary antibody, goat anti-mouse IgG (H+L) was reconstituted in PBS+10 mM acetic acid and desalted/exchanged into 50 mM Tris-HCl buffer, pH7.4 at 1.0 mg/mL. TCEP (tris(2-carboxyethyl)phosphine) was dissolved in 50 mM Tris-HCl buffer, pH7.4, added at 6 molar excess with a final TCEP concentration of 10 mM and mixed for 30 minutes at room temperature. The modified protein was purified over a PD-10 desalting column to remove excess TCEP and exchanged into reaction buffer, 100 mM NaPO4, pH 6.5 reaction buffer with 10 mM EDTA. Amine-activated polymer was dissolved in anyhydrous DMSO at 10 mg/mL and mixed with succinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SMCC) linker. The linker was added at 50 mg/mL, 20 molar excess in DMSO to the polymer solution and activated by diisopropylethylamine (DIPEA). The reaction was purified over Amicon Ultra centrifugation filters and exchanged into reaction buffer, 100 mM NaPO4, pH 6.5 reaction buffer with 10 mM EDTA. Immediately following disulfide reduction, maleimide functionalized polymer in reaction buffer at 10 mg/mL was added in 20 molar excess of antibody and allowed to mix for 4 hours. Ion exchange and size exclusion chromatographic techniques were then used to purify the bioconjugate of unreacted polymer and antibody, respectively. Degree of labeling (indicated as p above) is determined via absorbance at 405 nm and a corrected 280 nm value. The polymer conjugate provided in Example 36 (FIG. 20B) had an F/P (# of polymers per antibody) of approximately 2. This conjugate demonstrated flow performance as determined by stain index measurements which were greater than 4 fold higher than a Pacific Blue control conjugate of the same antibody. Malemide/Thiol Conjugation of Polymers to Thiol Modified Antibodies Secondary antibody, goat anti-mouse IgG (H+L) was reconstituted in PBS+10 mM acetic acid and desalted/exchanged into 100 mM phosphate pH7.5 buffer. SATA (N-succinimidyl-S-acetylthioacetate) was dissolved anhydrous DMSO, added at 15 molar excess and mixed for 60 minutes at room temperature. After quenching with a hydroxylamine solution, the modified protein was desalted over a PD-10 column to remove excess SATA and exchanged into reaction buffer, 5 mM EDTA, PBS pH 7.0 buffer. Amine-activated polymer was dissolved in anyhydrous DMSO at 10 mg/mL and mixed with succinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SMCC) linker. The linker was added at 50 mg/mL, 20 molar excess in DMSO to the polymer solution and activated by diisopropylethylamine (DIPEA). The reaction was purified over Amicon Ultra centrifugation filters and exchanged into reaction buffer, 5 mM EDTA, PBS pH 7.0 buffer. Immediately following activation of the antibody, maleimide functionalized polymer in reaction buffer at 10 mg/mL was added in 20 molar excess of antibody and allowed to mix for 4 hours. Ion exchange and size exclusion chromatographic techniques were then used to purify the bioconjugate of unreacted polymer and antibody, respectively. Degree of labeling (indicated as p above) is determined by absorbance at 405 nm and a corrected 280 nm value. The resulting purified conjugates were flow tested in similar fashion as those described in Example 36 for the conjugates prepared using TCEP reduction (data not provided). The polymer structures defined in Example 39 were used to prepare primary antiCD4 (RPA-T4) antibody conjugates in similar fashion to those described in the example above. 30 eq of polymer were reacted with the SATA modified antibody (CJ11-2, FIG. 22) and TCEP reduced antibody (CJ13-1, FIG. 20D and FIG. 22) to produce polymer conjugates for testing in flow cytometry assays after purification. SMCC modified polymers from Examples 23 and 26 were also successfully conjugated to antiCD4 (RPA-T4) and antiCD8 (RPA-T8) antibodies using the TCEP reduction method. DTT reduction was also successfully performed in place of TCEP. Performance in flow cytometry of the antiCD4 and antiCD8 conjugates were evaluated in similar fashion to those described in Example 39 (FIG. 22). Example 47: Polymer Conjugation to a DNA Oligomer Azide Polymer Synthesis for Click Conjugation to Alkyne Terminated DNA Oligo A solution of azidohexanoic acid NHS ester (2.5 mg) in anhydrous DMF (100 μL) was added to a solution of the amine-functional polymer (9.9 mg) in anhydrous DMF (100 μL) under argon. Diisopropylethylamine (2 μL) was then added. The reaction was agitated at room temperature for 15 hours. Water was then added (0.8 mL) and the azide-modified polymer was purified over a NAP-10 column. The eluent was freeze dried overnight. Yield 9.4 mg, 95%. Oligo Synthesis with Pendant Alkyne (Hexyne) for Click Conjugation to Azide Polymer The 3′ propanol oligo A8885 (sequence YATTTTACCCTCTGAAGGCTCCP, where Y=hexynyl group and P=propanol group (SEQ ID NO: 1)) was synthesized using 3′ spacer SynBase™ CPG 1000 column on an Applied Biosystems 394 automated DNA/RNA synthesizer. A standard 1.0 mole phosphoramidite cycle of acid-catalyzed detritylation, coupling, capping and iodine oxidation was used. The coupling time for the standards monomers was 40 s, and the coupling time for the 5′ alkyne monomer was 10 min. The oligo was cleaved from the solid support and deprotected by exposure to concentrated aqueous ammonia for 60 min at room temperature, followed by heating in a sealed tube for 5 h at 55° C. The oligo was then purified by RP-HPLC under standard conditions. Yield 34 OD. Solution Phase Click Conjugation: Probe Synthesis A solution of degassed copper sulphate pentahydrate (0.063 mg) in aqueous sodium chloride (0.2 M, 2.5 μL) was added to a degassed solution of tris-benzo triazole ligand (0.5 mg) and sodium ascorbate (0.5 mg) in aqueous sodium chloride (0.2 M, 12.5 μL). Subsequently, a degassed solution of oligo A8885 (50 nmole) in aqueous sodium chloride (0.2 M, 30 μL) and a degassed solution of azide polymer (4.5 mg) in anhydrous DMF (50 μL) were added, respectively. The reaction was degassed once more with argon for 30 s prior to sealing the tube and incubating at 55° C. for 2 h. Water (0.9 mL) was then added and the modified oligo was purified over a NAP-10 column. The eluent was freeze-dried overnight. The conjugate was isolated as a distinct band using PAGE purification and characterized by mass spectrometry. Yield estimated at 10-20%. Fluorescence Studies The oligo-polymer conjugate was used as a probe in fluorescence studies. The probe was hybridized with the target A8090 (sequence GGAGCCTTCAGAGGGTAAAAT-Dabcyl (SEQ ID NO: 2)), which was labeled with dabcyl at the 3′ end to act as a fluorescence quencher. The target and probe were hybridized, and fluorescence monitored in a Peltier-controlled variable temperature fluorimeter. The fluorescence was scanned every 5° C. over a temperature range of 30° C. to 80° C. at a rate of 2° C./min. FIG. 25 shows increasing fluorescence intensity or emission with increasing temperature, indicating that as the probe-target pair melt, the polymer and quencher separate and fluorescence is recovered. Polymer conjugation to nucleic acids can also be performed using methods adapted from the protocols described in Examples 14, 45 and 46. Example 48: Purification of Polymer Antibody Conjugates Polymer antibody conjugates produced via the protocols described in Examples 45, 46 and 49 were purified using a two step method. First ion exchange is used to remove free, unreacted polymer. As the polymers described in this invention do not possess any formal charge they do not bind to the ion exchange media. Proteins (antibodies), however, do contain charged groups and are commonly bound to various ion exchange media for purification. In the examples provided the pH and conductivity of the conjugate solution (post reaction) was lowered to improve the binding of the free antibody and conjugate to the cationic exchange resin. After loading the conjugate, the resin is washed to baseline (measuring both 280 and 407 nm absorbance) to ensure all free polymer is removed. Bound antibody and polymer antibody conjugate are eluted by increasing the pH and ionic strength. A representative example of this separation is provided below in FIG. 26 (left) where the left peak represents the free polymer and the right peak the eluted conjugate and free protein. Removal of free polymer can also be achieved using affinity chromatograph methods in a similar fashion. Specific affinity resin can be used to bind the free protein and conjugate while removing polymer. After the polymer is removed, the conjugate solution is concentrated and loaded on a size exclusion column to separate any un-reacted or free antibody from the polymer. The polymer compositions described in Examples 43 and 44 elute much earlier than then antibodies despite having a lower molecular weight. This is expected to be a result of the rigid polymer structure. The conjugates thus elute well before any free antibody providing near base line separation of the desired conjugate. Isolating fractions near the center of the distribution also ensures no free antibody is included. A representative example of this separation is provided below in FIG. 26 (right) where the left peak represents the conjugate and the small peak on the far right the free antibody. Retention times of the individual components was verified in an independant experiment. Taken together the purification ensures that both free antibody and free polymer are removed. Purity of the resulting conjugates is reasonably estimated at >95%. Pooled samples can be concentrated and concentration measured by absorbance at 280 and 407 nm, being sure to correct for the polymer absorbance at 280 nm. Such measurements also allow for the determination of polymer to antibody labelling ratios (F/P). Example 49: Dye Labeling and Linker Activation of Tandem Polymer Tandem Dye Conjugation In a glovebox, 93 mg tandem polymer (from Example 26) was dissolved at 15 mg/mL in anhydrous DMSO in a glass vial with stir bar. 22.5 mg Cy3-NHS ester was also dissolved at 15 mg/mL in anhydrous DMSO and added to the polymer solution, followed by 0.3 mL diisopropylethylamine. After stirring for 48 h at room temperature, the solution was diluted to 90 mL with 20% EtOH in water and concentrated over Amicon Ultra-15 filters. The retentate was repeatedly diluted and concentrated over the filters until excess Cy3 was removed. 90% yield. Labeling and linker content were validated by measuring and taking the ratio of polymer and dye absorbance as described in Example 38. Amine Modification of Tandem (Aqueous Conditions) 100 mg of polymer-dye conjugate was dissolved at 150 mg/mL in ethanol. This was added dropwise to 6 mL 50 mM MES buffer (pH 5) at 4° C. 38 mg N-hydroxy succinimide was added in one portion, and the solution was stirred to dissolve the solids. After dissolution, 192 mg of N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride was added in portions while stirring. After stirring the solution for 30 minutes, 33 μL of ethylene diamine was added. After stirring overnight at room temperature, the solution was diluted to 90 mL with 20% EtOH in water and concentrated over Amicon Ultra-15 filters. The retentate was repeatedly diluted and concentrated over the filters a total of four times to remove impurities. 90% yield, 60% conversion. Linker conversion was verified by conjugating a second dye to the terminal amine as described in Example 38. Tandem Conjugation to a Primary Antibody Primary monoclonal antibody, anti-CD8 (RPA-T8 clone) was desalted/exchanged into 5 mM EDTA, 50 mM phosphate 150 mM NaCl pH 7.0 buffer. TCEP (tris(2-carboxyethyl)phosphine) was dissolved water and added at 12 molar excess and mixed for 90 minutes at 30° C. The modified protein was purified over a PD-10 desalting column to remove excess TCEP and exchanged into 5 mM EDTA, 50 mM phosphate 150 mM NaCl pH 7.0 buffer. Amine-activated tandem polymer was dissolved in ethanol at 50 mg/mL and this solution was mixed with two volumes of 100 mM phosphate pH 7.5 buffer. This solution was then desalted/exchanged into 100 mM phosphate pH 7.5 buffer using a PD-10 desalting column. To this solution was added 25 molar excess of succinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SMCC) linker (prepared as a 10 mg/ml solution in anhydrous DMSO). The resulting solution was rollermixed at 20° C. for 60 minutes before being desalted/exchanged into 5 mM EDTA, 50 mM phosphate 150 mM NaCl pH 7.0 buffer using a PD-10 desalting column. Immediately following disulfide reduction, the maleimide functionalized polymer was added in 25 molar excess of antibody and allowed to mix for 2 hours at 20° C. Ion exchange and size exclusion chromatographic techniques were then used to purify the bioconjugate of unreacted polymer and antibody, respectively. Degree of labeling (indicated as p below) is determined via absorbance and a corrected 280 nm value. Flow Cytometry Analysis of Polymer Tandem Conjugate in Multicolor Experiment The resulting antiCD8 Tandem conjugate was evaluated on both compensation beads and whole blood samples on a flow cytometer. Anti mouse IgG compensation beads were used to capture the antibody and quantify signal spill over into detection channels (detectors with unique emission filters) other than that intended for the conjugate. FIG. 28 (left) shows the signal measured when the tandem conjugate was excited with a violet laser with emission detected using a 610 nm filter matched to the conjugates emission (labeled QDotA). Crosstalk into the flow cytometer's other channels paired with the violet excitation laser (DAPI-A and AmCyan-A) and two channels off the 488 nm laser (FITC-A and PE-A) are also shown in this panel of the figure. The data show minimal crosstalk in the 450/50 nm filter (DAPI-A) which specifically detects residual polymer (donor) emission. The significantly higher signal from the Cy3 reporter on the Tandem (610 nm filter) relative to the other channels above illustrates that minimal compensation (maximally no more than 6% in this example and case by case often much lower) is required. The Tandem anti CD8 conjugate was subsequently evaluated in a 4 color flow assay with other labeled antibodies (anti CD3 Pacific Blue, anti CD45 Phycoerythrin and anti CD4 fluorescein) on whole human blood from a healthy volunteer using staining and analysis protocols in accord and developed from Example 39. The data in FIG. 28 (right) clearly show the compatibility of the Tandem label with common multicolour flow cytometry instrumentation, reagents and protocols. Specifically, intense and specific staining of CD8 positive lymphocytes is observed and within the CD4 positive subset ready discrimination of CD8 expressive and non expressive cells is clear Collectively the data highlight the viability of the polymer-dye Tandem conjugates in multicolor flow assays as described in the disclosed invention (See, e.g., FIG. 20 and FIG. 22). Example 50: Validation of Non-Ionic Polymer Side Chains for Water Solubility and Flow Cytometry Application A series of different polyfluorene polymers were produced to investigate the interaction of water soluble conjugated polymers with cells. This was done by first synthesizing a range of monomers substituted with different solublizing side chains (e.g., PEG-, sulfonate-, quaternary amine-, zwitterion- substituted) which were then polymerized using Suzuki coupling. The purpose was to determine what influence the side chains had on both non-specific cell binding and polymer solubility in typical buffers used in biological assays, particularly those used in flow cytometry (e.g. PBS and DPBS). The number and property diversity of polymer candidates synthesized made it impractical to produce purified conjugates of each for flow cytometry testing. Thus, a system was developed to score each candidate polymer based on its contribution to non-specific binding to cells. Such a system enabled ranking of polymers, with predictive value on whether they would perform sufficiently once conjugated. A Non-specific Binding (NSB) “Index” was developed around a Jurkat cell model (lymphocyte cell line). In this, cells were incubated with a fixed concentration of each polymer, washed, and analyzed by flow. FIG. 33 displays the outcome following such analysis, and illustrates the wide variation in signal generated by each polymer type. The polymers in FIG. 33 were evaluated with a phtalamide protecting group on the pendant amine with the exception of P9. The data ranks these polymers in terms of signal generated purely by NSB. More accurate assessment of relative NSB was enabled by adjusting further normalizing the flow signal by differences in fluorescence efficiency (crude assessment of quantum yield) of each form of polymer when assayed independently in stain buffer using 405 nm excitation on a fluorometer and monitoring emission in the range of 420-460 nm (to estimate a 440/40 nm filter in the cytometer). Representative polymers P5, P2, P9 and P12 showed increasing NSB relative to unstained cells (far left curve, intensity represented on x-axis). The data in FIG. 34 go on to highlight the difference in polymers produced with neutral, non-ionic PEG side chains (designated P20) verses those which also incorporate anionic side chains (designated P4). The data are histograms collected from flow cytometry analysis (405 nm excitation in a BD LSR-II cytometer) using a Jurkat cell line as in FIG. 33. The panel on the left shows unstained cells and a negative control (cells treated with a non-specific Pacific Blue labeled conjugate) which are the two curves on the far left. Little if any non-specific staining is observed for the Pacific Blue control. In this same panel, however, curve on the right represents cells treated with the anionic P4 polymer and has a clear off set in signal (x-axis) as shown. Conversely the neutral polymer P20 showed almost no off set from the untreated cells which is in line with the Pacific Blue control. The panel in the middle represents a range of different polymer and polymer side chain combinations tested on the same cells. The data highlighted the advantage of neutral side chains. This advantage has also translated to other assay formats including plate based immunoassays and cytometric bead arrays (data not shown). The neutral side chains also unexpectedly resulted in a significant increase in the solubility of the conjugated polymers in aqueous solutions relative to those made previously with ionic side chains. This was particularly true in buffers containing even moderate ionic strength (such as those used in basic cell protocols). The solution quantum yields were also seen to increase, possibly due to the higher aqueous solubility (and less aggregation). The poor solubility in buffers also made protein conjugation more difficult and streptavidin conjugates produced from P4 showed signs of aggregation in typical assay buffers such as phosphate buffered saline (PBS). This was not true of polymers and conjugates produced in other examples disclosed herein. Example 51: Purification and Characterization of Polymer-Avidin Conjugates Gel Analysis of Polymer-Avidin Conjugates To verify successful conjugation to avidin (AvDN), an agarose gel electrophoresis method was developed and used to assess the relative mobility of AvDN as a function of the degree of conjugation with polymer (FIG. 35). Prior to gel loading, the conjugation reaction was stained with biotinyl-fluorescein, which bound polymer-AvDN conjugate and free AvDN. Electrophoresis was performed in 0.8% agarose gels, poured and run in a buffer of 10 mM Sodium Borate, pH 11. The gel was visualized under UV illumination (to visualize the polymer) and by 532 nm excitation (to visualize fluorescein) to assess the degree of conjugation. Under UV illumination, a single band was observed for polymer. Under 532 nm excitation, bands were observed for unbound biotinyl-fluorescein, unreacted AvDN, and polymer-AvDN conjugate which coincided with the free polymer band, indicating that unreacted polymer co-eluted with polymer-AvDN conjugate (FIG. 35). Conjugation was confirmed by the intensity of the conjugate band. The key at the top of the gel images (FIG. 35) indicates which components were included in the conjugation reaction, as well as whether the samples were pre-incubated with biotinyl fluorescein prior to loading and electrophoresis. The image on left visualizes polymer by UV-excitation, whereas the image on right captures the result of fluorescein excitation. On the right image, biotinylated fluorescein can be seen associating with polymer when conjugation was performed in the presence, but not in the absence, of hetero-bifunctional NHS-ethoxy-maleimide linkers (linkers were used to functionalize the polymer amine, while protein amines were partially converted to thiols using Traut's reagent, prior to the maleimide-thiol coupling). Abbreviations: AvDN=avidin DN, AA1=polymer, Linker=hetero-bifunctional NHS-Maleimide linker included in the reaction, Biot-F=biotinyl fluorescein pre-staining before electrophoresis. Purification: Removal of Unreacted Avidin by SEC Chromatography The crude conjugate mixture was fractionated on a Superdex 200 size exclusion column, while fractions were monitored by UV absorbance (FIG. 36, top). To validate the method, fractions were analyzed by agarose gel electrophoresis. As described above, this method of electrophoresis made it possible to visualize the degree to which avidin was attached to polymer, and in this case to analyze the composition of each fraction from the column. Selected fractions were incubated with biotinyl-fluorescein (1 molar equivalent relative to avidin) prior to gel loading, with biotinyl-fluorescein loaded separately as a marker (leftmost lane, FIG. 36, bottom). Electrophoresis was performed in 0.8% agarose gels, poured and run in a buffer of 10 mM Sodium Borate, pH 11. The gel was visualized by 532 nm excitation. Retardation of fluorescein-visualized bands for fractions C2-C6 indicates purified polymer-avidin conjugate, while the two bands observed for fraction C8 indicate a mixture of polymer-avidin conjugate and free avidin. Fractions C10-D2 show only free avidin. Evaluation of Conjugation Efficiency by Gel Analysis In order to determine the best ratio of polymer to streptavidin in conjugation reactions, the molar equivalents of polymer to streptavidin were varied from 0-24 equivalents. Post conjugation, the conjugation products were incubated with biotinyl-fluorescein prior to electrophoresis. The gel was visualized by UV illumination and 532 nm excitation (FIG. 37). At 0 molar equivalents of polymer to streptavidin, free streptavidin is observed as a band with relatively high mobility. As the molar equivalents for polymer are increased from 3 equivalents to 12 equivalents, the free streptavidin band decreases in intensity while the polymer-streptavidin conjugate band increases in intensity. At 24 equivalents of polymer, only the conjugate band is observed by 532 nm excitation. Impact of Purification on Conjugate Performance on Cell Analysis by Flow Cytometry Purification of polymer streptavidin conjugates (polymer structure exemplified in Example 9, denoted P30 in FIG. 38) was performed to determine the impact on flow cytometry performance. Cation-exchange chromatography was implemented in purification to improve removal of excess free polymer. Uncharged polymer eluted in the flow-through while protonated amines on proteins were retained by the media. Thus, streptavidin, whether conjugated to polymer or unreacted, was retained. This ion exchange phase of purification was kept simple with a step gradient, which resulted in co-elution of conjugated and unreacted SA. Further fractionation was enabled by subsequent size-exclusion chromatography, which provided better resolution of conjugate from free SA. Performance benefits in flow cytometry of this new purification method were observed using Jurkat cells incubated with polymer-streptavidin conjugate which were analyzed by flow cytometry. Comparisons were made between crude samples (FIG. 38—top) and purified conjugates (FIG. 38 bottom). Commercially available Pacific Blue-streptavidin conjugates were used as a comparator for brightness, nonspecific binding, and stain index. An improvement in overall Stain Index of approximately 3-fold was shown for Jurkat cells, with similar NSB for both Polymer conjugates and PB-SA based on the histograms shown in FIG. 38. Testing in blood (data not shown) indicated a significant reduction in NSB to levels similar to PB-SA upon conjugate purification. In a separate experiment with a similar polymer (exemplified in Example 11), conjugates with varying polymer to streptavidin ratios were obtained by SEC. Those with the higher ratio provided flow performance relative to those with lower labeling. Ratios were determined based on a ratio of absorbance at 385 nm/280 nm. Relative performance to a Pacific Blue control showed an increase from 10.9 times higher stain index (385/280 ratio of 3.6) to a stain index 13.8 times that of Pacific Blue (A385/280 ratio of 4.7). While preferred embodiments of the present invention have been shown and described herein, it will be obvious to those skilled in the art that such embodiments are provided by way of example only. Numerous variations, changes, and substitutions will now occur to those skilled in the art without departing from the invention. It should be understood that various alternatives to the embodiments of the invention described herein may be employed in practicing the invention. It is intended that the following claims define the scope of the invention and that methods and structures within the scope of these claims and their equivalents be covered thereby."},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE INVENTION <EOH>Fluorescent hybridization probes have developed into an important tool in the sequence-specific detection of DNA and RNA. The signals generated by the appended fluorescent labels (or dyes) can be monitored in real time and provide simple, rapid, and robust methods for the detection of biological targets and events. Utility has been seen in applications ranging from microarrays and real time PCR to fluorescence in situ hybridization (FISH). Recent work in the area of multichromophores, particularly regarding conjugated polymers (CPs) has highlighted the potential these materials have in significantly improving the detection sensitivity of such methods (Liu and Bazan, Chem. Mater., 2004). The light harvesting structures of these materials can be made water soluble and adapted to amplify the fluorescent output of various probe labels (See U.S. patent application Ser. No. 10/600,286, filed Jun. 20, 2003 and Gaylord, Heeger, and Bazan, Proc. Natl. Acad. Sci., 2002, both of which are incorporated herein by reference in their entirety). Results such as these indicate CPs to be highly promising in the field of nucleic acid diagnostics, particularly where sample quantities are scarce. However, there exist methods for the amplification (or replication) of nucleic acid targets, i.e., PCR. Comparatively, in the field of protein recognition, there are no such simple methods for amplifying the targeted materials. As such, signal enhancement arising from CP application is of high consequence in this area. Dye-labeled antibodies are regularly used for the detection of protein targets in applications such as immunohistochemistry, protein arrays, ELISA tests, and flow cytometry. Integrating CP materials into such methodologies promises to provide a dramatic boost in the performance of such assays, enabling detection levels previously unattainable with conventional fluorescent reporters (e.g., dyes). Beyond addition signal, one of the other key drivers in biological detection formats is the ability to detect multiple analytes in the same test or multiplexing. This is commonly achieved by using fluorescent reporters with operate at different, decernable wavelengths. CP materials are ideally suited to provide a platform for expanded multiplexing. This can be achieved by tuning the structure of different CPs to operate at different wavelengths or by incorporating a dye within the polymer-biomolecule conjugate. The material and methods to produce higher sensitivity biological assays and increase multiplexing are highly desired in both molecular (nucleic acid) and immunoassay formats."},"summary":{"kind":"string","value":"<SOH> SUMMARY OF THE INVENTION <EOH>Provided herein are water soluble conjugated polymers of Formula (I): wherein: each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 1 -C 12 alkoxy, C 2 -C 18 (hetero)aryloxy, C 2 -C 18 (hetero)arylamino, (CH 2 ) x′ (OCH 2 CH 2 ) y′ OCH 3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C 2 -C 18 (hetero)aryl group; each optional linker L 1 and L 2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another substrate, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G 1 and G 2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, and thiols within G 1 , G 2 , L 1 or L 2 that allows, for functional conjugation to another molecule, substrate or biomolecule; each dashed bond, - - - - - - , is independently a single bond, triple bond or optionally substituted vinylene (—CR 5 ═CR 5 —) wherein each R 5 is independently hydrogen, cyano, C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl or a C 2 -C 18 (hetero)aryl group, wherein each C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl or a C 2 -C 18 (hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkenyl, C 2 -C 12 alkynyl group, C 1 -C 12 alkoxy, or C 1 -C 12 haloalkyl; and n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. In one aspect, water soluble conjugated polymers of Formula (I) have the structure of Formula (Ia): wherein R, L 1 , L 2 , G 1 , G 2 , MU, a, b, c, d and n are described previously for formula (I). In some embodiments, each R is independently (CH 2 ) x (OCH 2 CH 2 ) y OCH 3 where each x is independently an integer from 0-20, each y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkoxy, or (OCH 2 CH 2 ) z OCH 3 where each z is independently an integer from 0 to 50. In some instances, each R is (CH 2 ) 3 (OCH 2 CH 2 ) 11 OCH 3 . In other embodiments, each R is a benzyl substituted with at least one (OCH 2 CH 2 ) 10 OCH 3 group. In some instances, the benzyl is substituted with two (OCH 2 CH 2 ) 10 OCH 3 groups. In other instances, the benzyl is substituted with three (OCH 2 CH 2 ) 10 OCH 3 groups. In some embodiments, optional linkers L 1 or L 2 have the structure: *=site for covalent attachment to unsaturated backbone; wherein R 3 is independently hydrogen, halogen, alkoxy(C 1 -C 12 ), C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl or a C 2 -C 18 (hetero)aryl group, wherein each C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl or a C 2 -C 18 (hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkenyl, C 2 -C 12 alkynyl group, C 1 -C 12 alkoxy, or C 1 -C 12 haloalkyl; and q is an integer from 0 to 4. In other embodiments, optional linkers L 1 or L 2 have the structure: *=site for covalent attachment to unsaturated backbone wherein A is a site for conjugation, chain extension or crosslinking and is [O—CH 2 —CH 2 ] q —W, or (C 1 -C 12 )alkoxy-X or C 2 -C 18 (hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule.; W is —OH or —COOH; X is —NH 2 , —NHCOOH, —NHCOOC(CH 3 ) 3 , —NHCO(C 3 -C 12 )cycloalkyl(C 1 -C 4 )alkyl-N-maleimide; or —NHCO[CH 2 —CH 2 —O] t NH 2 ; q is an integer from 1 to 20; and t is an integer from 1 to 8. In yet other embodiments, optional linkers L 1 or L 2 have the structure: *=site for covalent attachment to backbone wherein R 25 are each independently any one of or a combination of a bond, C 1 -C 20 alkyl, C 1 -C 20 alkoxy, C 2 -C 20 alkene, C 2 -C 20 alkyne, C 3 -C 20 cycloalkyl, C 1 -C 20 haloalkyl, (CH 2 ) x (OCH 2 CH 2 ) p (CH 2 ) x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C 2 -C 18 (hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups; wherein at least one R 25 is terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In further embodiments, optional linkers L 1 or L 2 have the structure: *=site for covalent attachment to unsaturated backbone; wherein R35 is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In further embodiments, optional linkers L 1 or L 2 are selected from the group consisting of a-h having the structures: *=site for covalent attachment to unsaturated backbone; wherein R′ is independently H, halogen, C 1 -C 12 alkyl, (C 1 -C 12 alkyl)NH 2 , C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 2 -C 18 (hetero)aryl, C 2 -C 18 (hetero)arylamino, —[CH 2 —CH 2 ] r′ —Z 1 , or (C 1 -C 12 )alkoxy-X 1 ; and wherein Z 1 is —OH or —COOH; X 1 is —NH 2 , —NHCOOH, —NHCOOC(CH 3 ) 3 , —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH 2 —CH 2 —O] s′ (CH 2 ) s′ NH 2 ; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH 2 ) 3 (OCH 2 CH 2 ) x″ OCH 3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkoxy, or (OCH 2 CH 2 ) y —OCH 3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein k is 2, 4, 8, 12 or 24; wherein R 15 is selected from the group consisting of 1-t having the structure: *=site for covalent attachment to backbone. In yet further embodiments, optional linkers L 1 or L 2 are In some embodiments, G 1 and G 2 are each independently selected from hydrogen, halogen, alkyne, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorine and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In some embodiments, G 1 and G 2 each independently have the structure wherein R 11 is any one of or a combination of a bond, C 1 -C 20 alkyl, C 1 -C 20 alkoxy, C 2 -C 20 alkene, C 2 -C 20 alkyne, C 3 -C 20 cycloalkyl, C 1 -C 20 haloalkyl, (CH 2 ) x (OCH 2 CH 2 ) p (CH 2 ) x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C 2 -C 18 (hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In other embodiments, G 1 and G 2 are each independently selected from the group consisting of 1-31 having the structures: *=site for covalent attachment to backbone wherein R 15 is selected from the group consisting of 1-t having the structure: and k is 2, 4, 8, 12 or 24. In further embodiments, G 1 and G 2 are optionally substituted aryl or heteroaryl wherein the optional substituent is selected from halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiol, boronic acid, boronate radical, boronic esters and optionally substituted fluorene. In some embodiments, G 1 and G 2 are the same. In other embodiments, G 1 and G 2 are different. In further embodiments, the polymer contains a single conjugation site at only one terminus of the polymer chain G 1 or G 2 . In yet further embodiments, G 1 and G 2 is In some embodiments, MU is selected from the group consisting of a′-k′ having the structure: *=site for covalent attachment to unsaturated backbone wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein at least one of G 1 or G 2 comprises a functional conjugation site. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein L 1 comprises a functional conjugation site. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein at least one of G 1 or G 2 comprises a functional conjugation site. In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In some instances, a signaling chromophore is attached to the polymer via the NH 2 group. In certain instances, the signaling chromophore is Cy3 or Dylight 594 dye. In certain instances, the linker, is about 10% of the entire polymer. In other instances, the polymer is conjugated to a secondary dye reporter and an antibody. In some embodiments of conjugated polymers described herein, the polymer is further conjugated to additional molecules. In some embodiments, the polymer is conjugated to a streptavidin, antibody or nucleic acid and used as a direct fluorescent reporter. In certain embodiments, the polymer is conjugated to a streptavidin. In other embodiments, the polymer is conjugated to thiol groups at the hinge region of an antibody. In yet other embodiments, the polymer is conjugated to an amine group on a protein which is modified with a heterobifuntional linker. In further embodiments, the polymer is conjugated to a nucleic acid. In yet further embodiments, the polymer is conjugated to an antibody. In certain instances, the polymer is conjugated to a monoclonal antibody, a secondary antibody or a primary antibody. In other instances, a polymer antibody conjugate is excited at about 405 nm in a flow cytometry assay where the specific signal is at least 3 fold greater than the same antibody conjugated to Pacific Blue. In some embodiments of conjugated polymers described herein, the polymer is purified by ion exchange chromatography. In other embodiments, the polymer is >95% pure. In some embodiments of conjugated polymers described herein, the polymer is used in flow cytometry assays to identify different cell markers or cell types. In other embodiments, the polymer is used to sort cells. In yet other embodiments, the polymer is used to sort cells for use in therapeutics. In some embodiments of conjugated polymers described herein, the polymer is used for intracellular staining. In certain instances, the polymer is used in flow cytometry assays to identify different cell markers or cell types. In some embodiments of conjugated polymers described herein, the polymer comprises a minimum number average molecular weight of greater than 40,000 g/mol and a water solubility of greater than 50 mg/mL in pure water or a phosphate buffered saline solution. In some embodiments of conjugated polymers described herein, the polymer comprises at least two unique conjugation linkers which can conjugated to two unique materials. Also provided herein are assay methods comprising providing a sample that is suspected of containing a target biomolecule; providing a sensor protein conjugated to at least one signaling chromophore and is capable of interacting with the target biomolecule or a target-associated biomolecule; providing a water soluble conjugated polymer described herein; contacting the sample with the sensor protein and the conjugated polymer in a solution under conditions in which the sensor protein can bind to the target biomolecule or a target-associated biomolecule if present; applying a light source to the sample that can excite the conjugated polymer; and detecting whether light is emitted from the signaling chromophore. In some embodiments, the sensor protein is an antibody. In other embodiments, the sensor protein comprises a plurality of sensor proteins conjugated to a plurality of signaling chromophores, wherein at least two of the plurality of chromophores emit different wavelengths of light upon energy transfer from the multichromophore. Also provided herein are conjugated polymer complexes comprising a polymer coupled to at least one biomolecule selected from the group consisting of a sensor biomolecule, a bioconjugate and a target biomolecule wherein the polymer is covalently bound by at least one bioconjugation site pendant thereto, and the polymer comprises a signaling chromophore or a signaling chromophore optionally is covalently bound to the polymer or the sensor biomolecule; wherein the polymer comprises the structure of formula: wherein: each R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 1 -C 12 alkoxy, C 2 -C 18 (hetero)aryloxy, C 2 -C 18 (hetero)arylamino, (CH 2 ) x′ (OCH 2 CH 2 ) y′ OCH 3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C 2 -C 18 (hetero)aryl group; each optional linker L 1 and L 2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another molecule, substrate or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G 1 and G 2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, and thiols within G 1 , G 2 , L 1 or L 2 that allows, for functional conjugation to another molecule, substrate or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. In some embodiments, the sensor biomolecule is selected from the group consisting of an avidin, streptavidin, neutravidin, avidinDN, and avidinD. In other embodiments, the conjugated polymer complex is further configured to bind to a complex selected from the group consisting of a biotin-labeled antibody, biotin-labeled protein, and biotin-labeled target biomolecule. In further embodiments, the sensor biomolecule is an antibody. In yet further embodiments, both the signaling chromophore and the sensor biomolecule are covalently linked to the multichromophore through a plurality of linkers. In some other embodiments, both the signaling chromophore and the sensor biomolecule are covalently linked to the polymer through a central linking site that covalently binds the polymer, the signaling chromophore and the sensor biomolecule. In yet other embodiments, the signaling chromophore, when covalently bound to the polymer or the sensor biomolecule, is an organic dye. Also provided herein are water soluble conjugated polymer having the structure of Formula (Ia): wherein: each R is independently (CH 2 ) x (OCH 2 CH 2 ) y OCH 3 where each x is independently an integer from 0-20, y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkoxy, or (OCH 2 CH 2 ) z OCH 3 where each z is independently an integer from 0 to 50; each optional linker L 1 or L 2 is selected from the group consisting of a-i having the structure *=site for covalent attachment to unsaturated backbone wherein R′ is independently H, halogen, C 1 -C 12 alkyl, (C 1 -C 12 alkyl)NH 2 , C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 2 -C 18 (hetero)aryl, C 2 -C 18 (hetero)arylamino, —[CH 2 —CH 2 ] r′ —Z 1 , or (C 1 -C 12 )alkoxy-X 1 ; and wherein Z 1 is —OH or —COOH; X 1 is —NH 2 , —NHCOOH, —NHCOOC(CH 3 ) 3 , —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH 2 —CH 2 —O] s′ (CH 2 ) s′ NH 2 ; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH 2 ) 3 (OCH 2 CH 2 ) x″ OCH 3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkoxy, or (OCH 2 CH 2 ) y″ OCH 3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein R 15 is selected from the group consisting of 1-t having the structure: and k is 2, 4, 8, 12 or 24; *=site for covalent attachment to backbone MU is a polymer modifying unit or band gap modifying unit that is selected from the group consisting of a′-k′ having the structure: *=site for covalent attachment to unsaturated backbone; wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; G 1 and G 2 are each independently selected from the group consisting of 1-31 having the structures: wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazids, hydrazones, azide, alkyne, aldehydes, and thiols within G 1 , G 2 , L 1 or L 2 that allows, for functional conjugation to another molecule, substrate or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. Also provided herein are water soluble conjugated polymer having the structure of Formula: wherein Ar is an aryl or heteroaryl and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 1 -C 12 alkoxy, C 2 -C 18 (hetero)aryloxy, C 2 -C 18 (hetero)arylamino, (CH 2 ) x′ (OCH 2 CH 2 ) y′ OCH 3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50; and dashed bonds, L 1 , L 2 , G 1 , G 2 , MU, a, b, c, d and n are described previously for formula (I)."},"cpc_label":{"kind":"string","value":"G01N3358"},"filing_date":{"kind":"string","value":"20170927"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180315"},"examiner_id":{"kind":"string","value":"86750.0"},"ipc_label":{"kind":"string","value":"G01N3358"},"npe_litigated_count":{"kind":"number","value":1,"string":"1"},"examiner_full_name":{"kind":"string","value":"TRUONG, DUC"},"invention_title":{"kind":"string","value":"Novel Reagents for Directed Biomarker Signal Amplification"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"G01N"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32889,"cells":{"application_number":{"kind":"number","value":15717580,"string":"15,717,580"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"Novel Reagents for Directed Biomarker Signal Amplification"},"abstract":{"kind":"string","value":"Described herein are methods, compositions and articles of manufacture involving neutral conjugated polymers including methods for synthesis of neutral conjugated water-soluble polymers with linkers along the polymer main chain structure and terminal end capping units. Such polymers may serve in the fabrication of novel optoelectronic devices and in the development of highly efficient biosensors. The invention further relates to the application of these polymers in assay methods."},"claims":{"kind":"string","value":"1.-40. (canceled) 41. A method of determining whether a target is present in a sample, the method comprising: contacting the sample with a conjugated polymer complex comprising a sensor for the target conjugated to a water soluble conjugated polymer having the structure of the formula: wherein: Ar is an aryl or heteroaryl unit substituted with a non-ionic side group capable of imparting solubility in water; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18 (hetero)aryloxy, C2-C18 (hetero)arylamino, a C2-C18 (hetero)aryl group and (CH2)x′(OCH2CH2)y′OCH3 where x′ is independently an integer from 0-20 and y′ is independently an integer from 0 to 50; optional linkers L1 and L2 are each independently an aryl or a heteroaryl group evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with: i) a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated ester, N-hydroxysuccinimidyl, hydrazine, hydrazide, hydrazone, azide, alkyne, aldehyde, thiol, and protected groups thereof for conjugation to a molecule or biomolecule; or ii) a conjugated organic dye or biomolecule; G1 and G2 are each independently selected from hydrogen, halogen, alkyne, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic ester, boronic acid, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with: i) a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazine, hydrazide, hydrazone, azide, alkyne, aldehyde, thiol, and protected groups thereof for conjugation to a molecule or biomolecule; or ii) a conjugated organic dye or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated ester, N-hydroxysuccinimidyl, hydrazines, hydrazide, hydrazone, azide, alkyne, aldehyde, and thiol within G1, G2, L1 or L2, or a conjugated organic dye or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. 42. The method according to claim 41, wherein MU is selected from optionally substituted benzothiadiazole, benzoxidazole, benzoselenadiazole, benzotellurodiazole, naphthoselenadiazole, 4,7-di(thien-2-yl)-2,1,3-benzothiadiazole, squaraine dyes, quinoxaline, perylene, perylene diimide, diketopyrrolopyrrole, thienopyrazine low bandgap commercial dyes, olefin, and cyano-substituted olefins and isomers thereof. 43. The method according to claim 41, wherein MU is selected from the group consisting of a′-k′ having the structure: wherein * is a site for covalent attachment to unsaturated backbone and each R is a non-ionic side group capable of imparting solubility in water. 44. The method according to claim 43, wherein MU is selected from one of the following: wherein * is site for covalent attachment to unsaturated backbone. 45. The method according to claim 41, wherein MU is a phenyl. 46. The method according to claim 45, wherein MU is wherein *=site for covalent attachment to unsaturated backbone. 47. The method according to claim 41, wherein the non-ionic side group comprises an ethylene glycol oligomer. 48. The method according to claim 47, wherein Ar is substituted with one or more non-ionic side groups comprising mPEG5, mPEG8, mPEG11 or mPEG24. 49. The method according to claim 47, wherein Ar is substituted with one or more groups selected from (CH2)x′(OCH2CH2)y′OCH3 where x′ is independently an integer from 0-20 and y′ is independently an integer from 0 to 50, and a benzyl substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)zOCH3 where z is independently an integer from 0 to 50. 50. The method according to claim 47, wherein Ar is substituted with one or more (CH2)x′(OCH2CH2)y′OCH3 where x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50. 51. The method according to claim 47, wherein Ar is substituted with a dendrimer of PAMAM, PEA, PEHAM, PPI, tri-branched benzoate, or glycerol with a generation of 1 to 4 and optional terminal substitutions selected from ( - - - )CH2CH2O)jCH3 and ( - - - )(OCH2CH2)jCH3 where j is an integer from 0 to 25 and the dotted lines ( - - - ) are each independently selected from any one or a combination of, C1-C12 alkyl, C1-C12 alkoxy, C2-C12 alkene, amido, amino, aryl, (CH2)r(OCH2CH2)s(CH2)r where each r is independently an integer from 0-20, s is independently an integer from 0 to 50, carbamate, carboxylate, C3-C12 cycloalkyl, imido, phenoxy and C4-C18(hetero)aryl group. 52. The method according to claim 41, wherein Ar is a substituted fluorene unit. 53. The method according to claim 41, wherein L1 and/or L2 is conjugated to a signaling chromophore. 54. The method according to claim 41, wherein L1 and/or L2 are present and have the structure: wherein: *=site for covalent attachment to backbone; each R25 is independently a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl; (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50; aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups; and at least one R25 is terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated ester, N-hydroxysuccinimidyl, hydrazine, hydrazide, hydrazone, azide, alkyne, aldehyde and thiols, or a conjugated organic dye or biomolecule. 55. The method according to claim 41, wherein at least one of G1 and G2 comprises a functional conjugation site. 56. The method according to claim 55, wherein at least one of G1 and G2 has the structure: wherein: *=site for covalent attachment to backbone; and R11 is a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x wherein each x is independently an integer from 0-20 and p is an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonate, sulfide, disulfide, or imido groups; and is terminated with: i) a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof, or ii) a conjugated organic dye or biomolecule. 57. The method according to claim 41, wherein at least one of G1 and G2 is selected from the group consisting of capping units 1-31 having the structures: wherein: *=site for covalent attachment to backbone; k is 2, 4, 8, 12 or 24; and R15 is selected from the group consisting of l-t having the structures: 58. The method according to claim 41, wherein the sensor is an antibody. 59. The method according to claim 41, wherein the method is configured for intracellular staining. 60. The method according to claim 41, wherein the method is configured for flow cytometry."},"description":{"kind":"string","value":"CROSS-REFERENCE This application is a continuation of application Ser. No. 15/239,713, filed Aug. 17, 2016; which application is a continuation of application Ser. No. 14/821,386, filed Aug. 7, 2015 and issued as U.S. Pat. No. 9,547,008; which application is a continuation of application Ser. No. 14/018,985, filed Sep. 5, 2013 and issued as U.S. Pat. No. 9,139,869; which application is a continuation of application Ser. No. 13/009,764, filed Jan. 19, 2011 and issued as U.S. Pat. No. 8,575,303, which claims the benefit of U.S. Provisional Application Ser. No. 61/296,379, filed Jan. 19, 2010 and U.S. Provisional Application Ser. No. 61/358,406, filed Jun. 24, 2010, which applications are incorporated herein by reference in their entireties. BACKGROUND OF THE INVENTION Fluorescent hybridization probes have developed into an important tool in the sequence-specific detection of DNA and RNA. The signals generated by the appended fluorescent labels (or dyes) can be monitored in real time and provide simple, rapid, and robust methods for the detection of biological targets and events. Utility has been seen in applications ranging from microarrays and real time PCR to fluorescence in situ hybridization (FISH). Recent work in the area of multichromophores, particularly regarding conjugated polymers (CPs) has highlighted the potential these materials have in significantly improving the detection sensitivity of such methods (Liu and Bazan, Chem. Mater., 2004). The light harvesting structures of these materials can be made water soluble and adapted to amplify the fluorescent output of various probe labels (See U.S. patent application Ser. No. 10/600,286, filed Jun. 20, 2003 and Gaylord, Heeger, and Bazan, Proc. Natl. Acad. Sci., 2002, both of which are incorporated herein by reference in their entirety). Results such as these indicate CPs to be highly promising in the field of nucleic acid diagnostics, particularly where sample quantities are scarce. However, there exist methods for the amplification (or replication) of nucleic acid targets, i.e., PCR. Comparatively, in the field of protein recognition, there are no such simple methods for amplifying the targeted materials. As such, signal enhancement arising from CP application is of high consequence in this area. Dye-labeled antibodies are regularly used for the detection of protein targets in applications such as immunohistochemistry, protein arrays, ELISA tests, and flow cytometry. Integrating CP materials into such methodologies promises to provide a dramatic boost in the performance of such assays, enabling detection levels previously unattainable with conventional fluorescent reporters (e.g., dyes). Beyond addition signal, one of the other key drivers in biological detection formats is the ability to detect multiple analytes in the same test or multiplexing. This is commonly achieved by using fluorescent reporters with operate at different, discernable wavelengths. CP materials are ideally suited to provide a platform for expanded multiplexing. This can be achieved by tuning the structure of different CPs to operate at different wavelengths or by incorporating a dye within the polymer-biomolecule conjugate. The material and methods to produce higher sensitivity biological assays and increase multiplexing are highly desired in both molecular (nucleic acid) and immunoassay formats. SUMMARY OF THE INVENTION Provided herein are water soluble conjugated polymers of Formula (I): wherein: each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x′(OCH2CH2)y′OCH3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C2-C18(hetero)aryl group; each optional linker L1 and L2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another substrate, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G1 and G2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, and thiols within G1, G2, L1 or L2 that allows, for functional conjugation to another molecule, substrate or biomolecule; each dashed bond, , is independently a single bond, triple bond or optionally substituted vinylene (—CR5═CR5—) wherein each R5 is independently hydrogen, cyano, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. In one aspect, water soluble conjugated polymers of Formula (I) have the structure of Formula (Ia): wherein R, L1, L2, G1, G2, MU, a, b, c, d and n are described previously for formula (I). In some embodiments, each R is independently (CH2)x(OCH2CH2)yOCH3 where each x is independently an integer from 0-20, each y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)zOCH3 where each z is independently an integer from 0 to 50. In some instances, each R is (CH2)3(OCH2CH2)11CH3. In other embodiments, each R is a benzyl substituted with at least one (OCH2CH2)10OCH3 group. In some instances, the benzyl is substituted with two (OCH2CH2)10OCH3 groups. In other instances, the benzyl is substituted with three (OCH2CH2)10OCH3 groups. In some embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to unsaturated backbone; wherein R3 is independently hydrogen, halogen, alkoxy(C1-C12), C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and q is an integer from 0 to 4. In other embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to unsaturated backbone wherein A is a site for conjugation, chain extension or crosslinking and is [O—CH2—CH2]q—W, or (C1-C12)alkoxy-X or C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; W is —OH or —COOH; X is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]tNH2; q is an integer from 1 to 20; and t is an integer from 1 to 8. In yet other embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to backbone wherein R25 are each independently any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups; wherein at least one R25 is terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In further embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to unsaturated backbone; wherein R35 is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In further embodiments, optional linkers L1 or L2 are selected from the group consisting of a-h having the structures: *=site for covalent attachment to unsaturated backbone; wherein R′ is independently H, halogen, C1-C12 alkyl, (C1-C12 alkyl)NH2, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C2-C18(hetero)aryl, C2-C18(hetero)arylamino, —[CH2—CH2]r′—Z1, or (C1-C12)alkoxy-X1; and wherein Z1 is —OH or —COOH; X1 is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]s′(CH2)s′NH2; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH2)3(OCH2CH2)x″OCH3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)y—OCH3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein k is 2, 4, 8, 12 or 24; wherein R15 is selected from the group consisting of l-t having the structure: *=site for covalent attachment to backbone. In yet further embodiments, optional linkers L1 or L2 are In some embodiments, G1 and G2 are each independently selected from hydrogen, halogen, alkyne, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorine and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In some embodiments, G1 and G2 each independently have the structure wherein R11 is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In other embodiments, G1 and G2 are each independently selected from the group consisting of 1-31 having the structures: *=site for covalent attachment to backbone wherein R15 is selected from the group consisting of l-t having the structure: and k is 2, 4, 8, 12 or 24. In further embodiments, G1 and G2 are optionally substituted aryl or heteroaryl wherein the optional substituent is selected from halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiol, boronic acid, boronate radical, boronic esters and optionally substituted fluorene. In some embodiments, G1 and G2 are the same. In other embodiments, G1 and G2 are different. In further embodiments, the polymer contains a single conjugation site at only one terminus of the polymer chain G1 or G2. In yet further embodiments, G1 and G2 is In some embodiments, MU is selected from the group consisting of a′-k′ having the structure: *=site for covalent attachment to unsaturated backbone wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein at least one of G1 or G2 comprises a functional conjugation site. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein L1 comprises a functional conjugation site. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein at least one of G1 or G2 comprises a functional conjugation site. In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In some instances, a signaling chromophore is attached to the polymer via the NH2 group. In certain instances, the signaling chromophore is Cy3 or Dylight 594 dye. In certain instances, the linker, is about 10% of the entire polymer. In other instances, the polymer is conjugated to a secondary dye reporter and an antibody. In some embodiments of conjugated polymers described herein, the polymer is further conjugated to additional molecules. In some embodiments, the polymer is conjugated to a streptavidin, antibody or nucleic acid and used as a direct fluorescent reporter. In certain embodiments, the polymer is conjugated to a streptavidin. In other embodiments, the polymer is conjugated to thiol groups at the hinge region of an antibody. In yet other embodiments, the polymer is conjugated to an amine group on a protein which is modified with a heterobifunctional linker. In further embodiments, the polymer is conjugated to a nucleic acid. In yet further embodiments, the polymer is conjugated to an antibody. In certain instances, the polymer is conjugated to a monoclonal antibody, a secondary antibody or a primary antibody. In other instances, a polymer antibody conjugate is excited at about 405 nm in a flow cytometry assay where the specific signal is at least 3 fold greater than the same antibody conjugated to Pacific Blue. In some embodiments of conjugated polymers described herein, the polymer is purified by ion exchange chromatography. In other embodiments, the polymer is >95% pure. In some embodiments of conjugated polymers described herein, the polymer is used in flow cytometry assays to identify different cell markers or cell types. In other embodiments, the polymer is used to sort cells. In yet other embodiments, the polymer is used to sort cells for use in therapeutics. In some embodiments of conjugated polymers described herein, the polymer is used for intracellular staining. In certain instances, the polymer is used in flow cytometry assays to identify different cell markers or cell types. In some embodiments of conjugated polymers described herein, the polymer comprises a minimum number average molecular weight of greater than 40,000 g/mol and a water solubility of greater than 50 mg/mL in pure water or a phosphate buffered saline solution. In some embodiments of conjugated polymers described herein, the polymer comprises at least two unique conjugation linkers which can conjugated to two unique materials. Also provided herein are assay methods comprising providing a sample that is suspected of containing a target biomolecule; providing a sensor protein conjugated to at least one signaling chromophore and is capable of interacting with the target biomolecule or a target-associated biomolecule; providing a water soluble conjugated polymer described herein; contacting the sample with the sensor protein and the conjugated polymer in a solution under conditions in which the sensor protein can bind to the target biomolecule or a target-associated biomolecule if present; applying a light source to the sample that can excite the conjugated polymer; and detecting whether light is emitted from the signaling chromophore. In some embodiments, the sensor protein is an antibody. In other embodiments, the sensor protein comprises a plurality of sensor proteins conjugated to a plurality of signaling chromophores, wherein at least two of the plurality of chromophores emit different wavelengths of light upon energy transfer from the multichromophore. Also provided herein are conjugated polymer complexes comprising a polymer coupled to at least one biomolecule selected from the group consisting of a sensor biomolecule, a bioconjugate and a target biomolecule wherein the polymer is covalently bound by at least one bioconjugation site pendant thereto, and the polymer comprises a signaling chromophore or a signaling chromophore optionally is covalently bound to the polymer or the sensor biomolecule; wherein the polymer comprises the structure of formula: wherein: each R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x′(OCH2CH2)y′OCH3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C2-C18(hetero)aryl group; each optional linker L1 and L2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another molecule, substrate or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G1 and G2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, and thiols within G1, G2, L1 or L2 that allows, for functional conjugation to another molecule, substrate or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. In some embodiments, the sensor biomolecule is selected from the group consisting of an avidin, streptavidin, neutravidin, avidinDN, and avidinD. In other embodiments, the conjugated polymer complex is further configured to bind to a complex selected from the group consisting of a biotin-labeled antibody, biotin-labeled protein, and biotin-labeled target biomolecule. In further embodiments, the sensor biomolecule is an antibody. In yet further embodiments, both the signaling chromophore and the sensor biomolecule are covalently linked to the multichromophore through a plurality of linkers. In some other embodiments, both the signaling chromophore and the sensor biomolecule are covalently linked to the polymer through a central linking site that covalently binds the polymer, the signaling chromophore and the sensor biomolecule. In yet other embodiments, the signaling chromophore, when covalently bound to the polymer or the sensor biomolecule, is an organic dye. Also provided herein are water soluble conjugated polymer having the structure of Formula (Ia): wherein: each R is independently (CH2)x(OCH2CH2)yOCH3 where each x is independently an integer from 0-20, y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)zOCH3 where each z is independently an integer from 0 to 50; each optional linker L1 or L2 is selected from the group consisting of a-i having the structure *=site for covalent attachment to unsaturated backbone wherein R′ is independently H, halogen, C1-C12 alkyl, (C1-C12 alkyl)NH2, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C2-C18(hetero)aryl, C2-C18(hetero)arylamino, —[CH2—CH2]r′—Z1, or (C1-C12)alkoxy-X1; and wherein Z1 is —OH or —COOH; X1 is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]s′(CH2)s′NH2; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH2)3(OCH2CH2)x″OCH3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)y″OCH3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein R15 is selected from the group consisting of l-t having the structure: and k is 2, 4, 8, 12 or 24; *=site for covalent attachment to backbone MU is a polymer modifying unit or band gap modifying unit that is selected from the group consisting of a′-k′ having the structure: *=site for covalent attachment to unsaturated backbone; wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; G1 and G2 are each independently selected from the group consisting of 1-31 having the structures: wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, and thiols within G1, G2, L1 or L2 that allows, for functional conjugation to another molecule, substrate or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. Also provided herein are water soluble conjugated polymer having the structure of Formula: wherein Ar is an aryl or heteroaryl and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x′(OCH2CH2)y′OCH3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50; and dashed bonds, L1, L2, G1, G2, MU, a, b, c, d and n are described previously for formula (I). INCORPORATION BY REFERENCE All publications, patents, and patent applications mentioned in this specification are herein incorporated by reference to the same extent as if each individual publication, patent, or patent application was specifically and individually indicated to be incorporated by reference. BRIEF DESCRIPTION OF THE DRAWINGS The novel features of the invention are set forth with particularity in the appended claims. A better understanding of the features and advantages of the present invention will be obtained by reference to the following detailed description that sets forth illustrative embodiments, in which the principles of the invention are utilized, and the accompanying drawings of which: FIG. 1. Schematic of binding of a conjugated polymer in one embodiment of the invention. FIG. 2. Schematic of a bioconjugated polymer of one embodiment of the invention. FIG. 3. Schematic of exemplary conjugated polymers conjugated (A) antibody; (B) an avidin; (C) nucleic acid; (D) dye, e.g., chromophore. FIG. 4. Schematic of (A) a polymer conjugated to dye-labeled antibody resulting in FRET; (B) a polymer conjugated dye-labeled strepavidin resulting in FRET; (C) nucleic acid probe sequences labeled with a quencher molecule conjugated to a conjugated polymer; (D) nucleic acid probe sequences labeled with a quencher molecule conjugated polymer-dye tandem complex. FIG. 5. Schematic of various methods of assaying for a target biomolecule or target associated biomolecule. (A) Conjugated polymer linked to a bioconjugate; (B) polymer and dye labeled antibodies recognize a common target; (C) sensor biomolecule conjugated to both a dye and a second bioconjugate; (D) second bioconjugate and the signaling chromophore both conjugated to a nucleic acid. FIG. 6. Schematic of an addition of a second linking site within the polymer. FIG. 7. Schematic of a polymer conjugated to a dye and a biomolecule and resulting energy transfer (A) polymer is conjugated to both a bioconjugate; (B) polymer is conjugated to a strepavidin and a dye; (C) polymer is conjugated to a nucleic acid and a dye. FIG. 8. Schematic of indirect associations with a sensor biomolecule or target associated biomolecule. (A) biotinylated antibody interacting with a covalent conjugate of the conjugated polymer; (B) biotinylated antibody conjugated polymer-dye tandem complex; (C) biotinylated nucleic acid interacting with a covalent conjugate of the conjugated polymer; (D) biotinylated nucleic conjugated polymer-dye tandem complex; (E) nucleic acid with digoxygenin moiety interacting with a covalent conjugate of the conjugated polymer; (F) nucleic acid with digoxygenin moiety conjugated polymer-dye tandem complex. FIG. 9. Schematic of exemplary conjugated polymers conjugated to secondary antibodies ( ) and primary antibodies (B). FIG. 10. Schematic of a sandwich-type complex. (A) conjugated polymer complex bioconjugated to a strepavidin; (B) biotin-labeled 1° antibody e used to probe the target protein directly. FIG. 11. Schematic of appending one or two phenyl capping units to a fluorene polymer. FIG. 12. Block diagram showing a representative example logic device. FIG. 13. Block diagram showing a representative example of a kit. FIG. 14. Schematic of a streptavidin conjugation with a conjugated polymer and the resulting conjugate structure (top) and Coomassie stained agarose gel representative of the streptavidin-attached CP (below). FIG. 15. Representative acrylamide gel depiction of biotinylated polymer alone or bound to Cy5-labeled streptavidin. FIG. 16. Schematic of streptavidin-attached conjugated polymer of FIG. 14 binding to biotinylated microspheres (top) and plot of fluorescence excitation of control biotinylated microspheres and microspheres bound to streptavidin conjugated polymer. FIG. 17. Schematic of streptavidin-attached conjugated polymer of FIG. 14 selectively bound to biotinylated microspheres and energy transfer to dye acceptors on co-localized streptavidin-dye conjugates (top) and plot of energy transfer from streptavidin-attached conjugated polymer to dye acceptor (bottom). FIG. 18. Schematic of biotinylated polymer of FIG. 14 binding to streptavidin coated microspheres (top) and plot of fluorescence excitation of control streptavidin coated microspheres and microspheres bound to biotinylated polymer. FIG. 19. Schematic of biotinylated polymer of FIG. 14 binding to dye-labeled streptavidin conjugates and FRET (top); plot of energy transfer from biotinylated polymer to two different dye acceptors (bottom left) and titration plot of polymer saturation (bottom right). FIG. 20. Flow cytometry analysis of CD4 marking of Cyto-trol cells with 440 nm polymer-streptavidin-conjugates. FIG. 21. (A) Polymer structure of Example 38b conjugated to (from left to right) FITC, Cy3, DyLight 594 and DyLight633; (B) Comparison of the fluorescence of the dye (DyLight594) excited near its absorbance maximum (lower curve) and polymer-dye conjugate excited at 405 nm (upper curve); (C) Comparison of the fluorescent signal of the base polymer (no dye, peak emission near 420 nm) to that of the polymer-dye conjugate (peak emission near 620 nm). FIG. 22. Plot of flow testing of monoclonal antibody (antiCD4) conjugates on whole lysed blood samples. FIG. 23. Plot of florescence of a dye (DyLight594) and a polymer-dye conjugate by excitation of dye at 594 nm and the polymer-dye conjugate at 380 nm. FIG. 24. Plot of fluorescent immunoassay (ELISA) with streptavidin-attached conjugated polymer. FIG. 25. Plot of fluorescent intensity vs. temperature of a DNA oligomer-polymer conjugate hybridized to a target. FIG. 26. Ion exchange chromatogram for a polymer antibody conjugate to remove free polymer (left) and an SEC chromatogram showing the separation of final conjugate from free antibody. In both chromatograms absorbance was monitored at 280 nm (lower curves) and 407 nm (upper curves). FIG. 27. Sandwich immunoassay on Luminex assay (left) and corresponding results on the Luminex system using 532 nm excitation of both the conjugated polymer and PE streptavidin detection conjugates. FIG. 28. Data on left show results obtained with compensation beads while the data set on the right results from a 4 color assay on human blood samples. FIGS. 29. (A) and (B) Schematic of covalent linkage of conjugated polymer to 2° antibody. FIG. 30. Schematic of conjugated polymers in Fluorescent Immuno Assay (FIA). (A) conjugated polymer covalently linked to a detection antibody; (B) biotin binding protein covalently bound to the conjugated polymer and interacting with a biotinylated detection antibody; (C) secondary antibody covalently linked to the conjugated polymer and interacting with a detection antibody. FIG. 31. (A) Schematic of nucleic acid probe sequences labeled with a quencher molecule conjugated to a conjugated polymer; (B) nucleic acid probe sequences labeled with a quencher molecule conjugated to a conjugated polymer-dye tandem complex. FIG. 32. Schematic of modifications of the HybProbe detection technique. (A) conjugated polymer covalently linked to the donor probe and resulting energy transfer to acceptor probe; (B) “Signal off” modification of the HybProbe approach where the conjugated polymer is quenched by an acceptor probe. FIG. 33. Comparison of non-specific binding in various polymers (top) in a Jurkat cell (lymphocyte cell line) model; (bottom) plot ranking the polymers in terms of signal generated purely by non-specific binding (NSB). FIG. 34. Histograms collected from flow cytometry analysis (405 nm excitation in a BD LSR-II cytometer) using a Jurkat cell line; (left) unstained cells and a negative control, anionic P4 polymer; (middle) range of different polymer and polymer side chain combinations tested on the same cells; (right) neutral polymer P20 showed almost no off set from the untreated cells. FIG. 35. Gel electrophoresis depicting relative mobility of avidin as a function of the degree of conjugation with polymer AA1. FIG. 36. Fractionation of crude polymer-avidin conjugate mixtures on a Superdex 200 size exclusion column; (top) monitoring fractions by UV absorbance; (bottom) gel electrophoresis of selected fractions to visualize the degree to which avidin was attached to polymer. FIG. 37. Gel electrophoresis of conjugation reactions performed with polymer in varying molar excess to streptavidin; (left) UV illumination; (right) 532 nm excitation. FIG. 38. Plot depicting purification of polymer streptavidin conjugates with polymers exemplified in Example 9, denoted P30, (top) crude samples; (bottom) purified conjugates). DETAILED DESCRIPTION OF THE INVENTION Before the present invention is described in further detail, it is to be understood that this invention is not limited to the particular methodology, devices, solutions or apparatuses described, as such methods, devices, solutions or apparatuses can, of course, vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the present invention. Use of the singular forms “a,” “an,” and “the” include plural references unless the context clearly dictates otherwise. Thus, for example, reference to “an aggregation sensor” includes a plurality of aggregation sensors, reference to “a probe” includes a plurality of probes, and the like. Additionally, use of specific plural references, such as “two,” “three,” etc., read on larger numbers of the same subject less the context clearly dictates otherwise. Terms such as “connected,” “attached,” “conjugated” and “linked” are used interchangeably herein and encompass direct as well as indirect connection, attachment, linkage or conjugation unless the context clearly dictates otherwise; in one example, the phrase “conjugated polymer” is used in accordance with its ordinary meaning in the art and refers to a polymer containing an extended series of unsaturated bonds, and that context dictates that the term “conjugated” should be interpreted as something more than simply a direct or indirect connection, attachment or linkage. Where a range of values is recited, it is to be understood that each intervening integer value, and each fraction thereof, between the recited upper and lower limits of that range is also specifically disclosed, along with each subrange between such values. The upper and lower limits of any range can independently be included in or excluded from the range, and each range where either, neither or both limits are included is also encompassed within the invention. Where a value being discussed has inherent limits, for example where a component can be present at a concentration of from 0 to 100%, or where the pH of an aqueous solution can range from 1 to 14, those inherent limits are specifically disclosed. Where a value is explicitly recited, it is to be understood that values which are about the same quantity or amount as the recited value are also within the scope of the invention, as are ranges based thereon. Where a combination is disclosed, each subcombination of the elements of that combination is also specifically disclosed and is within the scope of the invention. Conversely, where different elements or groups of elements are disclosed, combinations thereof are also disclosed. Where any element of an invention is disclosed as having a plurality of alternatives, examples of that invention in which each alternative is excluded singly or in any combination with the other alternatives are also hereby disclosed; more than one element of an invention can have such exclusions, and all combinations of elements having such exclusions are hereby disclosed. Unless defined otherwise or the context clearly dictates otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the invention, the preferred methods and materials are now described. All publications mentioned herein are hereby incorporated by reference for the purpose of disclosing and describing the particular materials and methodologies for which the reference was cited. The publications discussed herein are provided solely for their disclosure prior to the filing date of the present application. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention. Definitions In describing the present invention, the following terms will be employed, and are intended to be defined as indicated below. “Alkyl” refers to a branched, unbranched or cyclic saturated hydrocarbon group of 1 to 24 carbon atoms optionally substituted at one or more positions, and includes polycyclic compounds. Examples of alkyl groups include optionally substituted methyl, ethyl, n-propyl, isopropyl, n-butyl, s-butyl, t-butyl, n-pentyl, isopentyl, neopentyl, n-hexyl, n-heptyl, n-octyl, n-decyl, hexyloctyl, tetradecyl, hexadecyl, eicosyl, tetracosyl and the like, as well as cycloalkyl groups such as cyclopropyl, cyclobutyl, cyclopentyl, cyclohexyl, cycloheptyl, cyclooctyl, adamantyl, and norbornyl. The term “lower alkyl” refers to an alkyl group of 1 to 6 carbon atoms, preferably 1 to 4 carbon atoms. Exemplary substituents on substituted alkyl groups include hydroxyl, cyano, alkoxy, ═O, ═S, —NO2, halogen, haloalkyl, heteroalkyl, carboxyalkyl, amine, amide, thioether and —SH. “Alkoxy” refers to an “—Oalkyl” group, where alkyl is as defined above. A “lower alkoxy” group intends an alkoxy group containing one to six, more preferably one to four, carbon atoms. “Alkenyl” refers to a branched, unbranched or cyclic hydrocarbon group of 2 to 24 carbon atoms containing at least one carbon-carbon double bond optionally substituted at one or more positions. Examples of alkenyl groups include ethenyl, 1-propenyl, 2-propenyl (allyl), 1-methylvinyl, cyclopropenyl, 1-butenyl, 2-butenyl, isobutenyl, 1,4-butadienyl, cyclobutenyl, 1-methylbut-2-enyl, 2-methylbut-2-en-4-yl, prenyl, pent-1-enyl, pent-3-enyl, 1,1-dimethylallyl, cyclopentenyl, hex-2-enyl, 1-methyl-1-ethylallyl, cyclohexenyl, heptenyl, cycloheptenyl, octenyl, cyclooctenyl, decenyl, tetradecenyl, hexadecenyl, eicosenyl, tetracosenyl and the like. Preferred alkenyl groups herein contain 2 to 12 carbon atoms. The term “lower alkenyl” intends an alkenyl group of 2 to 6 carbon atoms, preferably 2 to 4 carbon atoms. The term “cycloalkenyl” intends a cyclic alkenyl group of 3 to 8, preferably 5 or 6, carbon atoms. Exemplary substituents on substituted alkenyl groups include hydroxyl, cyano, alkoxy, ═O, ═S, —NO2, halogen, haloalkyl, heteroalkyl, amine, thioether and —SH. “Alkenyloxy” refers to an “—Oalkenyl” group, wherein alkenyl is as defined above. “Alkylaryl” refers to an alkyl group that is covalently joined to an aryl group. Preferably, the alkyl is a lower alkyl. Exemplary alkylaryl groups include benzyl, phenethyl, phenopropyl, 1-benzylethyl, phenobutyl, 2-benzylpropyl and the like. “Alkylaryloxy” refers to an “—Oalkylaryl” group, where alkylaryl is as defined above. “Alkynyl” refers to a branched or unbranched hydrocarbon group of 2 to 24 carbon atoms containing at least one —C “Amide” refers to —C(O)NR′R″, where R′ and R″ are independently selected from hydrogen, alkyl, aryl, and alkylaryl. “Amine” refers to an —N(R′)R″ group, where R′ and R″ are independently selected from hydrogen, alkyl, aryl, and alkylaryl. “Aryl” refers to an aromatic group that has at least one ring having a conjugated pi electron system and includes carbocyclic, heterocyclic, bridged and/or polycyclic aryl groups, and can be optionally substituted at one or more positions. Typical aryl groups contain 1 to 5 aromatic rings, which may be fused and/or linked. Exemplary aryl groups include phenyl, furanyl, azolyl, thiofuranyl, pyridyl, pyrimidyl, pyrazinyl, triazinyl, biphenyl, indenyl, benzofuranyl, indolyl, naphthyl, quinolinyl, isoquinolinyl, quinazolinyl, pyridopyridinyl, pyrrolopyridinyl, purinyl, tetralinyl and the like. Exemplary substituents on optionally substituted aryl groups include alkyl, alkoxy, alkyl carboxy, alkenyl, alkenyloxy, alkenylcarboxy, aryl, aryloxy, alkylaryl, alkylaryloxy, fused saturated or unsaturated optionally substituted rings, halogen, haloalkyl, heteroalkyl, —S(O)R, sulfonyl, —SO3R, —SR, —NO2, —NRR′, —OH, —CN, —C(O)R, —OC(O)R, —NHC(O)R, —(CH2)n—CO2R or —(CH2)n—CONRR′ where n is 0-4, and wherein R and R′ are independently H, alkyl, aryl or alkylaryl. “Aryloxy” refers to an “—Oaryl” group, where aryl is as defined above. “Carbocyclic” refers to an optionally substituted compound containing at least one ring and wherein all ring atoms are carbon, and can be saturated or unsaturated. “Carbocyclic aryl” refers to an optionally substituted aryl group wherein the ring atoms are carbon. “Halo” or “halogen” refers to fluoro, chloro, bromo or iodo. “Halide” refers to the anionic form of the halogens. “Haloalkyl” refers to an alkyl group substituted at one or more positions with a halogen, and includes alkyl groups substituted with only one type of halogen atom as well as alkyl groups substituted with a mixture of different types of halogen atoms. Exemplary haloalkyl groups include trihalomethyl groups, for example trifluoromemyl. “Heteroalkyl” refers to an alkyl group wherein one or more carbon atoms and associated hydrogen atom(s) are replaced by an optionally substituted heteroatom, and includes alkyl groups substituted with only one type of heteroatom as well as alkyl groups substituted with a mixture of different types of heteroatoms. Heteroatoms include oxygen, sulfur, and nitrogen. As used herein, nitrogen heteroatoms and sulfur heteroatoms include any oxidized form of nitrogen and sulfur, and any form of nitrogen having four covalent bonds including protonated forms. An optionally substituted heteroatom refers to replacement of one or more hydrogens attached to a nitrogen atom with alkyl, aryl, alkylaryl or hydroxyl. “Heterocyclic” refers to a compound containing at least one saturated or unsaturated ring having at least one heteroatom and optionally substituted at one or more positions. Typical heterocyclic groups contain 1 to 5 rings, which may be fused and/or linked, where the rings each contain five or six atoms. Examples of heterocyclic groups include piperidinyl, morpholinyl and pyrrolidinyl. Exemplary substituents for optionally substituted heterocyclic groups are as for alkyl and aryl at ring carbons and as for heteroalkyl at heteroatoms. “Heterocyclic aryl” refers to an aryl group having at least 1 heteroatom in at least one aromatic ring. Exemplary heterocyclic aryl groups include furanyl, thienyl, pyridyl, pyridazinyl, pyrrolyl, N-lower alkyl-pyrrolo, pyrimidyl, pyrazinyl, triazinyl, tetrazinyl, triazolyl, tetrazolyl, imidazolyl, bipyridyl, tripyridyl, tetrapyridyl, phenazinyl, phenanthrolinyl, purinyl, perylene, perylene diimide, diketopyrrolopyrrole, benzothiadiazol, benzoxadiazol, thienopyrazine and the like. “Hydrocarbyl” refers to hydrocarbyl substituents containing 1 to about 20 carbon atoms, including branched, unbranched and cyclic species as well as saturated and unsaturated species, for example alkyl groups, alkylidenyl groups, alkenyl groups, alkylaryl groups, aryl groups, and the like. The term “lower hydrocarbyl” intends a hydrocarbyl group of one to six carbon atoms, preferably one to four carbon atoms. A “substituent” refers to a group that replaces one or more hydrogens attached to a carbon or nitrogen. Exemplary substituents include alkyl, alkylidenyl, alkylcarboxy, alkoxy, alkenyl, alkenylcarboxy, alkenyloxy, aryl, aryloxy, alkylaryl, alkylaryloxy, —OH, amide, carboxamide, carboxy, sulfonyl, ═O, ═S, —NO2, halogen, haloalkyl, fused saturated or unsaturated optionally substituted rings, —S(O)R, —SO3R, —SR, —NRR′, —OH, —CN, —C(O)R, —OC(O)R, —NHC(O)R, —(CH2)nCO2R or —(CH2)nCONRR′ where n is 0-4, and wherein R and R′ are independently H, alkyl, aryl or alkylaryl. Substituents also include replacement of a carbon atom and one or more associated hydrogen atoms with an optionally substituted heteroatom. “Sulfonyl” refers to —S(O)2R, where R is alkyl, aryl, —C(CN)═C-aryl, —CH2CN, alkylaryl, or amine. “Thioamide” refers to —C(S)NR′R″, where R′ and R″ are independently selected from hydrogen, alkyl, aryl, and alkylaryl. “Thioether” refers to —SR, where R is alkyl, aryl, or alkylaryl. As used herein, the term “binding pair” refers to first and second molecules that bind specifically to each other with greater affinity than to other components in the sample. The binding between the members of the binding pair is typically noncovalent. Exemplary binding pairs include immunological binding pairs (e.g. any haptenic or antigenic compound in combination with a corresponding antibody or binding portion or fragment thereof, for example digoxigenin and anti-digoxigenin, fluorescein and anti-fluorescein, dinitrophenol and anti-dinitrophenol, bromodeoxyuridine and anti-bromodeoxyuridine, mouse immunoglobulin and goat anti-mouse immunoglobulin) and nonimmunological binding pairs (e.g., biotin-avidin, biotin-streptavidin, hormone [e.g., thyroxine and cortisol]-hormone binding protein, receptor-receptor agonist or antagonist (e.g., acetylcholine receptor-acetylcholine or an analog thereof) IgG-protein A, lectin-carbohydrate, enzyme-enzyme cofactor, enzyme-enzyme-inhibitor, and complementary polynucleotide pairs capable of forming nucleic acid duplexes) and the like. One or both member of the binding pair can be conjugated to additional molecules. The terms “polynucleotide,” “oligonucleotide,” “nucleic acid” and “nucleic acid molecule” are used interchangeably herein to refer to a polymeric form of nucleotides of any length, and may comprise ribonucleotides, deoxyribonucleotides, analogs thereof, or mixtures thereof. These terms refer only to the primary structure of the molecule. Thus, the terms includes triple-, double- and single-stranded deoxyribonucleic acid (“DNA”), as well as triple-, double- and single-stranded ribonucleic acid (“RNA”). It also includes modified, for example by alkylation, and/or by capping, and unmodified forms of the polynucleotide. Additional details for these terms as well as for details of base pair formation can be found in U.S. application Ser. No. 11/344,942, filed Jan. 31, 2006, which is incorporate herein by reference in its entirety. “Complementary” or “substantially complementary” refers to the ability to hybridize or base pair between nucleotides or nucleic acids, such as, for instance, between a sensor peptide nucleic acid and a target polynucleotide. Complementary nucleotides are, generally, A and T (or A and U), or C and G. Two single-stranded polynucleotides or PNAs are said to be substantially complementary when the bases of one strand, optimally aligned and compared and with appropriate insertions or deletions, pair with at least about 80% of the bases of the other strand, usually at least about 90% to 95%, and more preferably from about 98 to 100%. Alternatively, substantial complementarity exists when a polynucleotide or PNA will hybridize under selective hybridization conditions to its complement. Typically, selective hybridization will occur when there is at least about 65% complementary over a stretch of at least 14 to 25 bases, preferably at least about 75%, more preferably at least about 90% complementary. See, M. Kanehisa Nucleic Acids Res. 12:203(1984). “Preferential binding” or “preferential hybridization” refers to the increased propensity of one polynucleotide or PNA to bind to its complement in a sample as compared to a noncomplementary polymer in the sample. Hybridization conditions for polynucleotides will typically include salt concentrations of less than about 1M, more usually less than about 500 mM and preferably less than about 200 mM. In the case of hybridization between a peptide nucleic acid and a polynucleotide, the hybridization can be done in solutions containing little or no salt. Hybridization temperatures can be as low as 5° C., but are typically greater than 22° C., more typically greater than about 30° C., and preferably in excess of about 37° C. Longer fragments may require higher hybridization temperatures for specific hybridization. Other factors may affect the stringency of hybridization, including base composition and length of the complementary strands, presence of organic solvents and extent of base mismatching, and the combination of parameters used is more important than the absolute measure of any one alone. Other hybridization conditions which may be controlled include buffer type and concentration, solution pH, presence and concentration of blocking reagents to decrease background binding such as repeat sequences or blocking protein solutions, detergent type(s) and concentrations, molecules such as polymers which increase the relative concentration of the polynucleotides, metal ion(s) and their concentration(s), chelator(s) and their concentrations, and other conditions known in the art. “Multiplexing” herein refers to an assay or other analytical method in which multiple analytes can be assayed simultaneously. “Having” is an open ended phrase like “comprising” and “including,” and includes circumstances where additional elements are included and circumstances where they are not. “Optional” or “optionally” means that the subsequently described event or circumstance may or may not occur, and that the description includes instances where the event or circumstance occurs and instances in which it does not. The embodiments disclosed herein relate generally to compositions of conjugated polymer materials that contain active functional groups for conjugation (or attachment) to other molecules, substrates or the like. Certain embodiments describe methods and compositions that provide for specific control of the incorporation and subsequent conjugation of such functional sites. Linkers can be incorporated at one or both ends of a conjugated polymer chain or internally controlled by ratio of monomers used in the polymerizations. Such linkers can be the same or different to allow for more than one distinct entity to be attached to the conjugated polymer structure. Further embodiments describe conjugated polymer compositions that not only provide for active conjugation sites but also are solubilized through the use of non-ionic side chains (no formal charges). Such embodiments exhibit exceptional water solubility and provide minimal interactions with biological molecules and other common biological assay components. The embodiments disclosed herein further relate generally to assays and complexes including conjugated polymers useful for the identification of target biomolecules or biomolecules associated with target molecules through enhanced signal afforded by their unique properties. In certain general embodiments the conjugated polymer serves directly as the optical reporter bound to a biomolecule, substrate or other assay component. The conjugated polymers act as extended light harvesting structures that when excited can absorb more energy than conventional organic dyes. The polymer then re-emits the light which can be detected or measured. The signals generated from such conjugated polymer complexes can be significantly greater than those obtained from other fluorescent reporters. In other embodiments one aspect includes energy transfer from conjugated polymers to dyes bound to the polymer or to a sensor which can be a biomolecule including a bioconjugate (e.g., an antibody, a streptavidin or nucleic acid sequence). In such embodiments it is common to observe amplified dye signal (relative to direct dye excitation) as a result of the conjugated polymer excitation and subsequent energy transfer. Further it is possible to use a range of dyes with varying energy to create a basis for a multicolor or multiplex detection format. In certain embodiments the neutral conjugated polymers are bound to antibodies for the identification of specific cell markers and cell types in flow cytometry and cell sorting assays. In other embodiments the conjugated polymers are further bound to a secondary dye reporter. In further embodiments the polymer and polymer-dye structures are bound to monoclonal antibodies. In other embodiments the neutral conjugated polymers are bound to antibodies for use in various sandwich immunoassays. In one embodiment, an approach modifying a format as followed in relation to nucleic acid sensor assays as described in Gaylord, Heeger, and Bazan, J. Am. Chem. Soc., 2003 can be followed. Specifically, signal amplification of conjugated polymers can be based on binding events to indicate a hybridization event. Any established conjugated polymers can be chosen as the donor, and one or more dye, preferably a dye with a history of efficient energy transfer, for example, fluorescein and Cy3, can be chosen as the acceptors. It is envisioned that the dye can be directly conjugated to a sensor molecule. As shown schematically in FIG. 1, the sensor can be a biomolecule (e.g., an antibody) in a solution or on a substrate, to which conjugated polymers can be added. In the embodiment shown in FIG. 1, a dye can be covalently linked (bioconjugated) to an antibody (Y-shaped structure), which possesses a net negative charge. Addition of conjugated polymers (shown as wavy lines) can result in interaction or binding between the conjugated polymer and the antibody, bringing the conjugated polymers and dye into close proximity. Interaction or binding can be achieved by any known method including, but not limited to, avidin/biotin labeling. Distance requirements for fluorescence resonance energy transfer (FRET) can thus be met, and excitation of the polymer with light (shown as hν) results in amplified dye emission. It is envisioned that the conjugated polymers can be excited at a wavelength where the dye does not have significant absorbance. In one embodiment the dye emission can be at a longer wavelength than the conjugated polymer emission. In use it is envisioned that an assay method can include the steps of providing a sample that is suspected of containing a target biomolecule, providing a sensor conjugated to a signaling chromophore and capable of interacting with the target biomolecule, providing a conjugated polymer that interacts with the sensor and upon excitation is capable of transferring energy to the sensor signaling chromophore and contacting the sample with the sensor and the conjugated polymer in a solution under conditions in which the sensor can bind to the target biomolecule if present. Next, the method can include applying a light source to the sample that can excite the conjugated polymer, and detecting whether light is emitted from the signaling chromophore. As disclosed herein, interaction or binding between conjugated polymers and dye-labeled antibodies can be a viable approach for increasing detection sensitivities, for example of a biomolecule target. In a further embodiment, covalently attaching the conjugated polymers to a dye, biomolecule (e.g., an antibody complex) or both offers several advantages including reduced background and/or improved energy transfer. In the case of direct linkage to a biomolecule, biorecognition events, rather than non-specific polymer interaction or binding events (such as those described above in FIG. 1), should govern conjugated polymer presence. In this manner, nonspecific binding of conjugated polymers to biomolecules can be eliminated, reducing any background emission resulting from the conjugated polymer itself. The abovementioned biomolecules include but are not limited to proteins, peptides, affinity ligands, antibodies, antibody fragments, sugars, lipids, enzymes and nucleic acids (as hybridization probes and/or aptamers). In general, in another aspect the invention includes the bioconjugation of polymers to affinity ligands (affinity ligands describing a biomolecule that has an affinity for another biomolecule). FIG. 2 illustrates a class of materials in which a conjugated polymer (shown as a wavy line) is linked to a dye, biomolecule, or biomolecule/dye complex (labeled X). Linking to the conjugated polymer can be via a first functionality linker A on the conjugated polymer that serves as a bioconjugation site capable of covalently linking with a second functionality linker A′ linked to a biomolecule and/or dye (see X). This arrangement can fix the distance between the conjugated polymer and X, thereby ensuring only specific interactions between polymer and X. It is envisioned that a biomolecule component X in this embodiment can be any of the various biomolecules disclosed herein, including but not limited to an antibody, protein, affinity ligand, enzyme or nucleic acid. Linker A can be anywhere on the conjugated polymer including terminal positions of the polymer, internally on a repeating subunit, in between repeating subunits or any combination thereof. Likewise, Linker A′ can be linked anywhere on a biomolecule and/or dye. The linking chemistry for A-A′ can include, but is not limited to, maleimide/thiol; thiol/thiol; pyridyldithiol/thiol; succinimidyl iodoacetate/thiol; N-succinimidylester (NHS ester), sulfodicholorphenol ester (SDP ester), or pentafluorophenyl-ester (PFP ester)/amine; bissuccinimidylester/amine; imidoesters/amines; hydrazine or amine/aldehyde, dialdehyde or benzaldehyde; isocyanate/hydroxyl or amine; carbohydrate-periodate/hydrazine or amine; diazirine/aryl azide chemistry; pyridyldithiol/aryl azide chemistry; alkyne/azide; carboxy-carbodiimide/amine; amine/Sulfo-SMCC (Sulfosuccinimidyl 4-[N-maleimidomethyl]cyclohexane-1-carboxylate)/thiol; and amine/BMPH (N—[B-Maleimidopropionic acid]hydrazide⋅TFA)/thiol. It is envisioned that the X in this context can be, but is not limited to, a dye, fluorescence protein, nanomaterial (e.g., Quantum Dot), chemiluminescence-generating molecule, a conjugate between dye and chemiluminescence-generating molecule, a conjugate between fluorescence protein and chemiluminescence-generating molecule, a conjugate between nanomaterial (e.g., Quantum Dot) and chemiluminescence-generating molecule, streptavidin, avidin, enzyme, substrate for an enzyme, substrate analog for an enzyme, receptor, ligand for a receptor, ligand analog for a receptor, DNA, RNA, modified nucleic acid, DNA aptamer, RNA aptamer, modified nucleic aptamer, peptide aptamer, antibody, antigen, phage, bacterium or conjugate of any two of the items described above. In another aspect, the invention includes the use of conjugated polymers as direct labels. FIG. 3 shows examples of labeled conjugated polymers. In one embodiment, FIG. 3A, a polymer (shown as encircled hexagons) is shown conjugated to an antibody which can be, for example, a 1° or 2° antibody. The conjugate of the polymer and the antibody can be used as a direct reporter, for example, in an assay. In additional embodiments, the signal from the polymer is not modulated by other assay components rather it is dependent on its presence in the assay at the time of detection as a function of specific biomolecule recognition. Excitation of the polymer with light (not shown) can result in polymer emission, indicating the presence of the antibody (1° or 2°) in the assay or assay solution. FIGS. 3B and 3C further exemplify the use of conjugated polymers as biomolecule labels capable of detecting specific targets and target associated biomolecules. FIG. 3B depicts a polymer avidin (streptavidin, neutraAvidin, etc.) conjugate capable of binding to biotin modified molecules, biomolecules or substrates. FIG. 3C depicts a nucleic acid (DNA, RNA, PNA, etc.) conjugate capable of hybridizing to complementary nucleic acid sequences. Linkage or conjugation of fluorescent conjugated polymer to a molecule capable of recognizing a target biomolecule or target associated molecule (such as those exemplified in FIG. 3) provides a direct means of detection. In additional embodiments, the signals generated from excitation of the conjugated polymer are not modulated by other assay components except those which are directly conjugated to the polymer. In such embodiments the polymer complex is acting directly as a fluorescent label. In another embodiment shown in FIG. 3D, the conjugated polymer is labeled with a dye, for example, a chromophore. In this case, the conjugated polymer can act as a donor and the dye can act as an acceptor in an energy transfer process. Here, the conjugated polymer can act as a light harvester, and excitation of the conjugated polymer is followed by the channeling of the excitations to the dye via an energy transfer process including, but not limited to, FRET. This results in amplified dye emission (as compared to direct excitation of the dye). The fluorescence of the donor conjugated polymer, in one embodiment, can be quenched (e.g., >90% quenching). This is exemplified in Example 38 and shown in FIG. 21, by way of example only. In some instances, the conjugated polymer in FIG. 3D (and similar drawings disclosed herein) can have multiple dye attachments which can be positioned internally or at the terminus of the polymer structure (single dye shown for illustrative purposes only). In the case of direct linkage to a dye (FIG. 3D) or biomolecule/dye complex (as exemplified in FIG. 4), donor-acceptor distances can be fixed, rather than dependent on the strength of interaction or binding, and energy transfer efficiency can be significantly increased. This has significant consequences in the context of improving dye signaling (or quenching) and reducing background fluorescence associated with donor-acceptor cross-talk. Cross-talk in this case refers to the overlap between conjugated polymer (donor) and dye (acceptor) emission peaks. Conjugated polymers which bind non-specifically at distances too great for energy transfer can contribute to the background fluorescence (or crosstalk). Shorter (fixed) distances between the donor and acceptor can not only facilitate direct dye amplification, but also can greatly quench the donor emission, as depicted in FIG. 21 by way of example only. This results in less donor emission at the acceptor emission wavelengths, which subsequently reduces or even eliminates the need for cross-talk correction. In further embodiments the localization of the conjugated polymer and a signaling chromophore are brought together by recognition event, for example by the binding of two affinity pairs or by co-recognition of the same target molecule or target associated molecule (FIG. 5). Such embodiments could be performed in solution based formats or in such configurations where one or more of elements is bound to another biomolecule (cell, tissue, protein, nucleic acid, etc.) or a substrate (bead, well plate, surface, tube, etc.). In general, another aspect the invention includes a method of assaying for a target biomolecule or target associated biomolecule. As shown in FIG. 5A, in one embodiment a conjugated polymer (shown as a wavy line) can be linked to a first bioconjugate (shown as a Y-shaped object), for example, a 2° antibody that is specific for second a dye-labeled bioconjugate, for example, a 1° antibody. Here, the recognition event between the 1° and 2° antibody will result in the reduction of distance between the donor conjugated polymer and acceptor dye. In a similar embodiment depicted in FIG. 5B, polymer and dye labeled antibodies recognize a common target. After either of these recognition events, excitation of the donor conjugated polymer with light (shown as hν) will result in energy transfer, e.g., FRET, to the acceptor dye (shown as curved arrow), and amplified dye emission (in comparison with direct excitation of the dye) will be observed. In use it is envisioned that an assay method could include providing a sample that is suspected of containing a target biomolecule by the steps of providing a first bioconjugate, for example, a 1° antibody conjugated to a signaling chromophore and capable of interacting with the target biomolecule. This is followed by providing a second bioconjugate, for example, a 2° antibody or 1° antibody, conjugated to a polymer, wherein the second bioconjugate can bind to the first bioconjugate or target and wherein upon such binding excitation of the conjugated polymer is capable of transferring energy to the signaling chromophore. Next, the method includes contacting the sample with the first bioconjugate in a solution under conditions in which the first bioconjugate can bind to the target biomolecule if present and contacting the solution with the second bioconjugate. The method then includes applying a light source to the target biomolecule or tagged target biomolecule, wherein the light source can excite the conjugated polymer and subsequently detecting whether light is emitted from the signaling chromophore. In another aspect, the invention includes a method of assaying a sample using a conjugated polymer and a sensor biomolecule complex. As shown in FIGS. 5C and D, a polymer (shown as a wavy line) can be conjugated to a first bioconjugate, for example, streptavidin (SA) which has a strong affinity for biotin. In FIG. 5C, a sensor biomolecule (e.g., an antibody which can be a 1° or 2° antibody), is conjugated to both a dye and a second bioconjugate (e.g., a biotin moiety). Similar embodiments are depicted in FIG. 5D where the second bioconjugate (e.g., a biotin moiety) and the signaling chromophore are both conjugated to a nucleic acid. After a biorecognition event between the first and second bioconjugates (e.g. between SA and biotin), the conjugated polymer and dye will be brought into close proximity, and excitation of the donor conjugated polymer will result in energy transfer to the acceptor dye. Dye emission will indicate the presence of the first bioconjugate (e.g., the antibody or nucleic acid). In comparison with direct excitation of the dye, amplification of the dye signal intensity will be observed when excited indirectly through an energy transfer process, e.g., FRET. A method of using the embodiment shown in FIGS. 5C and D can include the steps of providing a sample that is suspected of containing a target biomolecule, providing a conjugated polymer comprising a covalently linked first bioconjugate (e.g., SA), providing a sensor biomolecule complex comprising a sensor biomolecule capable of interacting with the target molecule, a signaling chromophore, and covalently linked second bioconjugate capable of binding with the first bioconjugate, wherein upon such binding excitation of the conjugated polymer is capable of transferring energy to the signaling chromophore. The method can further include the steps of contacting the sample with the sensor biomolecule complex in a solution under conditions in which the sensor biomolecule can bind to the target biomolecule if present, contacting the solution with the conjugated polymer, applying a light source to the sample that can excite the conjugated polymer, and detecting whether light is emitted from the signaling chromophore. Further the conjugated polymer can contain additional linking site suitable for conjugation or attachement to more than one species. FIG. 6 exemplifies the addition of a second linking site within the polymer. Such linkers A and B can be the same or different to allow for orthogonal conjugation of different species. The linkers can be anywhere on the polymer including terminal and internal positions. The linking chemistry for A-A′ and B-B′ (and optionally C-C′, D-D′, etc.) can include, but is not limited to, maleimide/thiol; thiol/thiol; pyridyldithiol/thiol; succinimidyl iodoacetate/thiol; N-succinimidylester (NHS ester), sulfodicholorphenol ester (SDP ester), or pentafluorophenyl-ester (PFP ester)/amine; bissuccinimidylester/amine; imidoesters/amines; hydrazine or amine/aldehyde, dialdehyde or benzaldehyde; isocyanate/hydroxyl or amine; carbohydrate-periodate/hydrazine or amine; diazirine/aryl azide chemistry; pyridyldithiol/aryl azide chemistry; alkyne/azide; carboxy-carbodiimide/amine; amine/Sulfo-SMCC (Sulfosuccinimidyl 4[N-maleimidomethyl]cyclohexane-1-carboxylate)/thiol; and amine/BMPH (N—[B-Maleimidopropionic acid]hydrazide⋅TFA)/thiol. A tri-functional linker such as the commercially available Sulfo-SBED Sulfosuccinimidyl[2-6-(biotinamido)-2-(p-azidobenzamido)-hexanoamido]-ethyl-1,3′-dithiopropionate can serve well in the three way linkage among X, Y, and conjugated polymer. In the embodiment illustrated in FIG. 6, X or Y can be, but are not limited to, a dye, fluorescence protein, nanomaterial (e.g., Quantum Dot), chemiluminescence-generating molecule, a conjugate between dye and chemluminescence-generating molecule, a conjugate between fluorescence protein and chemiluminescence-generating molecule, a conjugate between nanomaterial (e.g., Quantum Dot) and chemiluminescence-generating molecule, streptavidin, avidin, enzyme, substrate for an enzyme, substrate analog for an enzyme, receptor, ligand for a receptor, ligand analog for a receptor, DNA, RNA, modified nucleic acid, DNA aptamer, RNA aptamer, modified nucleic aptamer, peptide aptamer, antibody, antigen, phage, bacterium or conjugate of any two of the items described above. In general, in another aspect the invention provides a conjugated polymer complex including a polymer, a sensor biomolecule and a signaling chromophore for identifying a target biomolecule. As shown in FIG. 6, in one embodiment a polymer (wavy line) can be bioconjugated to a dye X via linker functionalities A-A′ and a biomolecule Y via linker functionalities B-B′. As depicted in FIG. 7, in one embodiment a polymer can be bioconjugated to both a dye and a biomolecule, for example a biorecognition molecule. Useful biomolecules can include but are not limited to antibodies (FIG. 7A), avidin derivatives (FIG. 7B) affinity ligands, nucleic acids (FIG. 7C), proteins, nanoparticles or substrates for enzymes. The benefits of covalently linking a dye in proximity to a polymer have been described above. By affixing both an acceptor dye and a biorecognition molecule to a polymer, the benefits are two fold, by both fixing donor-acceptor distances, such that an acceptor is guaranteed to be within the vicinity of a donor conjugated polymer (and vice versa), and also increasing the specificity of polymer binding to indicate a biorecognition event. These covalent complexes can be made via the monomer, polymer and linking chemistries described herein. In use, the embodiments shown in FIG. 6 can be a conjugated polymer complex for identifying a target biomolecule wherein the complex includes a conjugated polymer, a signaling chromophore covalently linked to the conjugated polymer and a sensor biomolecule covalently linked to the conjugated polymer. The signaling chromophore of the complex is capable of receiving energy from the conjugated polymer upon excitation of the conjugated polymer and the sensor biomolecule is capable of interacting with the target biomolecule. It is envisioned that the biomolecules can include but are not limited to an antibody, protein, affinity ligand, peptide, or nucleic acid. In one embodiment shown in FIG. 7A, a polymer is conjugated to both a bioconjugate, for example, an antibody (1° or 2°) and a dye. Covalent linkage between the donor conjugated polymer and acceptor dye ensures close proximity. Excitation of the donor conjugated polymer results in energy transfer, e.g., FRET, to the acceptor dye. Where the bioconjugate is an antibody, if the antibody binds to its target (e.g., antigen), this will be indicated by dye emission upon donor polymer excitation. In an alternative embodiment, as shown in FIG. 7B, a polymer can be conjugated to both a SA and a dye. Again, covalent linkage between the donor conjugated polymer and acceptor dye ensure close proximity, and excitation of the donor conjugated polymer results in energy transfer to the acceptor dye. The SA complex can be used to label or detect a biotin-labeled biomolecule such as a biotinylated antibody or nucleic acid. Polymer excitation followed by energy transfer to the dye label will result in greatly enhanced detection signals (i.e., greater sensitivity). The example exemplified in FIG. 7A is a conjugated polymer labeled with a dye acceptor and further conjugated to an antibody. This Tandem configuration can be used in similar fashion as those described for the structure in FIG. 3A but are useful in generating a secondary signal for detection, often in multiplex formats. The conjugated polymer complexes in FIG. 7 can have multiple dye attachments which can be positioned internally or at the terminus of the polymer structure (single dye shown for illustrative purposes only). In other embodiments as shown in FIGS. 3A and 7A, a sensor biomolecule for example a 1° antibody (Y shape) is conjugated covalently linked to the conjugated polymer (encircled hexagons) or conjugated polymer-dye tandem complex (hexagons with pendant encircled star). Upon conjugated polymer excitation, emission from the conjugated polymer (FIG. 3A) or dye (FIG. 7A) will indicate presence of the biocomplex and by extension with appropriate assay design that of the target recognized by the sensor molecule allowing use as a reporter, for example in an assay. FIGS. 29A and 29B represent comparable examples with covalent linkage of the conjugated polymer to a 2° antibody. As an alternative embodiment, the conjugated polymer may be associated indirectly with the sensor biomolecule or target associated biomolecule. FIGS. 8C and 8D illustrate a sequence specific oligonucleotide probe (wavy line) covalently conjugated to a biotin moiety (drop shape). Here the conjugated polymer (encircled hexagons) or conjugated polymer-dye tandem complex (hexagons with pendant encircled star) is covalently bound or conjugated to a biotin recognizing protein (for example, avidin, streptavidin or similar with high specific affinity for the ligand biotin). FIGS. 8A and 8B illustrate comparable examples with a biotinylated antibody interacting with a covalent conjugate of the conjugated polymer (FIG. 8A) and conjugated polymer-dye tandem complex (FIG. 8B) to the biotin recognizing protein. Indirect association of the target associated biomolecule with the conjugated polymer is not limited to biotin mediated interactions. FIGS. 8E and F represent sequence specific oligonucleotides (wavy line) which have been covalently labeled with a digoxygenin moiety (7 pointed star). In turn the digoxygenin moiety has been recognized by a primary antibody covalently linked to the conjugated polymer (FIG. 8E) and the conjugated polymer-dye tandem complex (FIG. 8F). Although not shown pictorially, further embodiments employing indirect detection of digoxygenin using biotinylated antibodies and biotin recognizing proteins covalently linked to conjugated polymers (or conjugated polymer-dye tandem complexes) or unlabelled primary antibodies recognizing digoxygenin and appropriate secondary antibodies covalently linked to the conjugated polymer (or conjugated polymer-dye tandem complexes) are intended. A number of further embodiments are also predicated on energy transfer (for example but not limited to FRET) between the conjugated polymer and an acceptor dye. Given the potential for multiplexing analysis, it is envisioned that the conjugated polymer can be linked to a number of dyes or signaling chromophores, including, but not limited to, fluorescein, 6-FAM, rhodamine, Texas Red, California Red, iFluor594, tetramethylrhodamine, a carboxyrhodamine, carboxyrhodamine 6G, carboxyrhodol, carboxyrhodamine 110, Cascade Blue, Cascade Yellow, coumarin, Cy2®, Cy3®, Cy3.5®, Cy5®, Cy5.5®, Cy7®, Cy-Chrome, DyLight 350, DyLight 405, DyLight 488, DyLight 549, DyLight 594, DyLight 633, DyLight 649, DyLight 680, DyLight 750, DyLight 800, phycoerythrin, PerCP (peridinin chlorophyll-a Protein), PerCP-Cy5.5, JOE (6-carboxy-4′,5′-dichloro-2′,7′-dime1hoxyfluorescein), NED, ROX (5-(and-6)-carboxy-X-rhodamine), HEX, Lucifer Yellow, Marina Blue, Oregon Green 488, Oregon Green 500, Oregon Green 514, Alexa Fluor® 350, Alexa Fluor® 430, Alexa Fluor® 488, Alexa Fluor® 532, Alexa Fluor® 546, Alexa Fluor® 568, Alexa Fluor® 594, Alexa Fluor® 633, Alexa Fluor® 647, Alexa Fluor® 660, Alexa Fluor® 680, 7-amino-4-methylcoumarin-3-acetic acid, BODIPY® FL, BODIPY® FL-Br2, BODIPY® 530/550, BODIPY® 558/568, BODIPY® 564/570, BODIPY® 576/589, BODIPY® 581/591, BODIPY® 630/650, BODIPY® 650/665, BODPY® R6G, BODIPY® TMR, BODIPY® TR, conjugates thereof, and combinations thereof. These embodiments include modifications of the above examples where the acceptor dye serves as the assay reporter (as exemplified in FIGS. 3D, 4D, 7, 8B, 8D, 8E, 29B, wherein the encircled ten pointed star represents the dye). In certain embodiments the conjugated polymer conjugates provided in FIGS. 2-10, 29 and 30 are intended for but not limited to use in flow cytometry, cell sorting, molecular diagnostics, fluorescence in situ hybridization (FISH), immunohistochemistry (IHC), polymerase chain reaction, microscopy (fluorescent, confocal, 2 photon, etc.), blotting (e.g. northern, southern, western), cytomic bead arrays (Luminex formats, etc.), fluorescent immune assay (FIA or ELISA), nucleic acid sequencing and microarrays. Embodiments are also envisaged where conjugated polymers are used to enhance the detection and quantification of nucleic acids using sequence specific fluorescent probes combined with nucleic acid amplification techniques such as but not limited to polymerase chain reaction, transcription mediated amplification, rolling circle amplification, recombinase polymerase amplification, helicase dependent amplification and Linear-After-The-Exponential polymerase chain reaction. FIG. 32 represents modifications of the HybProbe detection technique. In FIG. 32A, the dye conventionally used as an energy transfer donor is replaced by the conjugated polymer (hexagon chain) which is covalently linked to the donor probe (wavey helical structure represented as right hand helical duplex due to association with nucleic acid target depicted a longer helical wavy line). Upon sequence specific hybridization the donor and acceptor (represented similarly to donor probe but on left hand side of nucleic acid target) probes are spatially juxtaposed on the target nucleic acid strand of interest in sufficiently close proximity to allow energy transfer to take place between the fluors. Excitation energy is transduced through the conjugated polymer and emitted as a readable signal by the dye (encircled ten pointed star) to allow nucleic acid quantification, detection and/or characterization. Presence of increased template allows increased numbers of probe co-hybridisation events and thus correlates to increased specific signal from the acceptor dye. In combination with the melt curve technique commonly employed in HybProbe experiments it is envisaged that sequence specific information corresponding to sequence variations will be collectable in appropriately designed experiments. FIG. 32B represents a “signal off” modification of the HybProbe approach where the conjugated polymer is quenched by an acceptor probe consisting of a small molecule fluorescence quencher (for example but not limited to Black Hole Quenchers™ Iowa Black® or Dabsyl). In another embodiment, conjugated polymer and conjugated polymer-dye tandem complexes similar to those described in FIGS. 4C and 4D are used in the detection, quantification and/or characterization of nucleic acid targets. Nucleic acid probe sequences labeled with a quencher molecule (black circle, for example but not limited to Black Hole Quenchers™, Iowa Black® or Dabsyl) are also conjugated to a conjugated polymer (FIGS. 4C and 31A) and a conjugated polymer-dye tandem complex (FIGS. 4D and 31B). In FIGS. 4C and D the recognition of the target sequence leads to a hybridization and separation of the quencher from the conjugated polymer or conjugated polymer-dye tandem complex and upon polymer excitation produces an increase in fluorescent signal. In FIGS. 31A and 31B the nucleic acid probe conjugate will hybridize to a complementary target sequence and by treatment with specific enzymes the probe sequence is cleaved or hydrolyzed freeing the conjugated polymer or conjugated polymer-dye tandem complex from the quencher and upon polymer excitation produces an increase in fluorescent signal. The most common example of the methods described in FIG. 31 is the use of DNA polymerase enzymes which contain nuclease activity (e.g. TaqMan PCR assays). FIG. 9 shows examples of conjugated polymer (hexagons) conjugated to secondary antibodies (FIG. 9A) and primary antibodies (FIG. 9B) (antibodies shown as Y-shaped structures). In an assay, an unlabeled 1° antibody can bind to an antigen, for example, a target protein (shown as a black triangle). Addition of the 2° antibody, which is conjugated to a polymer, can bind specifically to the 1° antibody. After washing to remove unbound 2° antibody and upon application of light of suitable excitation wavelength, observance of polymer emission is indicative of specific binding (FIG. 9A). In other assay embodiments, a polymer-labeled 1° antibody can directly bind a target protein, shown as a black triangle, and after washing to remove unbound 1° antibody and upon application of light of suitable excitation wavelength, observance of polymer emission is indicative of specific binding (FIG. 9B). Optionally, whether conjugated to the 1° or 2° antibody, the polymer may be further conjugated to a dye. In such a case, optical excitation of the conjugated polymer can result in energy transfer to the dye, and amplified dye emission, in comparison to direct dye excitation results. Observance of dye emission is indicative of specific binding. FIG. 10 shows an example of a sandwich-type complex of one embodiment of the invention. In the assay shown in FIG. 10A the conjugated polymer complex is composed of a polymer (shown as hexagons) that is bioconjugated a biomolecule, for example, streptavidin (X shape). After an unlabeled 1° antibody binds the target (e.g. protein), shown as a black triangle, a biotin-labeled 2° antibody binds specifically to the 1° antibody. In a separate step, addition of the conjugated polymer complex will result in specific binding between the biotin and streptavidin. Excitation of the conjugated polymer will result in polymer emission, indicating the presence of the target protein. Additionally in another embodiment, a biotin-labeled 1° antibody may be used to probe the target protein directly (FIG. 10B). After this binding event takes place, addition of a streptavidin-polymer complex will result in specific binding between the biotin and streptavidin, and excitation of the conjugated polymer will result in polymer emission, indicating the presence of the target protein. Optionally, the polymer may be further conjugated to a dye. In such a case, optical excitation of the polymer will result in amplified dye emission, as compared to direct excitation of the dye. Signals arising from dye emission will indicate the presence of the target protein. FIG. 30 depicts example embodiments around the use of conjugated polymers in Fluorescent Immuno Assay (FIA). In FIG. 30 panels A-C analyte antigen is immobilised on a surface which can include but is not limited to a microtitre plate well, bead particle, glass slide, plastic slide, lateral flow strip, laminar flow device, microfluidic device, virus, phage, tissue or cell surface. Analyte molecules are then detected by use of labelled detection conjugates or sensor biomolecules. In FIG. 30A, a conjugated polymer covalently linked to a detection antibody is utilized for detection. In FIG. 30B, a biotin binding protein (for example but not limited to avidin, streptavidin or other high affinity biotin specific derivatives) covalently bound to the conjugated polymer and interacting with a biotinylated detection antibody is utilized for detection. In FIG. 30C, a secondary antibody covalently linked to the conjugated polymer and interacting with a detection antibody is utilized for detection. In FIG. 5B, a homogenous, solution based example is also embodied where two separate antibodies each bind to the antigen of interest. One antibody is covalently linked to the conjugated polymer, the other to a dye. When bound to the antigen, the respective fluorophores are brought into sufficient spatial proximity for energy transfer to occur. In assays predicated on the designs in FIG. 30 and FIG. 5B, the sample is interrogated with light matched to the excitation of the conjugated polymer and signal reported at the emission wavelength of the dye. In the examples embodied in FIG. 30 A-C the use of a polymer-dye tandem complex is further disclosed. In such cases, optical excitation of the polymer will result in amplified dye emission, as compared to direct excitation of the dye. Signals arising from dye emission will indicate the presence of the target. In a further aspect, the invention provides for the multiplexing of donor energy transfer to multiple acceptors. By using a conjugated polymer as a donor in an energy transfer system, benefits also include the ability to multiplex. A single donor can transfer energy to several dyes; thus with a single excitation source, the intensity of multiple dyes can be monitored. This is useful for applications including but not limited to cell imaging (i.e. immunohistochemistry), flow cytometry and cell sorting, where the different types of cells can be monitored by protein-antibody recognition events. In one embodiment, two dye-labeled antibodies can be incubated with a biological material, for example, a cultured cell line, tissue section or blood sample. Antibodies are able to recognize cells with a target protein expressed on its surface and specifically bind only to those proteins. By labeling the two antibodies with different dyes, it is possible to monitor for the expression of two different proteins or different cell types simultaneously. Typically, this would require two scans, excitations or images, once each with the correct excitation wavelength. As a final step prior to analysis, these two images or data sets would have to be overlaid or combined. By using antibodies conjugated with both a dye and a conjugated polymer, one excitation wavelength can be used for the conjugated polymer to excite both dyes, and a single image or scan will include data sets from each of the two antibodies. This can be done with any number of antibody combinations provided there is sufficient ability to resolve the resulting signals. It is envisioned that the invention described herein can be used to increase the sensitivity of any of a number of commercially available tests including but not limited to the OraQuick Rapid HIV-1/2 Antibody Test, manufactured by OraSure Technologies, Inc. (Bethlehem, Pa.), which is a FDA-approved HIV diagnostic test for oral fluid samples. This test can provide screening results with over 99 percent accuracy in as little as 20 minutes. Conjugated Polymers Light harvesting conjugated polymer systems can efficiently transfer energy to nearby luminescent species. Mechanisms for energy transfer include, for example, resonant energy transfer (Forster (or fluorescence) resonance energy transfer, FRET), quantum charge exchange (Dexter energy transfer) and the like. Typically, however, these energy transfer mechanisms are relatively short range, and close proximity of the light harvesting conjugated polymer system to the signaling chromophore is required for efficient energy transfer. Amplification of the emission can occur when the number of individual chromophores in the light harvesting conjugated polymer system is large; emission from a fluorophore can be more intense when the incident light (the “pump light”) is at a wavelength which is absorbed by the light harvesting conjugated polymer system and transferred to the fluorophore than when the fluorophore is directly excited by the pump light. The conjugated polymers used in the present invention can be charge neutral, cationic or anionic. In some embodiments, the conjugated polymers are polycationic conjugated polymers. In other embodiments, the conjugated polymers are polyanionic conjugated polymers. In further embodiments, the conjugated polymers can include cationic, anionic, and/or neutral groups in various repeating subunits. In yet other embodiments, the conjugated polymers are neutral conjugated polymers. In some instances, conjugated polymers contain groups such as ethylene glycol oligomers, ethylene glycol polymers, co-ammonium alkoxy salts, and/or w-sulfonate alkoxy salts that impart solubility in aqueous solutions. In some instances the neutral conjugated polymers with non-ionic side chains are soluble in greater than 10 mg/mL in water or phosphate buffered saline solutions and in certain cases the solubility is greater than 50 mg/mL. In some embodiments the conjugated polymers contain either a terminal linking site (e.g., capping unit), internal linking site or both. In some embodiments, a conjugated polymer is one that comprises “low bandgap repeat units” of a type and in an amount that contribute an absorption to the polymer in the range of about 450 nm to about 1000 nm. The low bandgap repeat units may or may not exhibit such an absorption prior to polymerization, but does introduce that absorption when incorporated into the conjugated polymer. Such absorption characteristics allow the polymer to be excited at wavelengths that produce less background fluorescence in a variety of settings, including in analyzing biological samples and imaging and/or detecting molecules. Shifting the absorbance of the conjugated polymer to a lower energy and longer wavelength thus allows for more sensitive and robust methods. Additionally, many commercially available instruments incorporate imaging components that operate at such wavelengths at least in part to avoid such issues. For example, thermal cyclers that perform real-time detection during amplification reactions and microarray readers are available which operate in this region. Providing polymers that absorb in this region allows for the adaptation of detection methods to such formats, and also allows entirely new methods to be performed. Incorporation of repeat units that decrease the band gap can produce conjugated polymers with such characteristics. Exemplary optionally substituted species which result in polymers that absorb light at such wavelengths include 2,1,3-benzothiadiazole, benzoxidazole, benzoselenadiazole, benzotellurodiazole, naphthoselenadiazole, 4,7-di(thien-2-yl)-2,1,3-benzothiadiazole, squaraine dyes, quinoxalines, perylene, perylene diimides, diketopyrrolopyrrole, thienopyrazine low bandgap commercial dyes, olefins, and cyano-substituted olefins and isomers thereof. Further details relating to the composition, structure, properties and synthesis of suitable conjugated polymers can be found in U.S. patent application Ser. No. 11/329,495, filed Jan. 10, 2006, now published as US 2006-0183140 A1, which is incorporated herein by reference in the entirety. In one aspect, provided herein are conjugated polymers of Formula (I): wherein: each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x′(OCH2CH2)y′OCH3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C2-C18(hetero)aryl group; each optional linker L1 and L2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another substrate, molecule or biomolecule selected from amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G1 and G2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, optionally substituted fluorine and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, and thiols within G1, G2, L1 or L2 that allows, for functional conjugation to another molecule, substrate or biomolecule; each dashed bond, , is independently a single bond, triple bond or optionally substituted vinylene (—CR5═CR5—) wherein each R5 is independently hydrogen, cyano, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. Non-ionic side groups capable of imparting solubility in water as used herein refer to side groups which are not charged and allow the resulting polymer to be soluble in water or aqueous solutions with no visible particulates. In some embodiments, each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL, in excess of 15 mg/mL, in excess of 20 mg/mL, in excess of 25 mg/mL, in excess of 30 mg/mL, in excess of 35 mg/mL, in excess of 40 mg/mL, in excess of 45 mg/mL, in excess of 50 mg/mL, in excess of 60 mg/mL, in excess of 70 mg/mL, in excess of 80 mg/mL, in excess of 90 mg/mL or in excess of 100 mg/mL. In some embodiments, conjugated polymers described herein comprises a minimum number average molecular weight of greater than 5,000 g/mol, greater than 10,000 g/mol, greater than 15,000 g/mol, greater than 20,000 g/mol, greater than 25,000 g/mol, greater than 30,000 g/mol, greater than 40,000 g/mol, greater than 50,000 g/mol, greater than 60,000 g/mol, greater than 70,000 g/mol, greater than 80,000 g/mol, greater than 90,000 g/mol, or greater than 100,000 g/mol. In some embodiments, each R is independently (CH2)x(OCH2CH2)yOCH3 where each x is independently an integer from 0-20, each y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)zOCH3 where each z is independently an integer from 0 to 50. In some instances, each R is (CH2)3(OCH2CH2)11OCH3. In other embodiments, each R is independently a benzyl substituted with at least one (OCH2CH2)zOCH3 group where each z is independently an integer from 0 to 50. In some instances, each R is a benzyl substituted with at least one (OCH2CH2)10OCH3 group. In other instances, each R is a benzyl substituted with at least two (OCH2CH2)10OCH3 groups. In further instances, each R is a benzyl substituted with at least three (OCH2CH2)10OCH3 groups. In further embodiments, each R is independently where k and l are independent integers from 0 to 25; *=site for covalent attachment. In yet further embodiments, each R is independently is a dendrimer of PAMAM, PEA, PEHAM, PPI, tri-branched benzoate, or glycerol with a generation of 1 to 4 and optionally terminal substitutions, said optionally terminal substitutions are ( - - - )CH2CH2O)jCH3 or ( - - - )(OCH2CH2)jCH3 and j is an integer from 0 to 25 and the dotted lines ( - - - ) are each independently selected from any one or a combination of, C1-C12 alkyl, C1-C12 alkoxy, C2-C12 alkene, amido, amino, aryl, (CH2)r(OCH2CH2)s(CH2)r where each r is independently an integer from 0-20, s is independently an integer from 0 to 50, carbamate, carboxylate, C3-C12 cycloalkyl, imido, phenoxy, or C4-C18(hetero)aryl groups. In alternative embodiments, each R is independently, Where k and l are independent integers from 0 to 25 and the dotted lines () are each independently selected from any one or a combination of, C1-C12 alkyl, C1-C12 alkoxy, C2-C12 alkene, amido, amino, aryl, (CH2)r(OCH2CH2)s(CH2)r where each r is independently an integer from 0-20, s is independently an integer from 0 to 50, carbamate, carboxylate, C3-C12 cycloalkyl, imido, phenoxy, or C4-C18(hetero)aryl groups; *=site for covalent attachment. In alternative embodiments, each R is independently, Where k and l are independent integers from 0 to 25 and the dotted lines ( - - - ) are each independently selected from any one or a combination of, C1-C12 alkyl, C1-C12 alkoxy, C2-C12 alkene, amido, amino, aryl, (CH2)r(OCH2CH2)s(CH2)r where each r is independently an integer from 0-20, s is independently an integer from 0 to 50, carbamate, carboxylate, C3-C12 cycloalkyl, imido, phenoxy, or C4-C18(hetero)aryl groups; *=site for covalent attachment. In some embodiments, conjugated polymers described herein contain no optional linkers, L1 and/or L2. In other embodiments, conjugated polymers contain at least about 0.01 mol %, at least about 0.02 mol %, at least about 0.05 mol %, at least about 0.1 mol %, at least about 0.2 mol %, at least about 0.5 mol %, at least about 1 mol %, at least about 2 mol %, at least about 5 mol %, at least about 10 mol %, at least about 20 mol %, or about 25 mol % of optional linkers, L1 and/or L2. In some embodiments, conjugated polymers contain up to 50 mol % total of optional linkers, L1 and L2, and may contain about 40 mol % or less, about 30 mol % or less, about 25 mol % or less, about 20 mol % or less, about 15 mol % or less, about 10 mol % or less, or about 5 mol % or less. Linkers can be evenly or randomly distributed along the polymer main chain. In some embodiments, optional linkers L1 or L2 have the structure: *=site for covalent attachment to unsaturated backbone wherein R3 is independently hydrogen, halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and q is an integer from 0 to 4. In some embodiments, optional linkers L1 or L2 have the structure represented by: *=site for covalent attachment to unsaturated backbone wherein A is a site for conjugation, chain extension or crosslinking and is —[O—CH2—CH2]t—W, or (C1-C12)alkoxy-X; W is —OH or —COOH; X is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]uNH2; t is an integer from 1 to 20; and u is an integer from 1 to 8. In other embodiments, optional linkers L1 or L2 are selected from the group consisting of a-h having the structure: *=site for covalent attachment to unsaturated backbone wherein R′ is independently H, halogen, C1-C12 alkyl, (C1-C12 alkyl)NH2, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C2-C18(hetero)aryl, C2-C18(hetero)arylamino, —[CH2—CH2]r′—Z1, or (C1-C12)alkoxy-X1; and wherein Z1 is —OH or —COOH; X1 is —NH2, —NHCOOH, —NHCOOC(CH3)3, —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH2—CH2—O]s′(CH2)s′NH2; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH2)3(OCH2CH2)x″OCH3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)y″OCH3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein R15 is selected from the group consisting of l-t having the structure: and k is 2, 4, 8, 12 or 24; *=site for covalent attachment to backbone. In certain embodiments, optional linkers L1 or L2 are In some embodiments, G1 and G2 are optionally substituted aryl wherein the optional substituent is selected from halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, boronic acid, boronate radical, boronic esters and optionally substituted fluorene. In other embodiments, G1 and G2 are the same. In further embodiments, G1 and G2 are different. G1 and G2 can be activated units that allow further conjugation, crosslinking, or polymer chain extension, or they may be nonactivated termination units. In some embodiments, G1 and G2 are independently selected from structures represented by: *=site for covalent attachment to backbone wherein R11 is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In other embodiments, G1 and G2 are independently selected from the group consisting of 1-18 having the structure: *=site for covalent attachment to backbone wherein R15 is selected from the group consisting of l-t having the structure: and k is 2, 4, 8, 12 or 24. In further embodiments, G1 and G2 is In some embodiments, optional linkers, L1 and/or L2, G1, and/or G2 can be further conjugated to an organic dye, a biomolecule or a substrate. Covalent linkage can be introduced by any known method and can include, but is not limited to, chemistry involving maleimide/thiol; thiol/thiol; pyridyldithiol/thiol; succinimidyl iodoacetate/thiol; N-succinimidylester (NHS ester), sulfodicholorphenol ester (SDP ester), or pentafluorophenyl-ester (PFP ester)/amine; bissuccinimidylester/amine; imidoesters/amines; hydrazine or amine/aldehyde, dialdehyde or benzaldehyde; isocyanate/hydroxyl or amine; carbohydrate-periodate/hydrazine or amine; diazirine/aryl azide chemistry; pyridyldithiol/aryl azide chemistry; alkyne/azide; carboxy-carbodiimide/amine; amine/Sulfo-SMCC (Sulfosuccinimidyl 4-[N-maleimidomethyl]cyclohexane-1-carboxylate)/thiol; and amine/BMPH (N-[β-Maleimidopropionic acid]hydrazide⋅TFA)/thiol. In some embodiments, MU is selected from the group consisting of a′-k′ having the structure: =site for covalent attachment to unsaturated backbone wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL. Non-ionic side groups include those previously described for polymers of Formula (I). As used herein, in some embodiments, a pendant chain is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups which connects a polymer with a functional group for conjugation to another substrate, molecule, or biomolecule. In some embodiments, conjugated polymers of Formula (I) have the structure of Formula (Ia): wherein R, L1, L2, G1, G2, MU, a, b, c, d and n are described previously for formula (I). In a further aspect, conjugated polymers of Formula I have the structure of Formula (Ib): wherein at least one of G1 or G2 comprises a functional conjugation cite. In a further aspect, conjugated polymers of Formula I have the structure of Formula (Ic): wherein L1 comprises a functional conjugation cite. In a further aspect, conjugated polymers of Formula I have the structure of Formula (Id): wherein at least one of G1 or G2 comprises a functional conjugation cite. In a further aspect, conjugated polymers of Formula I have the structure of Formula (II): wherein L1, G1, G2, a, c, n and dashed bonds are described previously for formula (I). In some embodiments, conjugated polymers of Formula (II) have the structure of Formula (IIa): wherein L1, G1, G2, a, c, and n are described previously for formula (I). In a further aspect, conjugated polymers of Formula I have the structure of Formula (III): wherein L1, G1, G2, a, c, n and dashed bonds are described previously for formula (I). In some embodiments, conjugated polymers of Formula (III) have the structure of Formula (IIIa): wherein L1, G1, G2, a, c, and n are described previously for formula (I). In a further aspect, conjugated polymers of Formula I have the structure of Formula (IV): wherein each R5 is independently hydrogen, cyano, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and L1, G1, G2, a, c, n and dashed bonds are described previously for formula (I). In a further aspect, conjugated polymers of Formula I have the structure of Formula (V): wherein each R5 is independently hydrogen, cyano, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group, wherein each C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl or a C2-C18(hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; and L1, G1, G2, a, c, n and dashed bonds are described previously for formula (I). Also provided herein are polymers having the structure of the following formula: wherein: G1 and G2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, optionally substituted aryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters and optionally substituted fluorene; L is a bond or an aryl or heteroaryl group that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkene, C2-C12 alkyne, C3-C12 cycloalkyl, C1-C12 haloalkyl, C1-C12 alkoxy, C2-C18(hetero)aryloxy, C2-C18(hetero)arylamino, (CH2)x(OCH2CH2)pOCH3 where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, or a C2-C18(hetero)aryl group; L1, L1′, L2 and L2′ are each independently a covalent bond, a C1-C12 alkylene, a C3-C12 cycloalkylene, a C2-C12 alkenylene, a C2-C12 alkynylene, a (C6-C18)aryl(C1-C12)alkylene, a (C6-C18)aryl(C2-C12)alkenylene, a (C6-C18)aryl(C1-C12)alkynylene, a C6-C18 arylene group, —Y1—[O—Y2]p—, —O—Y1—[O—Y2]p— wherein each C1-C12 alkylene, C3-C12 cycloalkylene, (C6-C18)aryl(C1-C12)alkylene, or C6-C18 arylene group is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, C1-C12 haloalkyl, —Y1—[O—Y2]p— or —O—Y1—[O—Y2]p—; q is 0 or an integer from 1 to 8; p is 0 or an integer from 1 to 24; Y1 and Y2 are each independently a covalent bond, or a C1-12 alkylene group, a C3-C12 cycloalkylene, a C2-C18(hetero)arylene, a (C6-C18)aryl(C1-C12)alkylene, wherein each C1-12 alkylene group, a C3-C12 cycloalkylene, a C2-C18(hetero)arylene, a (C6-C18)aryl(C1-C12)alkylene is optionally substituted with one or more halogen, hydroxyl, C1-C12 alkyl, C2-C12 alkenyl, C2-C12 alkynyl group, C1-C12 alkoxy, or C1-C12 haloalkyl; E1 and E1′ are each independently, hydrogen, C1-C6 alkyl, —OH, —COOH, —SH, —SR, —SHR+, SR2+, —SO3−, —PO4−, Br, —NH2, —NHR, —NR2, —NH3+, —NH2R+, —NHR2+or —NR3, wherein and each R is independently a C1-C6 alkyl and —SHR+, SR2+, —SO3−, —PO4−, —NH3+, —NH2R+, —NHR2+or —NR3+ each optionally has an associated counterion; and n is an integer from 1 to about 1,000. Also provided herein are polymers having the structure of the following formula: wherein each R is independently O(CHx), or (CH2)3(OCH2CH2)pOCH3 where each x is independently an integer from 0-20, each p is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C1-C12 alkoxy, or (OCH2CH2)mOCH3 where each m is independently an integer from 0 to 50; G1 is selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, optionally substituted aryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters and optionally substituted fluorene; and n is an integer from 1 to about 10,000. Additional embodiments of conjugated polymers are described in the following Examples. Preparation of Conjugated Polymers The synthesis of conjugated polymers described herein may be accomplished using means described in the chemical literature, using the methods described herein, or a combination thereof. Conjugated polymers described herein may be synthesized using standard synthetic techniques known to those of skill in the art or using methods known in the art in combination with methods described herein. In additions, solvents, temperatures and other reaction conditions presented herein may vary according to the practice and knowledge of those of skill in the art. The starting material used for the synthesis of the conjugated polymers of Formula (1) and polymers having the structures described in the prior section as described herein can be obtained from commercial sources, such as Aldrich Chemical Co. (Milwaukee, Wis.), Sigma Chemical Co. (St. Louis, Mo.), or the starting materials can be synthesized. The polymers described herein, and other related polymers having different substituents can be synthesized using techniques and materials known to those of skill in the art, such as described, for example, in March, ADVANCED ORGANIC CHEMISTRY 4th Ed., (Wiley 1992); Carey and Sundberg, ADVANCED ORGANIC CHEMISTRY 4th Ed., Vols. A and B (Plenum 2000, 2001), and Green and Wuts, PROTECTIVE GROUPS IN ORGANIC SYNTHESIS 3rd Ed., (Wiley 1999) (all of which are incorporated by reference in their entirety). General methods for the preparation of polymers as disclosed herein may be derived from known reactions in the field, and the reactions may be modified by the use of appropriate reagents and conditions, as would be recognized by the skilled person, for the introduction of the various moieties found in the formulae as provided herein. As a guide the following synthetic methods may be utilized. Generally, polymerization of fluorene polymeric structures may be accomplished using polymerization techniques known to those of skill in the art or using methods known in the art in combination with methods described herein. For example, polymerization can be achieved via Suzuki coupling with a commercially available fluorene-dihalide monomer, e.g., 2,7-dibromofluorene, and its diboronic acid or ester derivative: Structures A-1 and A-2 are catalyzed by a metal catalyst to form exemplary polymer A-3 with termination points, labeled Y. Each Y is independently —H, —Br, —B(OH)2, or boronic ester, e.g., 4,4,5,5-tetramethyl-1,3,2-dioxaborolanyl. Synthesis of diboronic ester derivatives from a fluorene-dihalide monomer can also be accomplished via Suzuki coupling with bis(pinacolato)diboron: Substituents such as ethylene glycol oligomers or ethylene glycol polymers may be attached to monomers prior to polymerization or to the polymer itself after polymerization. An exemplary scheme of synthesizing substituted fluorene monomers with mPEGylated groups is as follows: 2,7-dibromofluorene (B-1) and 3-bromopropanol in the presence of a strong base such as sodium hydroxide, potassium hydroxide, or the like and a phase transfer catalyst, e.g. tetrabutylammonium bromide, is heated and reacted to completion to form 2,7-dibromo-9,9-di(3′-hydroxypropanyl)fluorene (B-2). —OH groups of B-2 are tosylated with tosyl chloride in the presence of pyridine and allowed to react to completion to form 2,7-dibromo-9,9-di(3′-methylbenzenesulfonatopropanyl)fluorene (B-3). B-3 is then reacted with a mPEG(x) alcohol in the presence of potassium tert-butoxide to form B-4 with attached mPEG chains. mPEG alcohols can have 1-50 mPEG chains. Typical sizes include but are not limited to mPEG5, mPEG8, mPEG11, mPEG24. In an alternative scheme, mPEG alcohols can be tosylated first via tosyl chloride and then reacted to B-2 to form B-4. Substituted monomers, such as exemplary structure B-4, can be further derivatized to diboronic esters in the schemes disclosed herein and subsequently be used for polymerization such as via Suzuki coupling. Polymeric fluorenes may also be obtained through the use of other reaction schemes involving organometallic catalysis. For example, the Yamamoto reaction uses a nickel(0)-based catalyst for the homo-coupling of aryl halide monomers like exemplary structure B-4. Additionally, conjugated polymers can be synthesized using Stille, Heck, and Sonogashira coupling reactions. See, e.g., Yamamoto et al., Macromolecules 25: 1214-1223, 1992; Kreyenschmidt et al., Macromolecules 28: 4577-4582, 1995; and Pei et al., J. Am. Chem. Soc. 118: 7416-7417, 1996 regarding Yamamoto reaction schemes. See, also, Leclerc, Polym. Sci. Part A: Polym. Chem. 39: 2867-2873, 2001 for Stille reaction schemes; Mikroyannidis et al., J. Polym. Sci. Part A: Polym. Chem. 45: 4661-4670, 2007 for Heck reaction schemes; and Sonogashira et al., Tetrahedron Lett. 16: 4467-4470, 1975 and Lee et al., Org. Lett. 3: 2005-2007, 2001 for Sonogashira reaction schemes. Linkers and capping units can be conjugated to a fluorene polymer backbone via similar mechanisms as described previously. For example, bromo- and boronic esters of capping units can be used to append one or both ends of a polymer. Utilizing both bromo- and boronic esters of capping units will append both ends of polymer. Utilizing only one form, either a bromo- or boronic ester of a capping unit, will append only those ends terminated with its respective complement and for symmetric A-A+B-B polymerizations can be used to statistically modify only one end of a polymer. For asymmetric polymers this approach is used to chemically ensure the polymers are only modified at a single chain terminus. FIG. 11 depicts appending an exemplary fluorene polymer with Y ends with one or more phenyl groups with bromobenzene, phenyl boronic acid or both using Suzuki coupling. Capping units can also be appended asymmetrically by first reacting a bromo-capping unit with a polymer with Y ends and subsequently reacting the polymer with a boronic ester capping unit. Exemplary bromo- and boronic ester capping units include but are not limited to the following structures: Further capping units can be found in structures 1-31 described herein or in the following Examples and methods for their attachment. The incorporation of optional linkers into conjugated polymer backbones further described in U.S. application Ser. No. 11/868,870, filed Oct. 8, 2007 and published as U.S. Application No. 2008/0293164, which application is herein incorporated by reference in its entirety. A desired optional linker incorporation can be achieved by varying the molar ratio of optional linker to bi-functional monomer. For example, an optional linker can be incorporated by substituting a percentage of one of the bi-functional monomers with a similar bi-functional optional linker which comprises the conjugation site of interest. The number and type of linking site included in the polymer is controlled by the feed ratio of the monomers to optional linker in the polymerization reaction. By varying the feed ratio, conjugated polymers can contain at least about 0.01 mol % of linker, L, and may contain at least about 0.02 mol %, at least about 0.05 mol %, at least about 0.1 mol %, at least about 0.2 mol %, at least about 0.5 mol %, at least about 1 mol %, at least about 2 mol %, at least about 5 mol %, at least about 10 mol %, at least about 20 mol %, or at least about 30 mol %. The conjugated polymers may contain up to 100 mol % of linker, L, and may contain about 99 mol % or less, about 90 mol % or less, about 80 mol % or less, about 70 mol % or less, about 60 mol % or less, about 50 mol % or less, or about 40 mol % or less. Linkers can be evenly or randomly distributed along the polymer main chain. In further embodiments, an optional linker can further allow covalent attachment of the resulting polymer to biomolecules, secondary reporters or other assay components. In alternative embodiments, the methods described herein to incorporate optional linkers may be used in combination with methods of introducing capping units with linking sites to produce polymers with both internal and terminal linking sites for conjugation. A non-limiting application of a polymer with both optional linkers and terminal capping units with linking sites for conjugation are polymer-dye-biomolecule tandem conjugates where the polymer is used as an energy transfer donor, such as in FRET, to a secondary dye acceptor thus shifting the emission wavelength to that of the corresponding dye. The person skilled in the art may further appreciate various syntheses and polymerization methods and embodiments of the present disclosure upon review of the following illustrative and non-limiting Examples. Antigen-Antibody Interactions The interactions between antigens and antibodies are the same as for other noncovalent protein-protein interactions. In general, four types of binding interactions exist between antigens and antibodies: (i) hydrogen bonds, (ii) dispersion forces, (iii) electrostatic forces between Lewis acids and Lewis bases, and (iv) hydrophobic interactions. Certain physical forces contribute to antigen-antibody binding, for example, the fit or complimentary of epitope shapes with different antibody binding sites. Moreover, other materials and antigens may cross-react with an antibody, thereby competing for available free antibody. Measurement of the affinity constant and specificity of binding between antigen and antibody is a pivotal element in determining the efficacy of an immunoassay, not only for assessing the best antigen and antibody preparations to use but also for maintaining quality control once the basic immunoassay design is in place. Antibodies Antibody molecules belong to a family of plasma proteins called immunoglobulins, whose basic building block, the immunoglobulin fold or domain, is used in various forms in many molecules of the immune system and other biological recognition systems. A typical immunoglobulin has four polypeptide chains, containing an antigen binding region known as a variable region and a non-varying region known as the constant region. Native antibodies and immunoglobulins are usually heterotetrameric glycoproteins of about 150,000 Daltons, composed of two identical light (L) chains and two identical heavy (H) chains. Each light chain is linked to a heavy chain by one covalent disulfide bond, while the number of disulfide linkages varies between the heavy chains of different immunoglobulin isotypes. Each heavy and light chain also has regularly spaced intrachain disulfide bridges. Each heavy chain has at one end a variable domain (VH) followed by a number of constant domains. Each light chain has a variable domain at one end (VL) and a constant domain at its other end. The constant domain of the light chain is aligned with the first constant domain of the heavy chain, and the light chain variable domain is aligned with the variable domain of the heavy chain. Depending on the amino acid sequences of the constant domain of their heavy chains, immunoglobulins can be assigned to different classes. There are at least five (5) major classes of immunoglobulins: IgA, IgD, IgE, IgG and IgM, and several of these may be further divided into subclasses (isotypes), e.g. IgG-1, IgG-2, IgG-3 and IgG-4; IgA-1 and IgA-2. The subunit structures and three-dimensional configurations of different classes of immunoglobulins are well known. Further details regarding antibody structure, function, use and preparation are discussed in U.S. Pat. No. 6,998,241, issued Feb. 14, 2006, the entire contents of which are incorporated herein by reference. Sandwich Assays Antibody or multiple antibody sandwich assays are well known to those skilled in the art including a disclosed in U.S. Pat. No. 4,486,530, issued Dec. 4, 1984, and references noted therein. The structures described in FIGS. 6, 7, 8, 9, 10 and 14 can be used directly as described or in various sandwich configurations including those described in Example 37. A sandwich configuration or a sandwich assay refers to the use of successive recognition events to build up layers of various biomolecules and reporting elements to signal the presence of a particular biomolecule, for example a target biomolecule or a target-associated biomolecule. A standard example of this would be the successive use of antibodies. In these assays, a primary antibody binds the target, the secondary antibody binds the primary, a third antibody can bind the secondary and so on. With each successive layer additional reporting groups can be added. Another strategy is using a repetitive addition of alternating layers of two (or more) mutually-recognizable components, or more than two components in a chain-recognition relationship, which comprise one or both of the components in a form of multimeric structure. In such a setup, one or more of the functional group(s) in each of the multimeric structure can be labeled with reporting group(s) and the unoccupied functional group(s) can serve as the recognition site for the other component(s), and this system will subsequently provide a platform for signal amplification. A typical example of this approach is the use of streptavidin-reporter conjugate and biotinylated anti-streptavidin antibody. In such assays, a biotinylated sensor molecule (nucleic acid or antibody) can be used to bind a target biomolecule, which is subsequently recognized by a detection system containing a streptavidin-reporter conjugate and biotinylated anti-streptavidin antibody. The sandwich structure in this case can be built up by successive rounds of biotinylated antibodies and labeled streptavidin complexes interaction to achieve the signal amplification. With an additional conjugation of a conjugated polymer to either the biotinylated antibody or the streptavidin-reporter complex, it is possible to further increase the signal output. In essence, the integration of a conjugated polymer in this type of signal amplification system can further amplify signals to a higher level. The bioconjugated polymer complexes described in FIGS. 6, 7, 8, 9, 10, 14, 15, 16 and 17 can be used to create optically enhanced sandwich assays by directly integrating a light harvesting conjugated polymer into commonly utilized recognition elements. The benefits of the conjugated polymer conjugated structures can also be applied directly to the primary target recognition elements without the need for successive recognition elements. For example, a primary antibody can be directly conjugated to polymer-dye complex such as shown in FIG. 14. Such a complex can be used to directly probe the presence of a target biomolecule. Polynucleotides Amplified target polynucleotides may be subjected to post amplification treatments. For example, in some cases, it may be desirable to fragment the target polynucleotide prior to hybridization in order to provide segments which are more readily accessible. Fragmentation of the nucleic acids can be carried out by any method producing fragments of a size useful in the assay being performed; suitable physical, chemical and enzymatic methods are known in the art. An amplification reaction can be performed under conditions which allow the sensor polynucleotide to hybridize to the amplification product during at least part of an amplification cycle. When the assay is performed in this manner, real-time detection of this hybridization event can take place by monitoring for light emission during amplification. Real time PCR product analysis (and related real time reverse-transcription PCR) provides a well-known technique for real time PCR monitoring that has been used in a variety of contexts, which can be adapted for use with the methods described herein (see, Laurendeau et al. (1999) “TaqMan PCR-based gene dosage assay for predictive testing in individuals from a cancer family with INK4 locus haploinsufficiency” Clin Chem 45(7):982-6; Laurendeau et al. (1999) “Quantitation of MYC gene expression in sporadic breast tumors with a real-time reverse transcription-PCR assay” Clin Chem 59(12):2759-65; and Kreuzer et al. (1999) “LightCycler technology for the quantitation of bcr/abl fusion transcripts” Cancer Research 59(13):3171-4, all of which are incorporated by reference). Samples In principle, a sample can be any material suspected of containing a target biomolecule (e.g., antibody, protein, affinity ligand, peptide, nucleic acid and the like) capable of causing excitation of a conjugated polymer complex. In some embodiments, the sample can be any source of biological material which comprises biomolecules that can be obtained from a living organism directly or indirectly, including cells, tissue or fluid, and the deposits left by that organism, including viruses, mycoplasma, and fossils. The sample may comprise a target biomolecule prepared through synthetic means, in whole or in part. Typically, the sample is obtained as or dispersed in a predominantly aqueous medium. Nonlimiting examples of the sample include blood, urine, semen, milk, sputum, mucus, a buccal swab, a vaginal swab, a rectal swab, an aspirate, a needle biopsy, a section of tissue obtained for example by surgery or autopsy, plasma, serum, spinal fluid, lymph fluid, the external secretions of the skin, respiratory, intestinal, and genitourinary tracts, tears, saliva, tumors, organs, samples of in vitro cell culture constituents (including but not limited to conditioned medium resulting from the growth of cells in cell culture medium, putatively virally infected cells, recombinant cells, and cell components), and a recombinant library comprising polynucleotide sequences. The sample can be a positive control sample which is known to contain the target biomolecule or a surrogate therefore. A negative control sample can also be used which, although not expected to contain the target biomolecule, is suspected of containing it (via contamination of one or more of the reagents) or another component capable of producing a false positive, and is tested in order to confirm the lack of contamination by the target biomolecule of the reagents used in a given assay, as well as to determine whether a given set of assay conditions produces false positives (a positive signal even in the absence of target biomolecule in the sample). The sample can be diluted, dissolved, suspended, extracted or otherwise treated to solubilize and/or purify any target polynucleotide present or to render it accessible to reagents which are used in an amplification scheme or to detection reagents. Where the sample contains cells, the cells can be lysed or permeabilized to release the polynucleotides within the cells. One step permeabilization buffers can be used to lyse cells which allow further steps to be performed directly after lysis, for example a polymerase chain reaction. Organic Dyes Organic dyes include signaling chromophores and fluorophores. In some embodiments, a signaling chromophore or fluorophore may be employed, for example to receive energy transferred from an excited state of an optically active unit, or to exchange energy with a labeled probe, or in multiple energy transfer schemes. Fluorophores useful in the inventions described herein include any substance which can absorb energy of an appropriate wavelength and emit or transfer energy. For multiplexed assays, a plurality of different fluorophores can be used with detectably different emission spectra. Typical fluorophores include fluorescent dyes, semiconductor nanocrystals, lanthanide chelates, and fluorescent proteins. Exemplary fluorescent dyes include fluorescein, 6-FAM, rhodamine, Texas Red, tetramethylrhodamine, a carboxyrhodamine, carboxyrhodamine 6G, carboxyrhodol, carboxyrhodamine 110, Cascade Blue, Cascade Yellow, coumarin, Cy2 ®, Cy3 ®, Cy3.5®, Cy5®, Cy5.5®, Cy-Chrome, DyLight 350, DyLight 405, DyLight 488, DyLight 549, DyLight 594, DyLight 633, DyLight 649, DyLight 680, DyLight 750, DyLight 800, phycoerythrin, PerCP (peridinin chlorophyll-a Protein), PerCP-Cy5.5, JOE (6-carboxy-4′,5′-dichloro-2′,7′-dimelhoxyfluorescein), NED, ROX (5-(and-6)-carboxy-X-rhodamine), HEX, Lucifer Yellow, Marina Blue, Oregon Green 488, Oregon Green 500, Oregon Green 514, Alexa Fluor® 350, Alexa Fluor® 430, Alexa Fluor® 488, Alexa Fluor® 532, Alexa Fluor® 546, Alexa Fluor® 568, Alexa Fluor® 594, Alexa Fluor® 633, Alexa Fluor® 647, Alexa Fluor® 660, Alexa Fluor® 680, 7-amino-4-methylcoumarin-3-acetic acid, BODIPY® FL, BODIPY® FL-Br2, BODIPY® 530/550, BODIPY® 558/568, BODIPY® 564/570, BODIPY® 576/589, BODIPY® 581/591, BODIPY® 630/650, BODIPY® 650/665, BODIPY® R6G, BODIPY® TMR, BODIPY® TR, conjugates thereof, and combinations thereof. Exemplary lanthanide chelates include europium chelates, terbium chelates and samarium chelates. A wide variety of fluorescent semiconductor nanocrystals (“SCNCs”) are known in the art; methods of producing and utilizing semiconductor nanocrystals are described in: PCT Publ. No. WO 99/26299 published May 27, 1999, inventors Bawendi et al.; U.S. Pat. No. 5,990,479 issued Nov. 23, 1999 to Weiss et al.; and Bruchez et al., Science 281:2013, 1998. Semiconductor nanocrystals can be obtained with very narrow emission bands with well-defined peak emission wavelengths, allowing for a large number of different SCNCs to be used as signaling chromophores in the same assay, optionally in combination with other non-SCNC types of signaling chromophores. Exemplary polynucleotide-specific dyes include acridine orange, acridine homodimer, actinomycin D, 7-aminoactmomycin D (7-AAD), 9-amino-6-chlor-2-methoxyacridine (ACMA), BOBO™-1 iodide (462/481), BOBO™-3 iodide (570/602), BOPRO™-1 iodide (462/481), BOPRO™-3 iodide (575/599), 4′,6-diamidino-2-phenylindole, dihydrochloride (DAPI), 4′,6-diamidino-2-phenylindole, dihydrochloride (DAPI), 4′,6-diamidino-2-phenylindole, dilactate (DAPI, dilactate), dihydroethidium (hydroethidine), dihydroethidium (hydroethidine), dihydroethidium (hydroethidine), ethidium bromide, ethidium diazide chloride, ethidium homodimer-1 (EthD-1), ethidium homodimer-2 (EthD-2), ethidium monoazide bromide (EMA), hexidium iodide, Hoechst 33258, Hoechst 33342, Hoechst 34580, Hoechst S769121, hydroxystilbamidine, methanesulfonate, JOJO™-1 iodide (529/545), JO-PRO™-1 iodide (530/546), LOLO™-1 iodide (565/579), LO-PRO™-1 iodide (567/580), NeuroTrace™ 435/455, NeuroTrace™ 500/525, NeuroTrace™ 515/535, NeuroTrace™ 530/615, NeuroTrace™ 640/660, OliGreen, PicoGreen® ssDNA, PicoGreen® dsDNA, POPO™-1 iodide (434/456), POPO™-3 iodide (534/570), PO-PRO™-1 iodide (435/455), POPRO™-3 iodide (539/567), propidium iodide, RiboGreen®, SlowFade®, SlowFade® Light, SYBR® Green I, SYBR® Green II, SYBR® Gold, SYBR® 101, SYBR® 102, SYBR® 103, SYBR® DX, TO-PRO®-1, TO-PRO®-3, TO-PRO®-5, TOT™-1, TOTO®-3, YO-PRO®-1 (oxazole yellow), YO-PRO®-3, YOYO®-1, YOYO®-3, TO, SYTOX® Blue, SYTOX® Green, SYTOX® Orange, SYTO® 9, SYTO® BC, SYTO® 40, SYTO® 41, SYTO® 42, SYTO® 43, SYTO® 44, SYTO® 45, SYTO® Blue, SYTO® 11, SYTO® 12, SYTO® 13, SYTO® 14, SYTO® 15, SYTO® 16, SYTO® 20, SYTO® 21, SYTO® 22, SYTO® 23, SYTO® 24, SYTO® 25, SYTO® Green, SYTO® 80, SYTO® 81, SYTO® 82, SYTO® 83, SYTO® 84, SYTO® 85, SYTO® Orange, SYTO® 17, SYTO® 59, SYTO® 60, SYTO® 61, SYTO® 62, SYTO® 63, SYTO® 64, SYTO® Red, netropsin, distamycin, acridine orange, 3,4-benzopyrene, thiazole orange, TOMEHE, daunomycin, acridine, pentyl-TOTAB, and butyl-TOTIN. Asymmetric cyanine dyes may be used as the polynucleotide-specific dye. Other dyes of interest include those described by Geierstanger, B. H. and Wemmer, D. E., Annu. Rev. Vioshys. Biomol. Struct. 1995, 24, 463-493, by Larson, C. J. and Verdine, G. L., Bioorganic Chemistry: Nucleic Acids, Hecht, S. M., Ed., Oxford University Press: New York, 1996; pp 324-346, and by Glumoff, T. and Goldman, A. Nucleic Acids in Chemistry and Biology, 2nd ed., Blackburn, G. M. and Gait, M. J., Eds., Oxford University Press: Oxford, 1996, pp 375-441. The polynucleotide-specific dye may be an intercalating dye, and may be specific for double-stranded polynucleotides. The term “fluorescent protein” includes types of protein known to absorb and emit light. One of the more commonly used classes of such materials are phycobiliproteins. Examples include but are not limited to phycoerythrin (PE and R-PE), allophycocyanin (APC) and PerCP. Other classes include green fluorescent protein and related versions. The term “green fluorescent protein” refers to both native Aequorea green fluorescent protein and mutated versions that have been identified as exhibiting altered fluorescence characteristics, including altered excitation and emission maxima, as well as excitation and emission spectra of different shapes (Delagrave, S. et al. (1995) Bio/Technology 13:151-154; Heim, R. et al. (1994) Proc. Natl. Acad. Sci. USA 91:12501-12504; Heim, R. et al. (1995) Nature 373:663-664). Delgrave et al. isolated mutants of cloned Aequorea victoria GFP that had red-shifted excitation spectra. Bio/Technology 13:151-154 (1995). Heim, R. et al. reported a mutant (Tyr66 to His) having a blue fluorescence (Proc. Natl. Acad. Sci. (1994) USA 91:12501-12504). Substrates In some embodiments, an assay component can be located upon a substrate. The substrate can comprise a wide range of material, either biological, nonbiological, organic, inorganic, or a combination of any of these. For example, the substrate may be a polymerized Langmuir Blodgett film, functionalized glass, Si, Ge, GaAs, GaP, SiO2, SiN4, modified silicon, or any one of a wide variety of gels or polymers such as (poly)tetrafluoroethylene, (poly)vinylidenedifluoride, polystyrene, cross-linked polystyrene, polyacrylic, polylactic acid, polyglycolic acid, poly(lactide coglycolide), polyanhydrides, poly(methyl methacrylate), poly(ethylene-co-vinyl acetate), polysiloxanes, polymeric silica, latexes, dextran polymers, epoxies, polycarbonates, or combinations thereof. Conducting polymers and photoconductive materials can be used. Substrates can be planar crystalline substrates such as silica based substrates (e.g. glass, quartz, or the like), or crystalline substrates used in, e.g., the semiconductor and microprocessor industries, such as silicon, gallium arsenide, indium doped GaN and the like, and includes semiconductor nanocrystals. The substrate can take the form of a photodiode, an optoelectronic sensor such as an optoelectronic semiconductor chip or optoelectronic thin-film semiconductor, or a biochip. The location(s) of probe(s) on the substrate can be addressable; this can be done in highly dense formats, and the location(s) can be microaddressable or nanoaddressable. Silica aerogels can also be used as substrates, and can be prepared by methods known in the art. Aerogel substrates may be used as free standing substrates or as a surface coating for another substrate material. The substrate can take any form and typically is a plate, slide, bead, pellet, disk, particle, microparticle, nanoparticle, strand, precipitate, optionally porous gel, sheets, tube, sphere, container, capillary, pad, slice, film, chip, multiwell plate or dish, optical fiber, etc. The substrate can be any form that is rigid or semi-rigid. The substrate may contain raised or depressed regions on which an assay component is located. The surface of the substrate can be etched using well known techniques to provide for desired surface features, for example trenches, v-grooves, mesa structures, or the like. Surfaces on the substrate can be composed of the same material as the substrate or can be made from a different material, and can be coupled to the substrate by chemical or physical means. Such coupled surfaces may be composed of any of a wide variety of materials, for example, polymers, plastics, resins, polysaccharides, silica or silica-based materials, carbon, metals, inorganic glasses, membranes, or any of the above-listed substrate materials. The surface can be optically transparent and can have surface Si—OH functionalities, such as those found on silica surfaces. The substrate and/or its optional surface can be chosen to provide appropriate characteristics for the synthetic and/or detection methods used. The substrate and/or surface can be transparent to allow the exposure of the substrate by light applied from multiple directions. The substrate and/or surface may be provided with reflective “mirror” structures to increase the recovery of light. The substrate and/or its surface is generally resistant to, or is treated to resist, the conditions to which it is to be exposed in use, and can be optionally treated to remove any resistant material after exposure to such conditions. Polynucleotide or polypeptide probes can be fabricated on or attached to the substrate by any suitable method, for example the methods described in U.S. Pat. No. 5,143,854, PCT Publ. No. WO 92/10092, U.S. patent application Ser. No. 07/624,120, filed Dec. 6, 1990 (now abandoned), Fodor et al., Science, 251: 767-777 (1991), and PCT Publ. No. WO 90/15070). Techniques for the synthesis of these arrays using mechanical synthesis strategies are described in, e.g., PCT Publication No. WO 93/09668 and U.S. Pat. No. 5,384,261. Still further techniques include bead based techniques such as those described in PCT Appl. No. PCT/US93/04145 and pin based methods such as those described in U.S. Pat. No. 5,288,514. Additional flow channel or spotting methods applicable to attachment of sensor polynucleotides or polypeptides to the substrate are described in U.S. patent application Ser. No. 07/980,523, filed Nov. 20, 1992, and U.S. Pat. No. 5,384,261. Reagents are delivered to the substrate by either (1) flowing within a channel defined on predefined regions or (2) “spotting” on predefined regions. A protective coating such as a hydrophilic or hydrophobic coating (depending upon the nature of the solvent) can be used over portions of the substrate to be protected, sometimes in combination with materials that facilitate wetting by the reactant solution in other regions. In this manner, the flowing solutions are further prevented from passing outside of their designated flow paths. Typical dispensers include a micropipette optionally robotically controlled, an ink-jet printer, a series of tubes, a manifold, an array of pipettes, or the like so that various reagents can be delivered to the reaction regions sequentially or simultaneously. The substrate or a region thereof may be encoded so that the identity of the sensor located in the substrate or region being queried may be determined. Any suitable coding scheme can be used, for example optical codes, RFID tags, magnetic codes, physical codes, fluorescent codes, and combinations of codes. Excitation and Detection Any instrument that provides a wavelength that can excite the conjugated polymer complex and is shorter than the emission wavelength(s) to be detected can be used for excitation. Commercially available devices can provide suitable excitation wavelengths as well as suitable detection components. Exemplary excitation sources include a broadband UV light source such as a deuterium lamp with an appropriate filter, the output of a white light source such as a xenon lamp or a deuterium lamp after passing through a monochromator to extract out the desired wavelengths, a continuous wave (cw) gas laser, a solid state diode laser, or any of the pulsed lasers. Emitted light can be detected through any suitable device or technique; many suitable approaches are known in the art. For example, a fluorimeter or spectrophotometer may be used to detect whether the test sample emits light of a wavelength characteristic of the signaling chromophore upon excitation of the conjugated polymer. Compositions of Matter Also provided are compositions of matter of any of the molecules described herein in any of various forms. The conjugated polymers and complexes including conjugated polymers as described herein may be provided in purified and/or isolated form. The conjugated polymers and complexes including conjugated polymers may be provided in either crystalline or amorphous form. The conjugated polymers and complexes including conjugated polymers may be provided in solution, which may be a predominantly aqueous solution, which may comprise one or more of the additional solution components described herein, including without limitation additional solvents, buffers, biomolecules, polynucleotides, fluorophores, etc. In addition, a mixture of CPs in solution is also able to provide improved detection sensitivity as compared to that for a single CP/dye system. The conjugated polymers and complexes including conjugated polymers can be present in solution at a concentration at which a first emission from the first optically active units can be detected in the absence of biomolecule target or a biomolecule associated therewith. The solution may comprise additional components as described herein, including labeled probes such as fluorescently labeled antibodies or polynucleotides, specific for a species or a class of biomolecule target or a biomolecule associated therewith for the conjugated polymers and complexes including conjugated polymers. The conjugated polymers and complexes including conjugated polymers may be provided in the form of a film. The compositions of matter may be claimed by any property described herein, including by proposed structure, by method of synthesis, by absorption and/or emission spectrum, by elemental analysis, by NMR spectra, or by any other property or characteristic. In some embodiments expression of a gene is detected in a sample. In a further embodiment identification of a cell marker or cell type is detected in a sample either in a flow cytometer, cell sorter, microscope, plate reader or fluorescence imager. In a further embodiment the identification of cell type or marker is used in the diagnosis of lymphoma or other circulating cancers. In a further embodiment the identification of cell type or marker is used in the diagnosis and monitoring of HIV infection. In a further embodiment the identification of cell type or marker is used to sort cells for therapeutic application. In a further embodiment, a measured result of detecting a biomolecule target or a biomolecule associated therewith can be used to diagnose a disease state of a patient. In yet another embodiment the detection method of the invention can further include a method of diagnosing a disease state. In a related embodiment, the method of diagnosing a disease can include reviewing or analyzing data relating to the presence of a biomolecule target or a biomolecule associated therewith and providing a conclusion to a patient, a health care provider or a health care manager, the conclusion being based on the review or analysis of data regarding a disease diagnosis. Reviewing or analyzing such data can be facilitated using a computer or other digital device and a network as described herein. It is envisioned that information relating to such data can be transmitted over the network. In practicing the methods of the present invention, many conventional techniques in molecular biology are optionally utilized. These techniques are well known and are explained in, for example, Ausubel et al. (Eds.) Current Protocols in Molecular Biology, Volumes I, II, and III, (1997), Ausubel et al. (Eds.), Short Protocols in Molecular Biology: A Compendium of Methods from Current Protocols in Molecular Biology, 5th Ed., John Wiley & Sons, Inc. (2002), Sambrook et al., Molecular Cloning: A Laboratory Manual, 3rd Ed., Cold Spring Harbor Laboratory Press (2000), Innis et al. (Eds.) PCR Protocols: A Guide to Methods and Applications, Elsevier Science & Technology Books (1990), and Greg T. Hermanson, Bioconjugate Techniques, 2nd Ed., Academic Press, Inc. (2008) all of which are incorporated herein by reference. FIG. 12 is a block diagram showing a representative example logic device through which reviewing or analyzing data relating to the present invention can be achieved. Such data can be in relation to a disease, disorder or condition in a subject. FIG. 12 shows a computer system (or digital device) 800 connected to an apparatus 820 for use with the conjugated polymers or conjugated polymers complexes 824 to, for example, produce a result. The computer system 800 may be understood as a logical apparatus that can read instructions from media 811 and/or network port 805, which can optionally be connected to server 809 having fixed media 812. The system shown in FIG. 12 includes CPU 801, disk drives 803, optional input devices such as keyboard 815 and/or mouse 816 and optional monitor 807. Data communication can be achieved through the indicated communication medium to a server 809 at a local or a remote location. The communication medium can include any means of transmitting and/or receiving data. For example, the communication medium can be a network connection, a wireless connection or an internet connection. It is envisioned that data relating to the present invention can be transmitted over such networks or connections. In one embodiment, a computer-readable medium includes a medium suitable for transmission of a result of an analysis of a biological sample. The medium can include a result regarding a disease condition or state of a subject, wherein such a result is derived using the methods described herein. Kits Kits comprising reagents useful for performing described methods are also provided. In some embodiments, a kit comprises reagents including conjugated polymers or conjugated polymers complexes, bioconjugates, for example, antibodies, nucleic acids, and other components as described herein. The kit may optionally contain one or more of the following: one or more labels that can be incorporated into conjugated polymers or conjugated polymers complexes; and one or more substrates which may or may not contain an array, etc. The components of a kit can be retained by a housing. Instructions for using the kit to perform a described method can be provided with the housing, and can be provided in any fixed medium. The instructions may be located inside the housing or outside the housing, and may be printed on the interior or exterior of any surface forming the housing that renders the instructions legible. A kit may be in multiplex form for detection of one or more different target biomolecules or biomolecules associated therewith. As described herein and shown in FIG. 13, in certain embodiments a kit 903 can include a container or housing 902 for housing various components. As shown in FIG. 13, and described herein, in one embodiment a kit 903 comprising one or more conjugated polymers or conjugated polymers complexes reagents 905, and optionally a substrate 900 is provided. As shown in FIG. 13, and described herein, the kit 903 can optionally include instructions 901. Other embodiments of the kit 903 are envisioned wherein the components include various additional features described herein. EXAMPLES The following examples provide illustrative methods for making and testing the effectiveness of the conjugated polymers described herein. These examples are provided for illustrative purposes only and not to limit the scope of the claims provided herein. All of the methods disclosed and claimed herein can be made and executed without undue experimentation in light of the present disclosure. It will be apparent to those of skill in the art that variations may be applied to the methods and in the steps or in the sequence of steps of the method described herein without departing from the concept, spirit and scope of the claims. All such similar substitutes and modifications apparent to those skilled in the art are deemed to be within the spirit, scope and concept of the appended claims. Example 1: Synthesis of a Polymer of Formula (I) Example 1a: Synthesis of Monomers, 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) and 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (B) for Subsequent Polymerization Step 1: 2,7-dibromo-9,9-di(3′-hydroxypropanyl)fluorene 2,7-dibromofluorene (9.72 g, 30 mmol), tetrabutylammonium bromide (300 mg, 0.93 mmol), and DMSO (100 mL) were added to a 3-neck flask under nitrogen(g), followed by the addition of 50% NaOH (15 mL, 188 mmol) via syringe. The mixture was heated to 80° C., and 3-bromopropanol (6.70 mL, 77 mmol) was added dropwise via addition funnel, and the reaction mixture was stirred at 80° C. for another 2 hours. Upon completion, the mixture was cooled to room temperature and quenched with water (250 mL). The aqueous layer was extracted with ethyl acetate (3 150 mL portions). The organic layers were combined, washed with water, then dried over MgSO4, and filtered. The solvent was removed and the residual was recrystallized in chloroform to yield pale yellow needle crystals (9.20 g, 70%). Step 2: 2,7-dibromo-9,9-di(3′-methylbenzenesulfonatopropanyl)fluorene 2,7-dibromo-9,9-di(3′-hydroxypropanyl)fluorene (500 mg, 1.14 mmol) was dissolved in dichloromethane (5 mL) at 0° C. under nitrogen(g). To the mixture, added p-toluenesulfonyl chloride (650 mg, 3.40 mmol), followed by pyridine (0.39 mL, 4.77 mmol). Allowed reaction to stir at 0° C. and naturally rise to room temperature over night. The reaction was quenched with water (15 mL). Removal of solvent by vacuo resulted solids formation. Filtered off solids to yield white solids (758 mg, 89%). Step 3: 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) mPEG11 alcohol (770 mg, 1.49 mmol) was dissolved in anhydrous THF (2 mL) at 0° C. under nitrogen. To the mixture, was added potassium tert-butoxide (1.63 mmol, 1.63 mL, 1M in THF). After 10 min stirring, 2,7-dibromo-9,9-di(3′-methylbenzenesulfonatopropanyl)fluorene (504 mg, 0.673 mmol) in 10 mL of THF was added via a syringe. The mixture was allowed to room temperature and stirred overnight. The reaction mixture was diluted with THF. The insoluble inorganic salt was removed by filtration. Concentration of the filtrate yielded crude product, which was purified by column chromatography (DCM-MeOH) to yield a colorless oil (605 mg, 62.5%). Step 4: 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (B) 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (1.510 g, 1.501 mmol), bis(pinacolato)diboron (800 mg, 3.15 mmol), potassium acetate (619 mg, 6.31 mmol), Pd(dppf)Cl2 [1,1′-Bis(diphenylphosphino)ferrocene]dichloropalladium(II)] (51.5 mg, 0.063 mmol) and DMSO (30 mL) were mixed under N2. The mixture was heated at 80° C. for 5.5 hour. Upon completion, the DMF was distilled and water (50 mL) was added. The product was extracted with DCM (3×40 mL). The organic layers were combined and concentrated. The crude product was purified by column chromatography (DCM-MeOH) to give colorless oil (1.015 g, 63%). Example 1b: Polymerization of Monomers (A) and (B) 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) (0.084 mmol, 120 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (B) (0.088 mmol, 135 mg), and palladium tetra(triphenylphosphine) (0.0035 mmol, 4 mg) were combined in a round bottom flask equipped with a stirbar. Next, 0.35 mL of 2M potassium carbonate (aq) and 1.9 mL of tetrahydrofuran were added and the flask is fitted with a vacuum adaptor and put on a Schlenk line. The mixture was degassed using 3 freeze-pump-thaw cycles. The degassed mixture was heated to 80° C. under nitrogen with vigorous stirring for 18 hours. The reaction mixture was then cooled and the solvent removed with rotary evaporation. The resulting semisolid was diluted with ca. 50 mL water and filtered through glass fiber filter paper. Ethanol was added to adjust the solvent to 20% ethanol in water. Preparative gel permeation chromatography was performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions was removed with rotary evaporation and 100 mg of poly [2,7{9,9-bis (2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene] was collected as an amber oil. Example 2: Synthesis of Asymmetric Polymers of Formula (I) Via Suzuki Coupling Example 2a: Synthesis of Asymmetric Monomer, 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (C) for Subsequent Polymerization Step 1: 2-dibromo-7-iodofluorene 2-bromofluorene (10.01 g, 40.84 mmol), acetic acid (170 mL), water (8 mL), iodine (4.34 g, 17.20 mmol), potassium iodate (2.18 g, 10.19 mmol) and sulfuric acid (4 mL) were mixed under nitrogen. The resulting mixture was heated at 80° C. for 2h and cooled to room temperature. The formed precipitate which is the desired product was collected after filtration and acetic acid wash (13.68 g, 90%). Step 2: 2-dibromo-9,9-di(3′hydroxypropanyl)-7-iodofluorene 2-dibromo-7-iodofluorene (2.186 g, 5.892 mmol), tetrabutylammonium bromide (60 mg, 0.186 mmol), and DMSO (25 mL) were added to a 3-neck flask under nitrogen(g), followed by the addition of 50% NaOH (4 mL, 50 mmol) via syringe. The mixture was heated to 80° C., and 3-bromopropanol (1.33 mL, 14.7 mmol) was added slowly, and the reaction was stirred at 80° C. for another 1 hour. Upon completion, the mixture was cooled to room temperature and quenched with water. The precipitate as crude product was collected after filtration. The crude product was purified by column chromatography (eluant: hexane-ethylacetate) to give pale yellow solid (2.15 g, 75%). Step 3: 2-bromo-9,9-di(3′-hydroxypropanyl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene 2-dibromo-9,9-di(3′hydroxypropanyl)-7-iodofluorene (2.454 g, 5.037 mmol), bis(pinacolato)diboron (1.407 g, 5.541 mmol), potassium acetate (1.483 g, 15.11 mmol), Pd(dppf)Cl2 (123 mg, 0.15 mmol) and DMSO (25 mL) were mixed under N2. The mixture was heated at 80° C. for 1.5 hour. Upon completion, the mixture was cooled to room temperature and quenched with water (50 mL). The product was extracted with DCM (3×40 mL). The organic layers were combined and concentrated. The crude product was purified by column chromatography (eluant: hexane-ethylacetate) to give pale solid (2.09 g, 85%). Step 4: 2-bromo-9,9-di(3′-methanesulfanotopropanyl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene 2-bromo-9,9-di(3′-hydroxypropanyl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (2.280 g, 4.694 mmol) and p-toluenesulfonyl chloride (2.684 g, 14.08 mmol) were dissolved in dichloromethane at room temperature under N2. Triethylamine (3.95 mL, 28.2 mmol) was added slowly via syringe. The mixture was stirred at room temperature over night. The mixture was then concentrated and purified by column chromatography (Hexane-EtOAc) to yield pale solid (2.66 g, 72%). Step 5: 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorine (C) mPEG11 alcohol (3.331 g, 6.448 mmol) was dissolved in anhydrous THF (20 mL) at 0° C. under nitrogen. To the mixture, was added potassium tert-butoxide (7.74 mmol, 7.74 mL, 1M in THF). After 10 min stirring, 2-bromo-9,9-di(3′-methanesulfanotopropanyl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorine (2.052 g, 2.579 mmol) in 20 mL of anhydrous THF was added via a syringe. The mixture was allowed to room temperature and stirred overnight. After evaporation of THF, brine (50 mL) was added and crude product was extracted with dichloromethane (3×40 mL). The combined organic layers were concentrated and purified by column chromatography (DCM-isopropanol) to give colorless gel-like product (2.164 g, 57%). Example 2b: Synthesis of an Asymmetric Polymer Via Suzuki Coupling Polymerization Asymmetric polymers are synthesized using conditions similar to polymerization conditions as described in Example 1b. Example 3: Synthesis of a Linker or Capping Unit Example 3a: Synthesis of Linker or Capping Unit, Tert-butyl 4-(3,5-dibromophenoxy)butylcarbamate Step 1: 4-(3,5-dibromophenoxy)butan-1-amine 1-(4′-phthalimidobutoxy)3,5-dibromobenzene (1.0 g, 2.20 mmol) was dissolved in ethanol (45 mL) for 5 minutes under nitrogen. Hydrazine monohydrate (610 mg, 12.1 mmol) was added and the reaction was refluxed at 80° C. for 2 hours. To the reaction aqueous 1M HCl (17.7 mL, 17.7 mmol) was added and refluxed at 105° C. for another 2 hours. The aqueous layer was extracted with dichloromethane (2×150 mL). The organic layers were combined, washed with saturated NaHCO3 (3×), water, and brine, then dried over MgSO4, and filtered. Removal of solvent yielded a yellow oil (560 mg, 78%). Step 2: Tert-butyl 4-(3,5-dibromophenoxy)butylcarbamate 4-(3,5-dibromophenoxy)butan-1-amine (397 mg, 1.23 mmol) was dissolved in anhydrous THF (24.6 mL) under nitrogen. Di-tert-butyl dicarbonate (423 mL, 1.84 mmol) was added to the mixture and refluxed reaction at 40° C. for 2 hours. After extraction of the reaction with dichloromethane (2×50 mL), the organic layers were combined, washed with saturated NaHCO3, water, and brine, then dried over MgSO4, and filtered. The solvent is removed and the residue is purified by column chromatography (9:1, hexanes: EtOAc) to give a white solid (306 mg, 59%). Example 3b: Synthesis of Linker or Capping Unit, Tert-butyl-4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butylcarbamate Step 1: 2,7-dibromo-9-methyl-9H-fluorene 2,7-dibromofluorene (30 g, 92.59 mmol) was dissolved in anhydrous THF (300 mL) under nitrogen and cooled to −78° C. To solution at −78° C., added n-butyllithium (40.36 mL, 100.9 mmol) over 5 minutes and allowed reaction stir for another 10 minutes. To reaction, then add methyl iodide (6.29 mL, 100.9 mmol) and allowed reaction to stir at −78° C. for 2.0 hours. The reaction was poured into a mixture of dichloromethane and water. The organic layer was collected, and the water layer was further extracted with dichloromethane. Combined all organic layers and removed solvent via vacuo. The crude material was triturated with hexanes and filtered using Buchner funnel to give white solids (22 g, 70%). 1H NMR (500 MHz, CDCl3): δ=7.62 (s, 2H), 7.56-7.58 (d, 2H), 7.48-7.50 (dd, 2H), 3.90-3.94 (q, 1H), 1.49-1.51 (d, 3H). Step 2: 2-(4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butyl)isoindoline-1,3-dione 2,7-dibromo-9-methyl-9H-fluorene (10.0 g, 29.58 mmol) was dissolved in 50 mL DMSO under nitrogen. To mixture was added KOH (2.01 g, 35.79 mmol), water (1.5 mL), N-(4-bromobutyl)phthalimide (9.93 g, 35.2 mmol), and stirred reaction at room temperature for 2.0 hours, then at 50° C. for 3.0 hours. The reaction was cooled to room temperature and diluted with dichloromethane. The organic layer was washed with brine (2×), and water. Removal of solvent yield a solid, which was purified by column chromatography (7:3, hexanes:EtOAc) to yield white solids (3.08 g, 20%). 1H NMR (500 MHz, CDCl3): δ=7.81-7.83 (m, 2H), 7.68-7.71 (m, 2H), 7.48-7.51 (m, 4H), 7.41-7.44 (dd, 2H), 3.46-3.49 (t, 2H), 2.00-2.04 (p, 2H), 1.47-1.49 (m, 2H), 1.45 (s, 3H), 0.65-0.68 (m, 2H). Step 3: 4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butan-1-amine 2-(4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butyl)isoindoline-1,3-dione (3.08, 5.71 mmol) was dissolved in ethanol (250 mL) under nitrogen. To the mixture was added hydrazine monohydrate (2.77 mL, 57.1 mmol), and the reaction was refluxed at 80° C. for 3.0 hours. The reaction was cooled to room temperature, and added 1M HCl (˜100 mL). The mixture was stirred for 30 minutes or until all solids were dissolved. Dichloromethane was added to the solution and the organic layer was extracted with saturated NaHCO3 three times, and washed with water. The organic layers were collected and removed solvent by vacuo to give an yellow oil (2.33 g, 100%). 1H NMR (500 MHz, CD2Cl2): δ=7.57 (d, 2H), 7.52 (d, 2H), 7.46-7.48 (dd, 2H), 2.39-2.42 (t, 2H), 1.95-1.98 (t, 2H), 1.44 (s, 3H), 1.17-1.23 (m, 2H), 0.59-0.65 (m, 2H). Step 4: tert-butyl-4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butylcarbamate 4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butan-1-amine (2.39 g, 5.84 mmol) was dissolved in anhydrous THF (20 mL) under nitrogen. To solution, was added di-tert-butyl-dicarbonate (2.01 mL, 8.76 mmol), and the reaction was stirred at 40° C. for 3 hours. The reaction was cooled to room temperature and concentrated via vacuo. Crude solids were triturated with hexanes and filtered using buchner funnel to yield the desired white solids (2.34 g, 79%). 1H NMR (500 MHz, CDCl3): δ=7.53 (d, 2H), 7.45-7.47 (d, 4H), 4.30 (s, 1H), 2.88-2.90 (q, 2H), 1.93-1.96 (t, 2H), 1.43 (s, 3H), 1.41 (s, 9H), 1.25-1.28 (m, 2H), 0.59-0.66 (m, 2H). Example 4: Synthesis of a Linker or Capping Unit Example 4a: Synthesis of Tert-butyl 4-(4-bromophenoxy)butylcarbamate Step 1: N(4-(4-bromophenoxy)butyl)phthalimide Combined 4-bromophenol (4.64 g, 26.8 mmol), N-(4-bromobutylphthalimide) (6.30 g, 22.33 mmol), K2CO3 (11.09 g, 80.38 mmol), 18-crown-6 (265 mg, 1.00 mmol), and acetone (100 mL), and refluxed reaction under nitrogen at 70° C. over night. The reaction was cooled to room temperature and removed solvent by vacuum. The crude mixture was diluted with dichloromethane (200 mL) and washed with water (3×), then dried over MgSO4, and filtered. Removal of solvent, followed by trituration with hexanes, and filtered using Buchner funnel to yield a white solid (6.03 g, 71%). Step 2: 4-(4-bromophenoxy)butan-1-amine N(4-(4-bromophenoxy)butyl)phthalimide (6.01 g, 16.1 mmol) is dissolved in ethanol (200 mL) under nitrogen, followed by the addition of hydrazine monohydrate (7. 8 mL, 161 mmol). The reaction was refluxed at 80° C. for 2 hours. Once reaction completed (solids formed at the top layer), cooled reaction to room temperature and neutralized with 1M HCl (50 mL). The mixture is allowed to stir until all solids are completely dissolved and diluted with dichloromethane (150 mL). The solution was extracted with two portions of saturated NaHCO3 (2×). The organic layers were combined, washed with brine and water, then dried over MgSO4, and filtered. Removal of solvent yields a yellow oil (2.93 g, 75%). Step 3: Tert-butyl 4-(4-bromophenoxy)butylcarbamate 4-(4-bromophenoxy)butan-1-amine (1.0 g, 4.09 mmol) was dissolved in anhydrous THF (20 mL) under nitrogen and stirred until solution is homogenous. Di-tert-butyl-dicarbonate (1.34 g, 6.14 mmol) was added and the reaction was stirred at 40° C. for 2 hours. The reaction was quenched with water (30 mL) and stirred at room temperature for 1.0 hour. The aqueous layer was extracted with ethyl acetate (50 mL×2). The organic layers were combined, washed with saturated NaHCO3, water, and brine, then dried over MgSO4, and filtered. Removal of solvent yield a solid, which was purified by column chromatography (9:1, hexanes:EtOAc) to yield white solids (1.0 g, 71%). Example 4b: Synthesis of tert-butyl 4-(4-bromophenyl)butanoate Allowed tert-butanol to melt and added 20 mL to round bottom flask. To the solution, added di-tert-butyl-dicarbonate (1.79 g, 8.22 mmol) and 4-(4-bromophenyl)butyric acid (1.0 g, 4.11 mmol). To reaction, then added DMAP (150.7 mg, 1.23 mmol) and stirred reaction at room temperature over night. The reaction was concentrated via vacuo, and re-diluted in ethyl acetate. The organic layer was washed with 1M HCl, brine, and water. After removal of solvent, the crude solids were purified via column chromatography (20:1, hexanes:EtOAc) to give the desired product (570 mg, 46%), which is a clear oil. 1H NMR (500 MHz, CD2Cl2): δ=7.39-7.41 (d, 2H), 7.03-7.09 (d, 2H), 2.57-2.60 (t, 2H), 2.18-2.21 (t, 2H), 1.83-1.186 (p, 2H), 1.42 (s, 9H). Example 4c: Synthesis of 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid Combined 4-(4-bromophenyl)butyric acid (10 g, 41.13 mmol), bis(pinacolato)diboron (15.67 g, 61.70 mmol), potassium acetate (12.11 g, 123.4 mmol), and DMSO (100 mL), and purged mixture with nitrogen for 10 minutes at room temperature. To reaction under nitrogen, added Pd(dppf)Cl2 and purged reaction again with nitrogen for another 20 minutes at room temperature. The reaction was then refluxed at 80° C. over night. After cooling to room temperature, the reaction was quenched with water and stirred for 1.0 hour. The solids formed were filtered using Buchner funnel. The crude solids were purified via column chromatography (8.5:1.5, hexanes:EtOAc). The desired fractions were collected and concentrated via vacuo, and triturated with hexanes and filtered to give the desired white solids (6.7 g, 56%). Example 5: Synthesis of Linker or Capping Unit, Tert-butyl 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenoxy)butylcarbamate Combined tert-butyl 4-(4-bromophenoxy)butylcarbamate from Example 4a (500 mg, 1.45 mmmol), potassium acetate (428 mg, 4.36 mmol), bis(pinacolato)diboron (737 mg, 2.90 mmol) and DMSO (12 mL), and purged mixture with nitrogen for 10 minutes at room temperature. To mixture was added Pd(dppf)Cl2 (59.3 mg, 0.07 mmol) and continued to stir solution at room temperature under nitrogen for another 20 minutes. After refluxing at 80° C. for 3 hours, the reaction was cooled to room temperature and quenched with water (30 mL). The aqueous layer was extracted with dichloromethane (50 mL×2). The organic layers were combined, washed with brine, then dried over MgSO4, and filtered. Removal of solvent yield a dark brown oil, which was purified by column chromatography (9:1, hexanes:EtOAc) to yield a light yellow oil (539 mg, 95%). Example 6: Synthesis of Linker or Capping Unit with Long Oligoether Spacer Between Arylhalide Phenyl and FMOC Protected Primary Amine 4-(4-bromophenoxy)butan-1-amine+oligoether-FMOC+N,N′-dicyclohexylcarbodiimide (DCC) (9H-fluoren-9-yl)methyl 80-(4-bromophenoxy)-75-oxo-3,6,9,12,15,18,21,24,27,30,33,36,39,42,45,48,51,54,57,60,63,66,69,72-tetracosaoxa-76-azaoctacontylcarbamate. 4-(4-bromophenoxy)butan-1-amine (21.5 mg, 0.09 mmol), 1-(9H-fluoren-9-yl)-3-oxo-2,7,10,13,16,19,22,25,28,31,34,37,40,43,46,49,52,55,58,61,64,67,70,73,76-pentacosaoxa-4-azanonaheptacontan-79-oic acid (100 mg, 0.073 mmol), and N,N′-dimethylaminopyridine (5.4 mg, 0.044 mmol) were combined in a round bottom flask flushed with nitrogen and charged with a Teflon stirbar. Next 5 mL of anhydrous dichloromethane was added via syringe. N,N-Dicyclohexylcarbodiimide (23 mg, 0.11 mmol) is transferred to a second flask flushed with nitrogen and charged with a stirbar and 5 mL of anhydrous dichloromethane is added via syringe. While stirring the first solution, add the dicyclohexylcarbodiimide solution slowly, dropwise. The reaction is then allowed to proceed overnight. The following day solids from the reaction were filtered off and the filtrate was concentrated onto silica. Column chromatography in methanol and dichloromethane gave a clear thick oil (83.3 mg, 71% yield). Example 7: Synthesis of Polymer, Poly[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene}-co-3,5-phenylbut-V-oxy-4″-amine], with an Internal Linking Site The incorporation of internal conjugation sites into conjugated polymer backbones is described in U.S. application Ser. No. 11/868,870, filed Oct. 8, 2007 and published as U.S. Application No. 2008/0293164, which application is herein incorporated by reference in its entirety. Provided is a modified synthesis based on the protocol. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.084 mmol, 120 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (0.088 mmol, 135 mg), tert-butyl-4-(3,5-dibromophenoxy)butylcarbamate (0.0044 mmol, 2.0 mg), and palladium tetra(triphenylphosphine) (0.0035 mmol, 4 mg) are combined in a round bottom flask equipped with a stirbar. Next, 0.35 mL of 2M potassium carbonate (aq) and 1.9 mL of tetrahydrofuran are added and the flask is fitted with a vacuum adaptor and put on a Schlenk line. The mixture is degassed using 3 freeze-pump-thaw cycles. The degassed mixture is heated to 80 C under nitrogen with vigorous stirring for 18 hours. The reaction mixture is then cooled and the solvent is removed with rotary evaporation. Next, 4 mL of 4 M HCl in dioxane is added and the mixture is stirred for no less than 4 hours. The solution is neutralized with 2M potassium carbonate solution. The bulk of the solvent is again removed with rotary evaporation. The resulting semisolid is diluted with ca. 50 mL water and filtered through glass fiber filter paper. Ethanol is added to adjust the solvent to 20% ethanol in water. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and 100 mg of poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene}-co-3,5-tert-butyl-4-(4-bromophenoxy)amine] is collected as an amber oil. Example 8: Synthesis of Phenylene Vinylene Co-Polymer with an Internal Linking Site A modified synthesis similar to that described in Examples 7 and 15. Example 9: Synthesis of Polymer with Exclusively Terminal Amine Capping Units 2,7-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene])-diphen-4-oxybutyl-4′-amine. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.163 mmol, 235 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (0.163 mmol, 250 mg), and palladium tetra(triphenylphoshine) (0.0065, 7.5 mg) are combined in a round bottom flask equipped with a stirbar. Next, 0.75 mL of 2M potassium carbonate (aq) and 3 mL of tetrahydrofuran are added and the flask is fitted with a vacuum adaptor. The reaction mixture is put on a Schenk line and is degassed with three freeze-pump-thaw cycles and then heated to 80 C under nitrogen with vigorous stirring for 18 hours. A solution of tert-butyl 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenoxy)butylcarbamate (0.064 mmol, 25 mg) in 0.5 mL tetrahydrofuran is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction is allowed to continue for an additional 4 hours at 80 C with stirring. Next, a solution of tert-butyl 4-(4-bromophenoxy)butylcarbamate (0.192 mmol, 66 mg) in 0.5 mL of THF is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction was allowed to proceed overnight. The reaction mixture was allowed to cool and solvent was removed with rotary evaporation. A 4 mL portion of 4M HCl in dioxane was added to the residue and stirred for a minimum of 4 hours. The solution was neutralized with 2 M potassium carbonate (aq) and then the solvent was removed under vacuum. The resulting residue was diluted to ˜30 mL with 20% ethanol in water and filtered. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and 337 mg of polymer is collected as an amber oil. The order of end linker addition (aryl hylide or boronic ester/acid) can be reversed. Similar processes can be used to add alternative linkers or end capping units. Example 10: Synthesis of Polymer, 2-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene])-phen-4-oxybutyl-4′-amine, Statistically Enriched in Chains with a Single Terminal Amine Capping Unit 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.163 mmol, 235 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (0.163 mmol, 250 mg), and palladium tetra(triphenylphoshine) (0.0065, 7.5 mg) are combined in a round bottom flask equipped with a stirbar. Next, 0.75 mL of 2M potassium carbonate (aq) and 3 mL of tetrahydrofuran are added and the flask is fitted with a vacuum adaptor. The reaction mixture is put on a Schenk line and is degassed with three freeze-pump-thaw cycles and then heated to 80 C under nitrogen with vigorous stirring for 18 hours. A solution of tert-butyl 4-(4-bromophenoxy)butylcarbamate (0.049 mmol, 17 mg) in 0.5 mL tetrahydrofuran is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction is allowed to continue for an additional 4 hours at 80 C with stirring. Next, a solution of phenylboronic acid (0.150 mmol, 18 mg) in 0.5 mL of THF is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction was allowed to proceed overnight. The reaction mixture was allowed to cool and solvent was removed with rotary evaporation. A 4 mL portion of 4M HCl in dioxane was added to the residue and stirred for a at least 4 hours. The solution was neutralized with 2 M potassium carbonate (aq) and then the solvent was removed under vacuum. The resulting residue was diluted to ˜30 mL with 20% ethanol in water and filtered. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and 315 mg of polymer is collected as an amber oil. Resulting polymers contain chains with an enriched fraction of chains with one amine linker plus chains with 2 linkers and no linkers. Example 11: Synthesis of Polymer Statistically Enriched in Chains with a Single Terminal Capping Unit with a Long Oligoether Spacer (24 Repeats) Between the Polymer Chain and the Primary Amine Linking Group 2-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene])-phen-4-oxybutyl-4′-amine. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.163 mmol, 235 mg), 9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-2,7-di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)fluorene (0.163 mmol, 250 mg), and palladium tetra(triphenylphoshine) (0.0065, 7.5 mg) are combined in a round bottom flask equipped with a stirbar. Next, 0.75 mL of 2M potassium carbonate (aq) and 3 mL of tetrahydrofuran are added and the flask is fitted with a vacuum adaptor. The reaction mixture is put on a Schenk line and is degassed with three freeze-pump-thaw cycles and then heated to 80 C under nitrogen with vigorous stirring for 18 hours. A solution of tert-butyl 4-(4-bromophenoxy)butylcarbamate (0.049 mmol, 17 mg) in 0.5 mL tetrahydrofuran is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction is allowed to continue for an additional 4 hours at 80 C with stirring. Next, a solution of phenylboronic acid (0.150 mmol, 18 mg) in 0.5 mL of THF is degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction was allowed to proceed overnight. The reaction mixture was allowed to cool and solvent was removed with rotary evaporation. A 4 mL portion of 4M HCl in dioxane was added to the residue and stirred for a minimum of 4 hours. The solution was neutralized with 2 M potassium carbonate (aq) and then the solvent was removed under vacuum. The resulting residue was diluted to ˜30 mL with 20% ethanol in water and filtered. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and 315 mg of polymer is collected as an amber oil. Example 12: Synthesis of an Asymmetric Polymer with a Terminal Carboxylic Capping Unit Added During Polymerization Reaction The linking monomer is added during the polymerization reaction as described in Examples 9, 10 and 11. The carboxylic acid group can later be converted to an activated ester such as N-hydroxysuccinimidyl as is described in Example 29. Example 13: Synthesis of an Asymmetric Polymer with a Terminal Carboxylic Acid Capping Unit Added Post Polymerization The linking monomer is added after the polymerization reaction is completed and polymer purified. Linker addition is done under similar reaction conditions as those described in Examples 9, 10 and 11. The carboxylic acid group can later be converted to an activated ester such as N-hydroxysuccinimidyl as is described in Example 29. Example 14: Synthesis of an Polymer with Branched PEG Groups Example 14a: Synthesis of Monomers, (D) and (E) for Subsequent Polymerization Step 1: 2,7-dibromo-9,9-bis(3,5-dimethoxybenzyl)fluorene 2,7-dibromofluorene (4.16 g, 12.8 mmol) and tetrabutylammonium bromide (362 mg, 1.12 mmol) were added to a round bottom flask charged with a Teflon stirbar. Next, 60 mL of dimethylsulfoxide was added to the flask and the mixture was stirred for 5 minutes. A portion of 50% NaOH aqueous solution (5.2 mL) was added followed immediately by 3,5-dimethoxybenzyl bromide (7.14 g, 31 mmol). Over the course of 2 hours the solution changes color from orange to blue. The reaction is stirred overnight. The resulting mixture is slowly poured into 200 mL of water and then extracted with three 100 mL portions of dichloromethane. The organic layers are combined and dried over magnesium sulfate and then filtered. The crude product is purified by column chromatography using hexanes and dichloromethane as eluent to give a pale yellow solid (6.63 g, 79% yield). Step 2: 2,7-dibromo-9,9-bis(3,5-dihydroxybenzyl)-9H-fluorene 2,7-dibromo-9,9-bis(3,5-dimethoxybenzyl)-9H-fluorene (1.3 g, 2.08 mmol) was added to a round bottom flask charged with a stirbar and equipped with a rubber septum. The flask is purged with nitrogen for 10 min. Anhydrous dichloromethane (20 mL) is transferred to the flask via cannula and the mixture is stirred until the solids are completely dissolved. The solution is then cooled with a dry ice/acetone bath for 10 minutes. BBr3 (6.1 mL, 63.3 mmol) is added dropwise via cannula with constant stirring. The bath is allowed to warm to room temperature and the mixture is stirred overnight. The reaction is quenched with the slow addition of 125 mL of water. The solution is then extracted with 3 portions of ethyl acetate (50 mL). The organic layer is dried over MgSO3, filtered, and dried onto silica. Flash chromatography of the crude using ethyl acetate in dichloromethane gives an off-white crystalline solid (800 mg, 68% yield). Step 3: 2,7-dibromo-9,9-bis(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl) benzyl)-9H-fluorene (D) 2,7-dibromo-9,9-bis(3,5-dihydroxybenzyl)-9H-fluorene (537 mg, 0.945 mmol), 2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 4-methylbenzenesulfonate (2.788 g, 4.156 mmol), potassium carbonate (1.57 g, 11.34 mmol) and acetone (80 mL) are transferred to a round bottom flask charged with a Teflon stirbar and equipped with a reflux condenser. The mixture is refluxed with constant stirring overnight. The mixture is then allowed to cool to room temperature and the acetone is removed under vacuum. After extracting with 3 portions of dichloromethane, the organic layer is dried over MgSO4, filtered, and the filtrate is concentrated onto silica. Column chromatography using methanol and dichloromethane affords the product as a slightly colored thick oil (1.69 g, 70% yield). Step 4: 2,7- di(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolanyl)-9,9-bis(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl) benzyl)-9H-fluorene (E) Monomer (E) is synthesized using conditions similar to conditions as described in Example 1. Example 14b: Polymerization of (D) and (E) Polymerization of (D) and (E) are polymerized using conditions similar to polymerization conditions as described in Example 1b. Example 15: Synthesis of a neutral base phenylene vinylene co-polymer 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (0.25 mmol), 1,4-divinylbenzene (32.3 mg, 0.25 mmol), palladium acetate (3 mg, 0.013 mmol), tri-ortho-tolylphosphine, (10 mg, 0.033 mmol), and potassium carbonate (162 mg, 1.2 mmol) are combined with 5 mL of DMF in a small round bottom flask charged with a Teflon coated stirbar. The flask is fitted with a needle valve and put in a Schlenk line. The solution is degassed by three cycles of freezing, pumping, and thawing. The mixture is then heated to 100° C. overnight. The polymer can be subsequently reacted with terminal linkers or capping units using similar (in situ) protocols to those provided in the previous examples (9, 10 and 11) or by modifying them post polymerization work up as a separate set of reactions. Example 16: Synthesis of a Branched Phenylene Vinylene Co-Polymer 2,7-dibromo-9,9-bis(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl) benzyl)-9H-fluorene (636 mg, 0.25 mmol), 1,4-divinylbenzene (32.3 mg, 0.25 mmol), palladium acetate (3 mg, 0.013 mmol), tri-ortho-tolylphosphine, (10 mg, 0.033 mmol), and potassium carbonate (162 mg, 1.2 mmol) were combined with 5 mL of DMF in a small round bottom flask charged with a Teflon coated stirbar. The flask was fitted with a needle valve and put in a Schlenk line. The solution was degassed by three cycles of freezing, pumping, and thawing. The mixture was then heated to 100° C. overnight. The polymer can be subsequently reacted with terminal linkers or capping units using similar (in situ) protocols to those provided in Example 5 or by modifying them post polymerization work up as a separate set of reactions. Example 17: Synthesis of a branched phenylene vinylene co-polymer with functional amines for covalent conjugation. Poly [2,7-divinyl{9,9-bis(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl)benzyl)-9H-fluorene}-alt-1,4-benzene-co-4-phenoxybutyl-N-t-butylcarbamate] Step 1: Polymerization 2,7-dibromo-9,9-bi s(3,5-(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl) benzyl)-9H-fluorene (636 mg, 0.25 mmol), 1,4-divinylbenzene (32.3 mg, 0.25 mmol), palladium acetate (3 mg, 0.013 mmol), tri-ortho-tolylphosphine, (10 mg, 0.033 mmol), and potassium carbonate (162 mg, 1.2 mmol) were combined with 5 mL of DMF in a small round bottom flask charged with a Teflon coated stirbar. The flask was fitted with a needle valve and put in a Schlenk line. The solution was degassed by three cycles of freezing, pumping, and thawing. The mixture was then heated to 100° C. overnight. Step 2: Linker Addition The next morning divinylbenzene (10 mg, 0.077 mmol) was transferred to a small round bottom flask with 1 mL of DMF. The flask was fitted with a needle valve and put in a Schlenk line. The solution was degassed by three cycles of freezing, pumping, and thawing. The solution was transferred via cannula through the needle valves and into the polymerization reaction. After this addition the reaction was allowed to continue at 100° C. overnight. The next day tert-butyl 4-(4-bromophenoxy)butylcarbamate (53 mg, 0.15 mmol) and 1 mL of DMF were transferred to a small round bottom flask. The flask was fitted with a needle valve and put in a Schlenk line. The solution was degassed by three cycles of freezing, pumping, and thawing. The solution was transferred via cannula through the needle valves and into the polymerization reaction. After this addition the reaction was allowed to continue at 100° C. overnight. Step 3: Work Up The reaction is then cooled and diluted with 100 mL of water. The aqueous solution was filtered twice through G-6 glass fiber filter paper. The filtrate was evaporated to dryness and re-diluted with dichloromethane. The organic layer was dried over MgSO4 and filtered. The filtrate was evaporated to yield an amber colored oil (342 mg, 56% yield). A 4 mL portion of 4M HCl in dioxane was added to the polymer residue and stirred for a minimum of 4 hours. The solution was neutralized with 2 M potassium carbonate (aq) and then the solvent was removed under vacuum. The resulting residue was diluted to ˜30 mL with 20% ethanol in water and filtered. Preparative gel permeation chromatography is performed with G-25 desalting medium to remove excess salts from the polymer. Solvent in the fractions is removed with rotary evaporation and the polymer is collected as an amber oil. The linker or capping unit addition steps can be performed in the polymerization reaction as presented above or alternatively, in some embodiments, can be performed in a separate set of reactions after the polymerization work up. In the latter case, the polymer is reacted under the analogous conditions as those provided in the example. In other embodiments, it is also possible to react with a combination of terminal monomers to introduce polymers with bi-functionality, allowing the polymer to be conjugated to more than one entity. Example 18: Synthesis of a Fluorene Monomer with Glycerol-Based Dendrimers Step 1: Dimethyl 3,3′-(2,7-dibromo-9H-fluorene-9,9-diyl)dipropanoate 2,7-Dibromofluorene (1 g, 3.1 mmol), methyl acrylate (861 mg, 10 mmol) tetrabutylammonium bromide (100 mg, 0.3 mmol) and toluene (5 mL) were added to a small round bottom flask with a Teflon-coated stirbar. Next 2 mL of 50% NaOH (aq) is added while stirring. The reaction is allowed to proceed overnight. The next day the toluene layer is transferred to a flask and the aqueous layer extracted with two portions of toluene. The organic layers are combined, dried with Mg2SO4, and filtered. Silica (2 g) is added to the filtrate and the solution is evaporated. The product is obtained as a white solid (1.23 g, 80% yield) after purification by column chromatography. Step 2: 3,3′-(2,7-dibromo-9H-fluorene-9,9-diyl)dipropanoic acid Dimethyl 3,3′-(2,7-dibromo-9H-fluorene-9,9-diyl)dipropanoate (1.23 g, 2.5 mmol) is transferred to a small round bottom flask equipped with a Teflon-coated stirbar. A mixture of THF:MeOH:H2O, 3:2:1, (10 mL) is added and the mixture is stirred for 1 hr. Then a 1 mL portion of 1M NaOH (aq) is added and the mixture is stirred overnight. The next day the water layer is isolated and extracted with 20 mL portions diethyl ether three times. Next the water layer is acidified to ˜pH 2. The water layer is extracted three times with 20 mL portions of dichloromethane. The organic layers are combined and dried with Mg2SO4. The organic solution is filtered and the solvent evaporated to obtain the product as an off-white solid (948 mg, 90% yield). Step 3: 3,3′-(2,7-Dibromo-9H-fluorene-9,9-diyl)bis(N-(7,15-bis((2,3-dihydroxypropoxy)methyl)-1,3,19,21-tetrahydroxy-5,9,13,17-tetraoxahenicosan-11-yl)propanamide) 3,3′-(2,7-Dibromo-9H-fluorene-9,9-diyl)dipropanoic acid (500 mg, 1.1 mmol), 11-amino-7,15-bis((2,3-dihydroxypropoxy)methyl)-5,9,13,17-tetraoxahenicosane-1,3,19,21-tetraol (1.954, 3.3 mmol) (prepared as per ref. Heek, T.; Fasting, C.; Rest, C.; Zhang, X.; Wurthner, F.; Haag, R. Chem. Commun., 2010, 46, 1884-1886), and N,N′-dimethylaminopyridine (61 mg, 0.5 mmol) are combined in a round bottom flask equipped with a Teflon-coated stirbar and sealed with a rubber septum. The flask was flushed with N2 and 10 mL of anhydrous dichloromethane was added via syringe. The mixture is stirred to dissolve the solids. In another round bottom flask equipped with a Teflon-coated stirbar, dicyclohexylcarbodiimide (DCC, 910 mg 4.4 mmol) transferred and the flask is sealed with a rubber septum. Next, 5 mL of anhydrous dichloromethane is transferred to the flask via syringe. The DCC solution is transferred to the fluorene reaction mixture via a syringe dropwise. The reaction is allowed to react overnight. The next day the reaction mixture is filtered. The filtrate is purified by column chromatography to afford a clear oil (1.24 g, 70% yield). Example 19: Synthesis of a Fluorene Monomer PAMAM-Based Dendritic Side Chain Capped with methylPEG Chains Step 1: 9,9′-(3,3′-Diamido(tetramethyl PAMAM G[2])-2,7-dibromofluorene (i) Dimethyl 3,3′-(2,7-dibromo-9H-fluorene-9,9-diyl)dipropanoate (1 g, 2.0 mmol) is transferred to a round bottom flask equipped with a stirbar and sealed with a rubber septum. The flask is flushed with nitrogen and 10 mL of dry methanol is transferred to the flask via syringe and the solid is dissolved by stirring. Ethylenediamine (5.5 mL, 82 mmol) is added via syringe slowly and the mixture is allowed to stir for 2 hours. The septum is removed and the methanol and unreacted ethylenediamine is removed under vacuum. Another 10 mL portion of methanol is added and stirred and then was evaporated to remove any remaining ethylenediamine. The residue remaining in the flask was then sealed again with a septum, flushed with nitrogen, and dry methanol (10 mL) was added and stirred. Methyl acrylate (7.2 mL, 80 mmol) is added slowly via syringe and the mixture is allowed to stir for 2 hours. The septum is again removed and the methanol and methyl acrylate are removed under vacuum. A 10 mL portion of toluene is added, the mixture stirred, and the solvent removed under vacuum affording an off-white solid (1.79 g, quantitative yield). Step 2: 9,9′-(3,3′-Diamido(PAMAM G[2] tetraacid)-2,7-dibromofluorene (ii) 9,9′-(3,3′-Diamido(tetramethyl PAMAM G[2])-2,7-dibromofluorene (i) (1.79 g, 2 mmol) is transferred to a small round bottom flask equipped with a Teflon-coated stirbar. A mixture of THF:MeOH:H2O, 3:2:1, (10 mL) is added and the mixture is stirred for 1 hr. Then a 1 mL portion of 1M NaOH (aq) is added and the mixture is stirred overnight. The next day the water layer is isolated and extracted with 20 mL portions diethyl ether three times. Next the water layer is acidified to ˜pH 2. The water layer is extracted three times with 20 mL portions of dichloromethane. The organic layers are combined and dried with Mg2SO4. The organic solution is filtered and the solvent evaporated to obtain the product as an off-white solid (1.51 g, 90% yield). Step 3: 9,9′-(3,3′-Diamido(PAMAM G[2] N-(2,5,8,11,14,17,20,23-octaoxapentacosane-25-yl)propionamidyl)-2,7-dibromofluorene (iii). 9,9′-(3,3′-Diamido(PAMAM G[2] tetraacid)-2,7-dibromofluorene (ii) (500 mg, 0.6 mmol), 2,5,8,11,14,17,20,23-octaoxapentacosan-25-amine (1.15 g, 3 mmol)), and N,N′-dimethylaminopyridine (12 mg, 0.1 mmol) are combined in a round bottom flask equipped with a Teflon-coated stirbar and sealed with a rubber septum. The flask was flushed with N2 and 10 mL of anhydrous dichloromethane was added via syringe. The mixture is stirred to dissolve the solids. In another round bottom flask equipped with a Teflon-coated stirbar, dicyclohexylcarbodiimide (DCC, 825 mg 4.0 mmol) transferred and the flask is sealed with a rubber septum. Next, 5 mL of anhydrous dichloromethane is transferred to the flask via syringe. The DCC solution is transferred to the fluorene reaction mixture via a syringe dropwise. The reaction is allowed to react overnight. The next day the reaction mixture is filtered. The filtrate is purified by column chromatography to afford a clear oil (967 g, 70% yield). Example 20: Synthesis of a Fluorene Monomer with Highly Branched PEGylated Side Chains Based on a Trihydroxybenzene Linkage Step 1: Methyl 3,4,5-tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)benzoate (iv) Methyl 3,4,5-trihydroxybenzoate (200 mg, 1.1 mmol), 2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 4-methylbenzenesulfonate (2.58 g, 3.85 mmol), and 18-crown-6 (100 mg, 0.38 mmol) are transferred to a round bottom flask equipped with a Teflon-coated stirbar. Acetone (10 mL) is added and the flask is equipped with a reflux condenser. The mixture is refluxed with constant stirring overnight. The next day silica (4 g) is added and the solvent evaporated. After purification by column chromatography, a clear oil is obtained (887 mg, 48% yield). Step 2: 3,4,5-Tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)-N-(2-aminoethyl)benzamide (v) Methyl 3,4,5-tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)benzoate (iv) (887 mg, 0.52 mmol) flask is transferred to a round bottom flask equipped with a stirbar and sealed with a rubber septum. The flask is flushed with nitrogen and 10 mL of dry methanol is transferred to the flask via syringe and the solid is dissolved by stirring. Ethylenediamine (0.7 mL, 10.4 mmol) is added via syringe slowly and the mixture is allowed to stir for 2 hours. The septum is removed and the methanol and unreacted ethylenediamine is removed under vacuum. The product is obtained as an oil (886 mg, quantitative yield). Step 3:] 3,3′-(2,7-Dibromo-9H-fluorene-9,9-diyl)bis(N-(2-3,4,5-tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)-benzamidyl-N amidoethyl)propanamide) (vi) 3,4,5-Tris(2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yloxy)-N-(2-aminoethyl)benzamide (v) (886 mg, 0.52 mmol), 3,3′-(2,7-Dibromo-9H-fluorene-9,9-diyl)dipropanoic acid (112 mg, 0.24 mmol), and N,N′-dimethylaminopyridine (12 mg, 0.1 mmol) are combined in a round bottom flask equipped with a Teflon-coated stirbar and sealed with a rubber septum. The flask was flushed with N2 and 10 mL of anhydrous dichloromethane was added via syringe. The mixture is stirred to dissolve the solids. In another round bottom flask equipped with a Teflon-coated stirbar, dicyclohexylcarbodiimide (DCC, 148 mg 0.72 mmol) transferred and the flask is sealed with a rubber septum. Next, 5 mL of anhydrous dichloromethane is transferred to the flask via syringe. The DCC solution is transferred to the fluorene reaction mixture via a syringe dropwise. The reaction is allowed to react overnight. The next day the reaction mixture is filtered. The filtrate is purified by column chromatography to afford a clear oil (924 mg, 70% yield). Example 21. Dual End Capped Polymer Used to Create a Polymer-Dye Label for Biomolecule or Substrate Conjugation Step 1: Synthesis of an Asymmetric Neutral Water-Soluble Polymer with a t-BOC Protected Amine Pendant Group at One Terminus of the Polymer 2-bromo-7-(4″-phenoxybutyl-1-tert-butyl carbamate)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene. 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (1.0 g, 0.674 mmol), 3 mL of tetrahydrofuran, and 2 mL of 2M potassium carbonate (aqueous) were transferred to a small round bottom flask charged with a Teflon stirbar. The flask was fitted with a septum and the solution is degassed by sparging with Ar for 15 minutes. Palladium tetra(triphenylphoshine) (15.6 mg, 0.013 mmol) was added through the neck of the flask and the flask was transferred to a reflux condenser equipped with a needle valve and fixed to a Schlenk line. The solution was quickly frozen solid with liquid nitrogen and was further degassed using freeze-pump-thaw technique. Once degassed the reaction was heated to 80° C. with constant stirring. The reaction was allowed to proceed overnight. The next day tert-butyl 4-(4-bromophenoxy)butylcarbamate (35 mg, 0.10 mmol) in 1 mL of THF was degassed with three freeze-pump-thaw cycles and then added to the polymerization reaction via cannula under excess nitrogen pressure. The reaction continued overnight at 80° C. The next day the reaction mixture was cooled and the bulk of the solvent was removed under vacuum. The remaining material was transferred to a small Erlenmeyer flask with a total of ˜50 mL of dichloromethane. The solution was stirred for 30 minutes. Approximately 1 g of MgSO4(anhydrous) was added to the solution and the mixture was filtered through a fluted paper filter. The filtrate was evaporated and 410 mg (47% yield) of an amber oil was collected. Step 2: Synthesis to Append a Terminal Linking Monomer with a t-Butyl Ester at the Terminus Opposite the Protected Amine Pendant 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-tert-butyl carbamate)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene. 2-Bromo-7-(4″-phenoxybutyl-1-tert-butyl carbamate)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene (410 mg, 0.32 mmol of repeat unit), tert-butyl 1-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenoxy)-3,6,9,12,15,18,21-heptaoxatetracosan-24-oate (33 mg, 0.048 mmol), 2 mL of tetrahydrofuran, and 1.5 mL of 2M potassium carbonate (aqueous) were transferred to a small round bottom flask charged with a Teflon stirbar. The flask was fitted with a septum and the solution is degassed by sparging with Ar for 15 minutes. Palladium tetra(triphenylphoshine) (15 mg, 0.013 mmol) was added through the neck of the flask and the flask was transferred to a reflux condenser equipped with a needle valve and fixed to a Schlenk line. The solution was quickly frozen solid with liquid nitrogen and was further degassed using freeze-pump-thaw technique. Once degassed the reaction was heated to 80° C. with constant stirring. The reaction was allowed to proceed overnight. The remaining material was transferred to a small Erlenmeyer flask with a total of ˜50 mL of dichloromethane. The solution was stirred for 30 minutes. Approximately 1 g of MgSO4(anhydrous) was added to the solution and the mixture was filtered through a fluted paper filter. The filtrate was evaporated and 351 mg (78% yield) of an amber oil was collected. Step 3: Synthesis of a Neutral Water-Soluble Polymer with Primary Amine at One Terminus and a t-Butyl Ester Pendant on the Other 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-amino)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene. 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-tert-butyl carbamate)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene (23 mg, 0.018 mmol) and 0.5 mL of 4M HCl in dioxane were combined in a 1 dram vial with a Teflon-coated stirbar. The mixture was stirred for 4 hours. The mixture was neutralized with 2M potassium carbonate (aqueous). The solution was then diluted to 50 mL of roughly 20% ethanol in water and filtered through G-6glass fiber filter paper. The filtrate was desalted by centrifugation in a 4 mL 10 KDa cutoff centrifuge filter. The retentate was evaporated under vacuum and two 1 mL portions of toluene were added and removed under vacuum to remove any remaining water. A thick amber liquid was recovered from the desalting (21 mg, 85% yield). Step 4: Attachment of an NHS-Functionalized Dye to a Primary Amine Pendant on a Neutral Water-Soluble Polymer 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-amido-DYE)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene. 2-(4-(tert-butyl 1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosan-27-oate))-7-(4″-phenoxybutyl-1-amino)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene (518 ug, 0.4 μM) was dissolved in 100 μL of dry dichloromethane in a glass vial. A small crystal of 4-N,N′-dimethylaminopyridine was added. In another vial 65 μg (0.06 □uM) of NHS-functionalized DyLight 594 (Pierce) was dissolved in 50 of dry dichloromethane. The two solutions were combined and allowed to stir in a sealed vial for 4 hours covered in foil. The solvent was then evaporated and the remaining material was dissolved in 95% ethanol and injected onto a Sepharose 6 column. The remaining dye was separated from the polymer. A solution of dye-labeled polymer was obtained from combining fractions (100 μg, 20% yield). Step 5: Hydrolysis of the t-Butyl Ester Pendant on the Dye-Labeled Neutral Water-Soluble Polymer to Form the Carboxylic Acid Pendant on One of the Termini 2-(4-(1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosane-27-acid))-7-(4″-phenoxybutyl-1-amido-DYE)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene. The polymer was combined with ZnBr2 in dichloromethane and stirred overnight. The next day a portion of water was added and the mixture was stirred for 1 hour. The solvent was evaporated and the residue was dissolved in 20% ethanol in water. The filtrate was then desalted by centrifugation in a 4 mL 10 KDa cutoff centrifuge filter. The retentate was evaporated under vacuum and two 1 mL portions of toluene were added and removed under vacuum to remove any remaining water. Activation (for subsequent conjugation) of the second functional group in this example (carboxylic acid) can be achieved using a number of different methods including those described in Examples 29 and other examples with carboxylic acid to amine to maleimide. One such method is given below in Step 6, by way of example only. Step 6: NHS Activation of the Carboxylic Acid Penant of a Dye-Labeled Neutral Water-Soluble Polymer 2-(4-(1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosane-27-N-hydroxysuccinimidyl ester))-7-(4″-phenoxybutyl-1-amido-DYE)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene. 2-(4-(1-phenoxy-3,6,9,12,15,18,21,24-octaoxaheptacosane-27-acid))-7-(4″-phenoxybutyl-1-amido-DYE)-poly-2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene and O—(N-Succinimidyl)-1,1,3,3-tetramethyluronium tetrafluoroborate and DIPEA are combined in dry acetonitrile and allowed to react under nitrogen for 30 min. The solution is evaporated and the solid is resuspended in dry dichloromethane. Solids are filtered off and the filtrate is evaporated to afford the NHS ester. In further embodiments, various commonly used protecting groups can be used with those functional groups provided (amine and carboxylic acid). Additionally different capping monomers and protecting group combinations can be used to produce polymers with different functional groups for conjugation. Eliminating or substituting the dye labeling step for another entity will result in a polymer with two different functional groups for conjugation. The dye attachment via NHS/amine chemistry can be performed under a variety of commonly used conditions. Dye attachment can also be performed with other functional chemistries. Example 22. Asymmetric Polyfluorene Synthesis Using Non-Regulated Suzuki Conditions Step 1: Polymerization Method A: A solution of K2CO3 in water (2M, 4 mL) was added to a stirred mixture of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (A) (2.3 g, 1.5 mmol) and THF (6 mL) in a round bottom flask. This mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (38.5 mg, 0.03 mmol) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. The reaction mixture was cooled to 23° C. and solvent removed by rotary evaporation. The resulting residue was transferred to an Erlenmeyer flask and diluted with 20% EtOH/H2O (75 mL). EDTA (300 mg, 1.0 mmol) was added to the mixture and stirred at 23° C. for 1 h. The mixture was filtered through a glass fiber filter paper and the filter paper rinsed with 20% EtOH/H2O. The resulting filtrate was then filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (regenerated cellulose Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until conductivity of the filtrate measured less than 0.01 mS/cm. The solvent was then removed under vacuum to give poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene] (B) as a gel-like product (1.41 g, 71%) Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=51,000, Mw=108,000, Mp=90,000, D=2.1). The extent of end linker incorporation was determined by first converting the acid to an NHS ester (similar protocol to that provided in Example 29) then reacting with an amine functional dye. After purification of free dye the ratio of dye to polymer was determined from absorbance measurements, factoring in the difference in extinction coefficients and polymer molecular weight. Method B: A solution of K2CO3 in water (2M, 4 mL) was added to a stirred mixture of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (A) (2.3 g, 1.5 mmol) and DMF (6 mL) in a round bottom flask. This mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (38.5 mg, 0.03 mmol) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. Work-up and purification was performed in a manner similar to previously described Method A. Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=96,000, Mw=231,000, Mp=185,000, D=2.4). Method C: Cs2CO3 (2.08 g, 6.4 mmol) was added to a stirred mixture of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (A) (200 mg, 0.135 mmol) and DMF (7 mL) in a round bottom flask. This mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (15.6 mg, 10 mol %) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. Work-up and purification was performed in a manner similar to previously described Method A. Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=95,000, Mw=218,000, Mp=206,000, D=2.3). Step 2: End Capping -(4-iodophenyl)butanoic acid (227 mg, 0.783 mmol) was washed into a flask containing poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene] (B) (1.00 g, 0.783 mmol) using THF (3.5 mL). A solution of K2CO3 in water (2M, 2.3 mL) was added to the flask and this mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (36 mg, 4 mol %) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. The reaction mixture was cooled to 23° C. and the solvent removed with rotary evaporation. The resulting residue was transferred to an Erlenmeyer flask and diluted with 20% EtOH/H2O (150 mL). EDTA (500 mg) was added to the mixture and stirred at 23° C. for 1 h. The mixture was filtered through a glass fiber filter paper and the filter paper rinsed with 20% EtOH/H2O. The resulting filtrate was then filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (regenerated cellulose Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until conductivity of the filtrate measured less than 0.01 mS/cm. The solvent was then removed under vacuum to give 4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)phenyl)butanoic acid (C) as a gel-like product (388 mg, 39%) Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=89,000, Mw=196,000, Mp=124,000, D=2.2). The extent of end linker incorporation was determined by first converting the acid to an NHS ester (similar protocol to that provided in Example 29) then reacting with an amine functional dye. After purification of free dye the ratio of dye to polymer was determined from absorbance measurements, factoring in the difference in extinction coefficients and polymer molecular weight. Step 3: Amine Activation 4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)phenyl)butanoic acid (C) (200 mg, 0.156 mmol) was dissolved in 2 mL ethanol, then added drop-wise to 23 mL of MES buffer (50 mM, pH 5) at 4° C. while stirring. N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride (576 mg, 3.00 mmol) was added in portions, followed by N-hydroxy succinimide (115 mg, 1.00 mmol) in one portion. The solution was stirred for 30 minutes, ethylene diamine (0.501 mL, 7.50 mmol) was added drop-wise and the reaction mixture was stirred overnight at room temperature. The reaction mixture was then desalted over a G25 desalting column and the solvent removed via rotary evaporation to give N-(2-aminoethyl)-4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)butanamide as a clear yellow oil (190 mg, 95%). Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=89,000, Mw=196,000, Mp=124,000, D=2.2). Extent of amine conversion was determined by reacting the amine polymer with an NHS active dye in similar fashion as that described in Example 38. Example 23. Asymmetric Polyfluorene Synthesis Using Linker Modified End Caps to Regulate the Suzuki Polymerization Step 1: Polymerization/End Capping/Work-Up A solution of K2CO3 in water (2M, 4 mL) was added to a stirred mixture of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene (A) (2.3 g, 1.55 mmol), 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid (B) (6.7 mg, 2 mol %), and DMF (6 mL) in a round bottom flask equipped with a side-arm stopcock. This mixture was degassed with argon for 25 min. Palladium tetrakis(triphenylphosphine) (38.5 mg, 2 mol %) was then added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was further degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. Separately, 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid (B) (230 mg, 0.793 mmol) was dissolved in DMF (3 mL) in a found bottom flask equipped with a side arm stopcock. This solution was sparged with argon for 15 minutes, attached to a reflux condenser, and degassed via three freeze-pump thaw cycles. Upon thawing the solution was added to the reaction mixture after two hours of reaction time using an argon flushed syringe. The reaction mixture was stirred for an additional 12 h at 80° C. The reaction mixture was cooled to 23° C. and solvent removed with rotary evaporation. The resulting residue was transferred to an Erlenmeyer flask and diluted with 20% EtOH/H2O (75 mL). EDTA (300 mg, 1.00 mmol) was added to the mixture and stirred at 23° C. for 1 h. The mixture was filtered through a glass fiber filter paper and the filter paper rinsed with 20% EtOH/H2O. The resulting filtrate was then filtered through a 0.45 um cup filter. The filtered reaction mixture was purified and size fractionated using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 30,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until conductivity of the filtrate measured less than 0.01 mS/cm and Mn of the retentate measured more than 70,000 by GPC. The solvent was then removed under vacuum to give 4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)phenyl)butanoic acid as a gel-like product (1.41 g, 71%). Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=68,000, Mw=134,000, Mp=122,000, D=1.9). The extent of end linker incorporation was determined by first converting the acid to an NHS ester (similar protocol to that provided in Example 29) then reacting with an amine functional dye. After purification of free dye the ratio of dye to polymer was determined from absorbance measurements, factoring in the difference in extinction coefficients and polymer molecular weight. Despite having a molecular weight in excess of 50,000 g/mole the polymer is soluble in both water and phosphate buffered saline solutions at concentrations easily greater than 10 mg/mL. In many conjugation experiments the polymer provided (and other described herein with similar structure) was concentrated to 50 mg/mL or higher which is remarkable for a neutral conjugated polymer. The moderate molecular weight also provides extinction coefficients greater than 2,500,000 M−1cm−1. The large extinction coefficient and quantum yield of 60% (PBS) provide for exceptionally bright fluorescent reporters for use in biological assays including their use in flow cytometry. Step 2: Amine Activation 4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)phenyl)butanoic acid (C) (500 mg, 0.13 mmol) was dissolved in 2 mL ethanol, then added drop-wise to 23 mL of MES buffer (50 mM, pH 5) at 4° C. while stirring. N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride was added in portions, followed by N-hydroxy succinimide (0.52 g) in one portion. The solution was stirred for 30 minutes, ethylene diamine (2.8 mL) was added drop-wise and the reaction mixture was stirred overnight at room temperature. The reaction mixture was then desalted over a G25 desalting column and the solvent removed via rotary evaporation to give N-(2-aminoethyl)-4-(Poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene]yl)butanamide as a yellow oil (450 mg, 90%). Extent of amine conversion was determined by reacting the amine polymer with an NHS active dye in similar fashion as that described in Example 38. Example 24. Yamamoto polymerization of PEG modified polyfluorene Step 1: Yamamoto Polymerization/Work-Up In a dry box, Ni(COD)2(0.387 g, 1.41 mmol), 2,2′-bipyridyl (0.220 g, 1.41 mmol), COD (0.152 g, 1.41 mmol) and anhydrous DMF (16 ml) were added to a long-neck round bottom flask. [00251] 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) (1.00, 0.696) was weighed into a 40 ml vial and dissolved in anhydrous DMF (8 ml). The flask was sealed with a septum and the vial was closed with a septum screw cap. The catalyst mixture and the monomer solution were transferred out of the dry box and were placed under static argon. The reaction flask was heated to 70° C. for 45 min. The monomer solution was then was quickly transferred from the vial to the catalyst mixture flask with an argon flushed syringe. The reaction mixture was then heated to 70° C. for 6 h. The reaction mixture was cooled and solvent removed by rotary evaporation. The resultant black residue was re-dissolved in 20% EtOH (80 mL) and centrifuged at 2400 rpm for 12 hours. The supernatant was then decanted and filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until GPC analysis of retentate indicated the absence of low molecular weight material. The solvent was then removed under vacuum to give poly [2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene] (B) as a viscous oil (0.700 g, 79%) Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=62,000, Mw=127,000, Mp=93,000, D=2.0). Step 2: End Capping: End Capping is Performed in a Manner Similar to Example 22, Step 2 Step 3: Amine Activation: Amine Activation is Performed in a Manner Similar to Example 22, Step 3 Example 25. Synthesis of a Tandem Polymer with Two Different Linkers Step 1: Polymerization In a dry box, Ni(COD)2 (0.765 g, 2.78 mmol), 2,2′-bipyridyl (0.435 g, 2.78 mmol), COD (0.301 g, 2.78 mmol) and anhydrous DMF (20 ml) were added to a long-neck round bottom flask. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) (1.80, 1.26 mmol) and tert-butyl 4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butylcarbamate (B) (0.071 g, 0.126 mmol) were added to a 40 ml vial and dissolved in anhydrous DMF (30 ml). The flask was sealed with a septum and the vial was closed with a septum screw cap. The catalyst mixture and the monomer solution were transferred out of the dry box and were placed under static argon. The reaction flask was heated to 70° C. for 45 min. The monomer solution was then was quickly transferred from the vial to the catalyst mixture flask with an argon flushed syringe. The reaction mixture was then heated to 70° C. for 6 h. The reaction mixture was cooled and solvent removed by rotary evaporation. The resultant black residue was re-dissolved in 20% EtOH (80 mL) and centrifuged at 2400 rpm for 12 hours. The supernatant was then decanted and filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until GPC analysis of retentate indicated the absence of low molecular weight material. The solvent was then removed under vacuum to give 2,7-dibromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)] (C) as a viscous oil (1.3 g, 45%) Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=72,000, Mw=156,000, Mp=138,000, D=2.1). Step 2: End Capping A solution of K2CO3 in water (2M, 4 mL) was added to a stirred mixture of 2,7-dibromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)] (C) (800 mg, 0.67 mmol), 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid (D) (120 mg, 0.41 mmol), and DMF (6 mL) in a round bottom flask. This mixture was degassed with argon for 15 min. Palladium tetrakis(triphenylphosphine) (50 mg, 6 mol %) was added to the mixture and the flask was attached to a reflux condenser. The reaction vessel was degassed via 3 freeze-pump-thaw cycles and then heated to 80° C. for 12 h. The reaction mixture was cooled to 23° C. and concentrated in vacuo to a volume of 2 mL. The crude reaction mixture was transferred to an Erlenmeyer flask and diluted with 20% EtOH/H2O (75 mL). EDTA (300 mg, 2.00 mmol) was added to the mixture and stirred at 23° C. for 1 h. The mixture was filtered through a glass fiber filter paper and the filter paper rinsed with 20% EtOH/H2O. The resulting filtrate was then filtered through a 0.45 um cup filter. The filtered reaction mixture was purified and size fractionated using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until conductivity of the filtrate measured less than 0.01 mS/cm. The solvent was then removed under vacuum to give 4-(4-(2-bromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)])phenyl)butanoic acid (E) as a yellow oil (660 mg, 82%). Step 3: Linker Deprotection Trifluoroacetic acid (4 mL) was added dropwise to a stirred solution of 4-(4-(2-bromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)])phenyl)butanoic acid (E) (200 mg, 0.169 mmol) and dichloromethane (16 mL) in a round bottom flask. The reaction mixture was stirred at room temperature for 2 hours and then concentrated in vacuo. The residue was redissolved in minimal 20% EtOH and 1M HCl was added to the solution until pH=7. The neutralized solution was then desalted over G25 gel and the resultant material was concentrated to dryness to yield a clear pale yellow oil (F). Examples of dye incorporation, linker activation and bioconjugation are contained in further Example 38 and related examples. Example 26: Synthesis of a Tandem Polymer with Two Different Linkers Using End Capping Units to Regulate the Polymerization Reaction Step 1: Yamamoto Polymerization In a dry box, Ni(COD)2 (0.433 g, 8.40 mmol), 2,2′-bipyridyl (0.246 g, 8.40 mmol), COD (0.170 g, 8.40 mmol) and anhydrous DMF (15 ml) were added to a long-neck round bottom flask. 2,7-dibromo-9,9-di(2′,5′,8′,11′,14′,17′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)fluorene (A) (1.00, 0.696 mmol), tert-butyl 4-(2,7-dibromo-9-methyl-9H-fluoren-9-yl)butylcarbamate (B) (0.037 g, 0.069 mmol), and tert-butyl 4-(4-bromophenyl)butanoate (C) (0.004 g, 0.007 mmol) were added to a 40 ml vial and dissolved in anhydrous DMF (10 ml). The flask was sealed with a septum and the vial was closed with a septum screw cap. The catalyst mixture and the monomer solution were transferred out of the dry box and were placed under static argon. The reaction flask was heated to 70° C. for 45 min. The monomer solution was then was quickly transferred from the vial to the catalyst mixture flask with an argon flushed syringe. The reaction mixture was then heated to 70° C. for 6 h. The reaction mixture was cooled and solvent removed by rotary evaporation. The resultant black residue was re-dissolved in 20% EtOH (80 mL) and centrifuged at 2400 rpm for 12 hours. The supernatant was then decanted and filtered through a 0.45 um cup filter. The filtered reaction mixture was purified using tangential flow filtration (TFF) and was diafiltered into 20% ethanol using a 10,000 molecular weight cutoff membrane (polyethersulfone Prep/Scale TFF cartridge system, Millipore, Billerica, Mass.) until GPC analysis of retentate indicated the absence of low molecular weight material. The solvent was then removed under vacuum to give tert-butyl 4-(4-(2-bromo-poly-[2,7{9,9-bis(2,5,8,11,14,17,20,23,26,29,32,35-dodecaoxaoctatriacontane)fluorene-co-2,7-(9-methyl-9′-(butyl-4-t-butylcarbamate)fluorene)])phenyl)butanoate (D) as a viscous oil (664 g, 80%). Molecular weight determined by GPC analysis relative to polystyrene standards (Mn=50,000, Mw=88,000, Mp=174,000, D=1.8). Step 2: Linker Deprotection Trifluoroacetic acid (6 mL) was added dropwise to a stirred solution of Polymer (300 mg, X mmol) and dichloromethane (24 mL) in a round bottom flask. The reaction mixture was stirred at room temperature for 2 hours and then concentrated in vacuo. The residue was redissolved in minimal 20% EtOH and 1M HCl was added to the solution until pH=7. The neutralized solution was then desalted over G25 gel and the resultant material was concentrated to dryness to yield a clear pale orange oil (261 mg, 87%). Examples of dye incorporation, linker activation and bioconjugation are contained in further Example 38 and related examples. Example 27. Dual Functional Asymmetric Polymer with Both Internal and Terminal Conjugation Sites Used to Create a Polymer-Dye Label for Biomolecule or Substrate Conjugation Suzuki polymerization of 2-bromo-9,9-di(2′,5′,8′,11′,14′,17′,20′,23′,26′,29′,32′,35′-dodecaoxaoctatriacontan-38′-yl)-′7-(4″,4″,5″,5″-tetramethyl-1″,3″,2″-dioxaborolan-2-yl)fluorene is performed under those conditions described in Example 23 where y % is the mol % of the end linker used to regulate the polymerization and ensure high incorporation of linker. The linker in this example is 4-(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)butanoic acid. In this example, x mol % of the internal linker is also added to the polymerization to incorporate the second linking site into the polymer. This method for incorporating the internal linker is generally described in Examples 21, 25 and 26. The internal linker must be incorporated during the polymerization as indicated, however, it is expected that it would be possible to add the terminal linker as a separate step as described in Examples 9, 10, 11 and 21. Example 28: Enrichment of Linker-Functionalized Polymers The synthesis of linker-functionalized polymers can yield a mixture of chains with and without linker functionalities. Because conjugation efficiency is expected to improve with higher purity polymers for conjugation, the methods described in this example address this by enriching for chains containing linker. For a polymer batch containing a mixture of a COOH-modified and unmodified polymer: Dissolve polymer in 95% EtOH, then dilute with water to a final EtOH concentration of 20%. Desalt the polymer using 10 kDa MWCO filter until conductance is <0.1 mS/cm. Inject onto Q-Sepharose column, ensuring that the polymer load is suitable for the column capacity. Pass 20% EtOH in water over column to wash out unbound polymer. Release bound material by changing the eluting buffer to 1M NaCl in 20% EtOH in water for two column volumes to trigger the release of the bound polymeric material. Collect enriched material. The polymer is passed over a strong anion exchanger such as a Q-Sepharose column. Polymer chains bearing a functional carboxylic acid group will bind the strong anion exchanger, and polymer that is not functionalized will not bind and instead will wash through. After the non-functionalized polymer has passed through the column, the column is washed with 1M NaCl, which triggers the release of the acid-functionalized polymer by screening the acid group from the media. By using this method, the percent functional polymer has been shown to increase from 25% of polymer chains bearing a carboxylic acid group to >80% of polymer chains bearing a carboxylic acid group. This increase in functional chains has been shown by analyzing the absorbance ratios of polymer-dye conjugates pre- and post-enrichment. This procedure is also described in Example 38. A similar process has been validated for the enrichment of amine containing polymers. In that case an anionic exchange resin, SP Sephrose (or similar), is loaded at reduced conductivity (below 0.01 mS/cm). Example 29: Preparation of Polymer-Streptavidin Conjugates Via NHS/Amine Coupling Example 29a: Polymer Modifications Polymer Modification—Carboxylic Acid to Amine Conversion 1.35 g of a carboxylic acid terminated polymer was dissolved at in 9 mL ethanol, then added dropwise to 80 mL of 4° C. 50 mM MES, pH 5 while stirring. 0.52 g N-hydroxy succinimide was added in one portion. Once the N-hydroxy succinimide had dissolved, 2.3 g N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride was added in portions. After stirring the solution for 30 minutes, 2.8 mL of ethylene diamine was added dropwise. The solution was stirred overnight at room temperature and purified by tangential flow filtration (MWCO=10 kDa). 1.22 g yield (90%). Polymer Modification—Amine to Carboxylic Acid Conversion 70 mg of an amine-terminated polymer was dissolved in 7 mL DMSO. 2.3 mg DIPEA was added to the polymer solution. 2.2 mg DMAP was dissolved in 220 μL DMSO and added to the resulting polymer solution. 5.5 mg succinic anhydride was dissolved in 550 μL DMSO and added to the resulting polymer solution. The solution was agitated at room temperature overnight. The reaction was then purified over Amicon Ultra centrifugal filtration units (MWCO=10 kDa) with 25 mM MES pH 5 buffer. 62 mg yield (89%). Polymer Modification—Carboxylic Acid to NETS-Ester Conversion 60 mg of a carboxylic acid-terminated polymer was dissolved in 600 μL acetonitrile. 1.2 μg DIPEA was added to the polymer solution. 2.8 mg N,N,N′,N′-Tetramethyl-O—(N-succinimidyl)uronium was dissolved in 370 μL acetonitrile and added to the polymer solution. The solution was agitated at room temperature for 15 minutes. After the reaction is complete, the solvent was evaporated under reduced pressure. 50 mg yield (83%). Example 29b: Protein-Polymer Conjugation Streptavidin protein is dissolved in 50 mM NaHCO3 pH 8.2 buffer to make a 1 mg/mL solution. Crude activated polymer (10-15 eq or as required) solution from Step 2 is added to the aqueous streptavidin protein solution; the protein concentration is adjust with buffer to ensure that the volume of organic solvent added is <10% of the total volume, if necessary. The solution is agitated at room temperature for 3 hr and the reaction transferred to a Amicon Ultra filter (MWCO=10 kDa) to remove DMF. The protein is recovered into the initial volume with 25 mM PO4 pH 6.5 buffer. Purification of the Protein-Polymer Conjugate A 1 mL HiTrap SP Sepharose FF column is equilibrated with 20 mM Na Citrate pH 3 buffer. 1 mL (0.3-1 mg/mL) of Streptavidin-polymer conjugate is loaded in 25 mM NaHPO4 pH 6.5. The sample is wash through column with 20 mM Na Citrate pH 3 buffer until a stable baseline is obtained. Multiple 1 mL aliquots of sample may subsequently be loaded and washed. The column is washed with a minimum of 10 column volumes of 20 mM Na Citrate pH 3 buffer. The conjugate is eluted with 10 column volumes of 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer and the column is stripped with 10 column volumes of 20% ethanol in the elution buffer. The elution peak is concentrated with an Amicon Ultra filter (MWCO=10 kDa) to reduce the volume to ˜200 μl. A 10×300 mm Superose 12 column is equilibrated with 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer. 200 μL of concentrated Streptavidin-polymer conjugate is loaded and eluted with 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer. Fractions are pooled and buffer exchanged into PBS+0.05% NaN3 using Amicon Ultra Centrifugation filters (10 kD MWCO). Elutions are concentrated to desired concentration for testing; at around 2 μM Streptavidin. Characterization of a Purified Protein-Polymer Conjugate A 4-20% acrylamide Tris-HCl Ready Gel (BioRad) is prepared and the gel is loaded with the conjugate along with free streptavidin and free polymer in separate lanes. Gel electrophoresis is performed in 25 mM Tris 192 mM, Glycine pH 8.3 and stained with Coomassie to visualize the protein. The gel is stained for 30 minutes then destained with commercial destain overnight. Agarose gel conditions were also used to characterize polymer-streptavidin conjugates, an example which is shown in FIG. 29. In alternative embodiments, the above example can be adapted to allow for conjugation of the polymer to biomolecules or dyes, including but not limited to, antibodies and nucleic acids. The amine on the polymer is converted to a maleimide and a carboxylic acid (further activated to form the NHS ester) using alternative crosslinkers or modifiers. In certain embodiments, conjugation of the same polymer to other biomolecules (streptavidin, antibody fragments, nucleic acids) is facilitated using maleimide-thiol chemistry (using SATA linkers to convert free amines on the biomolecule or TCEP (or DPP) reduction of an antibody to create free thiols). Example 30: Preparation of Polymer-Streptavidin Conjugates Via Hydrazide/Benzaldehyde Coupling Step 1: Streptavidin-4FB Modification Streptavidin protein is reconstituted at 1.7 mg/mL and exchange into reaction buffer, 50 mM NaHCO3, pH 8. 15 molar equivalents of bifunctional benzaldehyde/succinimidyl linker, S-4FB (Solulink, San Diego, Calif.) 20 mg/mL in anhydrous DMSO is added to streptavidin, ensuring that the organic phase is less than 10% of the total volume. Reaction is mixed on shaker for 4 hours at room temperature and unreacted linker is subsequently filtered away via Amicon Ultra filter, 10 kD MWCO with 50 mM MES buffer, pH 5; centrifuged at 2400 rpm and a repeated wash ×3. Streptavidin protein is recovered in its initial volume, targeting 1.7 mg/mL in conjugation buffer, 50 mM NaPO4, pH 6.5. Step 2: Polymer Modification Polymer with terminal amine group (1 molar eq) is dissolved with DMF to make a 10 mg/mL solution. 20 molar equivalents of a bifunctional hydrazine/succinimidyl linker, SHTH (Solulink, San Diego, Calif.) at 80 mg/mL in anhydrous DMSO is added to the polymer solution. 1 drop of DIPEA is added to the reaction by a syringe and 22 g needle. The solution is agitated at room temperature for 4 hr and the reaction transferred to a Amicon Ultra filter (MWCO=10 kDa) filled with 25 mM MES pH 5 buffer. The solution is then centrifuged. The filter is refilled and washed with the following wash buffers: 1×DI H2O+1 drop 1 M HCl 1×DI H2O+1 drop 1M NaOH 3×50 mM MES, pH 5 Step 3: Protein-Polymer Conjugation 15 equivalents of modified polymer from Step 2 are added with desired amount of modified protein from Step 1. Aniline is added to the reaction for a final concentration of 10 mM and allowed to mix for 12 hours. The reaction is purified with Amicon Ultra filter (MWCO=10 kDa) to remove DMF and recovered with 25 mM PO4 pH 6.5 buffer. Step 4: Purification of the Protein-Polymer Conjugate A 1 mL HiTrap SP Sepharose FF column is equilibrated with 20 mM Na Citrate pH 3 buffer. 1 mL (0.3-1 mg/mL) of Streptavidin-polymer conjugate is loaded in 25 mM NaHPO4 pH 6.5. The sample is wash through column with 20 mM Na Citrate pH 3 buffer until a stable baseline is obtained. Multiple 1 mL aliquots of sample may subsequently be loaded and washed. The column is washed with a minimum of 10 column volumes of 20 mM Na Citrate pH 3 buffer. The conjugate is eluted with 10 column volumes of 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer and the column is stripped with 10 column volumes of 20% ethanol in the elution buffer. The elution peak is concentrated with an Amicon Ultra filter (MWCO=10 kDa) to reduce the volume to ˜200 μl. A 10×300 mm Superose 12 column is equilibrated with 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer. 200 μL of concentrated Streptavidin-polymer conjugate is loaded and eluted with 20 mM Na Citrate in 0.6 M NaCl pH 7.6 buffer. Fractions are pooled and buffer exchanged into PBS+0.05% NaN3 using Amicon Ultra Centrifugation filters (10 kD MWCO). Elutions are concentrated to desired concentration for testing; at around 2 μM Streptavidin. Step 5: Characterization of a Purified Protein-Polymer Conjugate A 4-20% acrylamide Tris-HCl Ready Gel (BioRad) is prepared and the gel is loaded with the conjugate along with free streptavidin and free polymer in separate lanes. Gel electrophoresis is performed in 25 mM Tris 192 mM, Glycine pH 8.3 and stained with Coomassie to visualize the protein. The gel is stained for 30 minutes then destained with commercial destain overnight. FIG. 14 top, depicts conjugation of streptavidin to a polymer of formula (Vb) in cartoon format. FIG. 14, bottom, is a Coomassie stain of acrylamide gel which depicts the mobility of the conjugate is retarded relative to the free protein indicating an increase in mass. A neutral polymer alone shows no evidence of staining and without a formal charge, the polymer is not mobile in the electrophoretic field. In alternative embodiments, the above example can be adapted to allow for conjugation of the polymer to biomolecules or dyes, including but not limited to, antibodies and nucleic acids. The amine on the polymer is converted to a maleimide and a carboxylic acid (further activated to form the NHS ester) using alternative crosslinkers or modifiers. In certain embodiments, conjugation of the same polymer to other biomolecules (streptavidin, antibody fragments, nucleic acids) is facilitated using maleimide-thiol chemistry (using SATA linkers to convert free amines on the biomolecule or TCEP reduction of an antibody to create free thiols) and NETS-amine chemistry (reacting the NETS polymer directly with lysines on the protein or nucleic acid). Example 31: Preparation of Biotin-Labeled Polymers Amine functionalized polymer of formula (Vc) is dissolved at 10 mg/mL in anhydrous DMF and divided into two portions. NHS-biotin (0.9 mg in 90 μL, 88 equivalents) (Pierce, 20217) and NHS-LC-LC-biotin (Pierce, 21343) at 10 mg/mL (1.5 mg in 150 μL, 88 equivalents) are dissolved in anhydrous DMF. The NHS-biotin and NHS-LC-LC-biotin solutions are immediately added to the two portions of polymer solution and allowed to mix on a shaker overnight in the dark. Excess reactant is removed by washing the solution using Amicon Ultra-4 mL 10 kD MWCO filter cartridges in a series of wash steps: First, the cartridge is first filled approximately halfway with water, and the reaction solution (by pipet) subsequently added directly into the water. Next, the cartridge is filled with water until it is full. The solution is mixed by pipetting up and down. Then, the cartridge is centrifuged at 2400 rpm for 30 minutes, or until the volume is reduced to 250 μL. The cartridge is then refilled with water 1 drop of 1M HCl is added; the solution is mixed, and centrifuged at 2400 rpm for 30 minutes, or until the volume was reduced to 250 μL. Next, the cartridge is refilled with water, 1 drop of 1M NaOH is added; the solution is mixed, and centrifuged at 2400 rpm for 30 minutes, or until the volume is reduced to 250 μL. The cartridge is then refilled with water, mixed and centrifuged at 2400 rpm for 30 minutes, or until the volume is reduced to 250 μL. This final step is repeated for a total of 5 washes. Characterization of a Purified Biotin-Labeled Polymer Excess biotin-labeled polymer is incubated with a Cy5-labeled streptavidin in DPBS buffer plus 0.2% BSA and 0.05% NaN3. A 0.8% agarose gel is prepared and the gel is loaded with the conjugate along with free Cy5-streptavidin and free biotinylated polymer in separate lanes. Gel electrophoresis is performed in 10 mM NaHCO3 pH10 and visualized using a Typhoon gel imager with 457 nm and 635 nm laser excitation. FIG. 15 (bottom) depicts retardation of mobility of the polymer-streptavidin complex relative to the free protein indicating an increase in mass. The polymer alone shows little mobility on its own due to a lack of formal charge. This protocol is adapted to successfully biotin-modify a range of conjugated polymers containing both internal and terminal amine linkers. Example 32: Functional Testing of Covalent Polymer Streptavidin Conjugates by Selective Binding to Biotinylated Microspheres Materials Required: 1×TBST: 50 mM Tris-HCl, 150 mM NaCl, 0.1% Tween20, pH 7.5; Biotin microspheres (10 mg/mL in TBST); BSA (1 mg/mL); AvDN (220 μM); and Polymer-Strepavidin (SA) conjugate: (1 μM with regard to SA, provided at 5 μM). Preparation of Master Mixes: Prepare in labelled 1.5 mL microfuge tubes: Experimental Negative control master mix master mix 14 μl TBST 9 μl TBST 6 μl BSA stock 6 μl BSA stock 5 μl bead stock 5 μl avidin stock 5 μl bead stock Briefly vortex both tubes and allow 20-30 minutes to pre-incubate the negative control beads with excess avidin before proceeding. A variable speed orbital mixer at 800 RPM for incubation is suggested to keep beads from settling. Bead Hybridization: Pipette 10 μL of each master mix into separate labelled 1.5 ml microfuge tubes. Add 2 μL of polymer-SA conjugate to each. Prepare additional tube containing 10 μL master mix and no polymer to be used as a blank. Briefly vortex and pulse spin all tubes. Transfer to variable speed orbital mixer and incubate for 30 mins at 800 RPM. Bead Processing/Washing: Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 480 μl supernatant being diligent not to disturb bead pellet. Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 500 μl supernatant being diligent not to disturb bead pellet. Repeat steps 3 and 4. Remove as much of remaining supernatant as possible using P200 pipette without disturbing bead pellet. Add 100 μL TBST and vortex briefly to re-suspend beads. Bead Measurement: Transfer 100 μL of positive, negative and blank beads to a BLACK 96 well plate. Excite wells at 430 nm and collect emission in the range 450-650 nm using required slit widths and/or sensitivity setting to achieve measurable signals above background. Compare emission of positive and negative control beads. FIG. 16 shows the polymer streptavidin conjugate was bound to a biotinylated microsphere. Excitation at 440 nm in a fluorometer resulted in emission from the polymer as indicated by the solid curve. The dashed curve represents the negative control where the biotin bead was first treated with excess avidin to block the biotin binding sites prior to treatment with the polymer streptavidin conjugate. Example 33: Functional Testing of Covalent Polymer Streptavidin Conjugates by Selective Binding to Biotinylated Microspheres and FRET to Dye Acceptors on Co-Localized Streptavidin-Dye Conjugates Materials Required: 1×TBST: 50 mM Tris-HCl, 150 mM NaCl, 0.1% Tween20, pH 7.5. Biotin microspheres (10 mg/mL in TBST). Cy3-SA (1 μM or 50 μg/mL). Polymer-Strepavidin (SA) conjugate: (1 μM with regard to SA, provided at 5 μM).. Bead Preparation and Hybridization: Prepare in labelled 1.5 mL microfuge tubes: Blank control Cy3-SA control FRET-SA Control 16 μl TBST 14 μl TBST 14 μl TBST 4 μl bead stock 2 μl Cy3-SA stock 2 μl Cy3-SA stock 4 μl bead stock 2 μl polymer-SA stock 4 μl bead stock Briefly vortex all tubes and transfer to variable speed orbital mixer for incubation of at least 30 mins at 800 RPM. Bead Processing/Washing: Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 48 μl supernatant being diligent not to disturb bead pellet. Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 500 μL supernatant being diligent not to disturb bead pellet. Repeat steps 3 and 4. Remove as much of remaining supernatant as possible using P200 pipette without disturbing bead pellet. Add 100 TBST and vortex briefly to re-suspend beads. Bead Measurement: Transfer 100 μL of all samples to a BLACK 96 well plate. Excite wells at 430 nm and collect emission in the range 450-650 nm using required slit widths and/or sensitivity setting to achieve measurable signals above background. Detect and record polymer emission in the range of 480-500 nm and Cy3 emission at the expected 570 nm. FIG. 17 shows the polymer streptavidin conjugate was bound to a biotinylated microsphere. Excitation at 440 nm in a fluorometer resulted in energy transfer between the polymer and a Cy3 dye conjugated to a different streptavidin protein as indicated by the solid upper curve. The dashed curve shows beads alone and the lower solid curve direct excitation of the Cy3-streptavidin conjugate at 440 nm. Example 34: Functional Testing of Biotin-Labeled Polymers by Selective Binding to Avidin Coated Microspheres Materials Required: 1×TBST: 50 mM Tris-HCl, 150 mM NaCl, 0.1% Tween20, pH 7. SA microspheres (10 mg/mL in TBST). Biotin (1 mM). 440 nm biotin-polymer conjugate: (46 μM). Bead Preparation and Hybridization: Prepare in labelled 1.5 mL microfuge tubes: Blank control Negative control Positive Control 16 μl TBST 11 μl TBST 15 μl TBST 4 μl bead stock 4 μl biotin stock 4 μl bead stock 4 μl bead stock Briefly vortex all tubes and transfer to variable speed orbital mixer for incubation of 20-30 mins at 800 RPM to ensure biotin has blocked all SA sites on negative control beads. Add 1 uL of polymer-biotin stock to both positive and negative control tubes. Vortex briefly and transfer to variable speed orbital mixer and incubate for 30 mins at 800 RPM. Bead Processing/Washing: Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 480 μL supernatant being diligent not to disturb bead pellet. Add 0.5 ml TBST to all samples and controls and vortex briefly. Centrifuge at 1200 g for 2 min and remove 500 μl supernatant being diligent not to disturb bead pellet. Repeat steps 3 and 4. Remove as much of remaining supernatant as possible using P200 pipette without disturbing bead pellet. Add 100 μL TBST and vortex briefly to re-suspend beads. Bead Measurement: Transfer 100 μL of all samples to a BLACK 96 well plate. Excite wells at 430 nm and collect emission in the range 450-650 nm using required slit widths and/or sensitivity setting to achieve measurable signals above background. Compare emission of positive and negative control beads. FIG. 18 shows the biotin modified polymer was bound to a streptavidin microsphere (top). In FIG. 18 (bottom), excitation at 440 nm in a fluorometer resulted in emission from the polymer as indicated by the solid upper curve. The lower solid curve represents the negative control where the streptavidin bead was first treated with excess biotin to block the binding sites prior to treatment with the biotinylated polymer. The lower solid curve represents beads alone. Example 35: Selective Binding of Biotin-Labeled Polymer to Dye-Labeled SA Conjugates to Validate FRET Properties and Functional Activity of the Polymer Modification Materials Required: Biotin-Polymer Conjugate: (46 Cy3-SA conjugate (1 mg/mL or 18.9 μM). BLACK 96-well plate. Forming the Biotin-Streptavidin Complex: In a 1.5 mL microfuge tube, combine 9.4 μL of the biotin-polymer conjugate and 2.9 μL of the Cy3-SA. Vortex to mix, then incubate on a shaker (under foil) for 0.5 h. Longer incubation times are also suitable. Instrument Settings: Model experiments were conducted on a BioTek Synergy 4 in the Fluorescence mode with the following settings: Emission: 400-750 nm in 5 nm steps and Sensitivity level: 50. Plate Layout: Prepare solutions in a BLACK 96-well plate as in the below table. Take care to add the A+B solution last, after all other materials have been added: Material Well 1 Well 2 Well 3 Polymer-biotin 9.4 μL* 9.4 μL — Cy3-SA 2.9 μL* — 2.9 μL Buffer 100 μL 100 μL 100 μL *Pre-incubated in the first step, Forming the Biotin-Streptavidin Complex. FIG. 19 shows the biotin modified polymer was bound to a dye labeled streptavidin (Cy3 or Texas Red—top). Excitation at 440 nm in a fluorometer resulted in emission from the dye acceptors at their respective emission wavelength (approximately 570 nm and 620 nm respectively—bottom left) as well as some residual emission from the polymer (approximately 520 nm). A titration was also performed to saturate the binding of polymer to the streptavidin (bottom right). The solid curve indicates the emission from the Cy3 label on the streptavidin via energy transfer from the polymer at 440 nm excitation. The dotted curve represents the negative control where the streptavidin was first treated with excess biotin to block the binding sites prior to treatment with the biotinylated polymer. Example 36: Polymer-Streptavidin Conjugates for Use in Flow Cytometry Polymer bioconjugates are evaluated by Stain Index, as defined by Becton Dickinson (BD) Biosciences on a flow cytometer. See, e.g., H. Maeker and J. Trotter, BD Biosciences Application Note: “Selecting Reagents for Multicolour Flow Cytometry”, September 2009. The stain index reports a measure of the polymer's brightness, nonspecific binding and can also be related by the Resolution Index on a flow cytometer. Flow cytometry provides a method through which to measure cells of a specific phenotype or analytes of interest on specific microspheres. This can be done with direct labeling of a primary antibody or, if signal amplification is desired, through a secondary antibody or the avidin-biotin complexation with avidin-polymer conjugates. Procedure for Cell Staining Cells of interest are taken up in sufficient quantity, at least 105 per test condition. Cells are then spun down at 250 rcf for 3 minutes, washed in DPBS+0.2% BSA and 0.05% NaN3 (staining buffer), then resuspended in staining buffer at 1×107 cells/mL. For primary incubation, cells are incubated with a primary conjugate (reporter labeled antibody) specific to an antigen of interest, negative cells serve as a negative non-specific binding reference. A control population or an established commercial conjugate is used as a positive control. Primary polymer conjugates are incubated at 4° C. with 4×105 cell aliquots at concentrations with volume dilutions from 10-330 nM for 30 minutes. Following primary incubation, cells are rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse is repeated three times. Cells are resuspended for testing at 8×105 cells/mL in DPBS+0.2% BSA, 0.05% NaN3. For secondary antibody labeling, an unlabeled primary antibody to the antigen of interest is incubated at 0.4 ug/uL, or other titrated amount, at 4° C. with 4×105 cells per test condition for 30 min. Following primary incubation, cells are rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse is repeated three times. Species reactive secondary polymer conjugates are incubated at 4° C. with 4×105 cell aliquots at concentrations with volume dilutions from 10-330 nM for 30 minutes. Following secondary incubation, cells are rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse is repeated three times. Cells are resuspended for testing at 8×105 cells/mL in DPBS+0.2% BSA, 0.05% NaN3. For streptavidin-polymer conjugate labeling, cells are incubated with a biotinylated primary antibody to the marker of interest, as detailed above for the secondary antibody labeling, instead of an unlabeled primary. Following the primary washing, cells are resuspended and divided in 4×105 cell aliquots and incubated with streptavidin-polymer conjugates at 1-100 nM volume dilutions for 30 minutes at 4° C. Following secondary incubation, cells are rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse is repeated three times. Cells are resuspended for testing at 8×105 cells/mL in DPBS+0.2% BSA, 0.05% NaN3. If further signal amplification is desired, cells and be incubated with an unlabeled primary antibody and then subsequently follow with a species reactive biotinylated secondary antibody prior to incubation with streptavidin conjugates. The incubation steps, washing protocol and testing protocol should follow as previously detailed. These flow testing procedures have been developed specific to CD4 markers on Cyto-trol cells. Cell preparation and incubation protocols may vary with cell type and an optimal staining, washing and handling protocol should be developed specific to cell type. Working concentration ranges of antibodies have been identified as optimal for both CD4 (35-50% population) and CD45 (85% population) markers on Cyto-trol control lymphocytes as well as on Whole Lysed Blood (for primary antibody only). Markers which have populations significantly different than these ranges may fall outside of the suggested titration ranges. Testing was also done on a Jurkat cell line grown in culture following similar protocols. In these tests a CD45 marker was used. As there are no negative cell populations a different negative control procedure was used. In the negative control samples the primary antibody was omitted from the primary incubation step. This step and all subsequent steps were performed according to the standard protocol. Again a commercially dye-antibody or dye-strepatvidin conjugate were used as a positive control. Procedure for Flow Cytometry Analysis Flow testing was done in test tubes, at 0.5 mL volumes on a BD LSR II Flow Cytometer. Flow testing is performed using the voltage settings determined from daily calibration of the cytometer with calibration particles by flow facility staff. Lymphocyte specific gating by forward scatter vs. side scatter is performed on unstained cell samples as a background control. Standard doublet gating is performed for both forward scatter and side scatter area vs. width profiles. With only a single color, no compensation is required. Data are collected for all forward and side scatter parameters and fluorescence measurements are made using BD's standard Pacific Blue channel. Pacific Blue data utilizes excitation with the 408 nm Violet lasers and a 450/50 BP filter. Samples are collected for 30,000 events within the stated gating parameters. Representative Experiments: CD4 marking was measured on Cyto-trol cells, lyophilized human lymphocytes for analysis of polymer performance in flow. Cyto-trol cells (Beckman Coulter) were reconstituted in the provided reconstitution buffer and allowed to swell for 15 minutes at room temperature. Cells were then spun down at 250 rcf for 3 minutes, washed in DPBS+0.2% BSA and 0.05% NaN3 (staining/testing buffer), then resuspended in staining buffer at 1×107 cells/mL. Cell suspension was divided in two; half the cells were incubated with biotinylated anti-CD4 at 0.4 ug/uL, the other half of the cells were incubated with staining buffer as a negative control for 30 min. Following primary incubation, cells were rinsed with 5 volumes staining buffer and spun down at 250 rcf for 3 minutes; this rinse was repeated three times. Cells were resuspended at prior volume in staining buffer. 4×105 cells were measured per test and divided out accordingly, streptavidin-fluorophore conjugates prepared in Example 19 were incubated at 100 nM with each aliquot of cells for 30 min, allowing the avidin-biotin complex to form. Following the secondary incubation, cells were rinsed and detailed previously. Final cell suspensions were made for testing at 8×105 cells/mL. Flow analysis was performed on a BD LSR II flow cytometer at The Scripps Research Institute (TSRI), San Diego, Calif. Routine calibration with Rainbow fluorescent particles for aligning fluorescent channels on the cytometer was performed by staff at TSRI, all calibrated voltages were used, per staff recommendation. All samples were excited with a 408 nm Violet laser, the polymer conjugate was measured in the AmCyan channel with a 525/50 filter. All samples were initially referenced to unstained cells. The polymer streptavidin conjugate from FIG. 14 showed specific secondary labeling of the primary identified CD4 positive cells, with the positive cells as 44% of the population. The polymer streptavidin conjugate demonstrated a positive stain index showed low non-specific binding with reference to unstained cells and its respective negative control (FIG. 20. (A)). This provides evidence that the polymer, although its peak absorbance is a 440 nm, is a viable fluorescent material for use in flow cytometry with Violet laser excitation. Secondary Antibody polymer conjugate on Cyto-trol cells Amine-functionalized 405 polymer was conjugated to goat anti-mouse IgG κ1 purified antibody by route of maleimide-thiol conjugation and TCEP partial reduction of the antibody. The polymer and conjugation procedure are provided specifically in Example 46. Conjugates were tested on Cyto-trol cells (Beckman Coulter), a fixed and lyophilized lymphocyte cell population for control testing of specific human antigens. Cell staining followed secondary cell staining protocol. Cells were incubated with and without (negative control) unlabeled anti-CD4 (RPA-T4 clone, BD Biosciences) raised in mouse against the human antigen. After complete washing of primary antibody incubation, cells were incubated with polymer labeled goat anti-mouse conjugates for specific labeling of primary identified CD4 positive cells. Secondary labeling occurs by Fc recognition and binding of the mouse primary antibody by the secondary goat IgG, raised against murine species. A positive control was used by incubation with commercially available Pacific Blue goat anti-mouse IgG (Invitrogen) as the secondary labeling species. FIG. 20 (B) depicts the specific recognition of CD4 specific cells by the secondary fluorescent conjugates. Unstained cells show a negative control and natural autofluorescence of the cells, and incubation of polymer conjugate on cells with no primary labeling show minimal non-specific binding of the conjugate to unlabeled cells. Positive control, Pacific Blue goat anti-mouse shows the commercially available standard for CD4 labeling by secondary antibody with Violet excitation. 405 polymer-goat anti-mouse conjugate (red) shows positive identification of CD4 positive cells, a minimal shift in the negative cell population and great fluorescent signal and resolution that Pacific Blue standard. FIG. 20 (C) depicts Streptavidin polymer conjugates on Jurkat cells. Conjugates were produced with the polymer provided in Example 11 using the protocol defined in Example 29. The stain index for the polymer streptavidin conjugate was over 10 fold higher than that obtained for the commercially available Pacific Blue streptavidin control conjugate. FIG. 20 (D) depicts a primary monoclonal antibody polymer (antiCD4, RPA-T4) conjugate evaluated on Cyto-trol cells using the protocols defined above. The conjugate was prepared using the polymers and protocols defined in Example 46. Additional details on the conjugation can also be found in Example 39. Example 37: Preparation of Polymer Conjugated to —COOH Beads Via EDC Coupling Materials (Per 100 μL of Beads) LodeStars —COOH functionalized magnetic beads (Varian, Inc. PL6727-0001) (100 μL of suspension at spec′ d 30 mg/mL). Polymer with amine terminal ends from Example 17 (125 μL at 1.6 μM in 25 mM MES pH 5, for a 10-fold excess over theoretical bead capacity). 10 mM NaOH (2 mL). DI H2O (3 mL). 25 mM cold MES, pH 5. EDC at 50 mg/mL in 25 mM cold MES, pH 5 (100 μL). NHS at 50 mg/mL in 25 mM cold MES, pH 5 (100 μL). 100 mM Tris/HCl pH 7.4 (1 mL). Centrifuge and black flat-bottom 96-well plate. Antibody capacity was given at 10 ug/mg bead, giving an amine coupling capacity of 2 nmol polymer/mL bead (at 30 mg/mL). A 10 fold-excess of polymer over the suggested capacity was used to target the antibody concentration given in Varian's protocol. Bead Washing Beads were washed collectively as 600 μL and then split into 6×100 μL samples for coupling. Beads were washed 2× with 1 mL 10 mM NaOH, then 3x with 1 mL DI H2O; in between washes, the tube was centrifuged 1 min at 3000 rpm to recollect the beads as a pellet, supernatant was discarded and beads were resuspended in the next wash. After the final wash, beads were resuspended in 600 μL cold 25 mM MES, pH 5 and aliquoted into 6×100 μL volumes in microcentrifuge tubes. Beads were centrifuged again 1 min at 3000 rpm and supernatant was discarded. EDC Activation 100 μL of the EDC solution was added to each reaction set. 100 μL of the NHS solution was added to each reaction set. Beads were resuspended by vortexing and then allowed to mix on a rotator for 30 minutes. Beads were washed 2x in cold 25 mM MES pH 5, pelleted by centrifuging for 1 min at 3000 rpm and the supernatant was discarded. Beads were resuspended in 125 μL cold 25 mM MES, pH 5. Polymer Coupling 125 μL of polymer at 1.6 μM was added. Samples were vortexed to mix thoroughly and then reacted at RT on a mixer for 3 hours. Beads were pelleted by centrifuging for 1 min at 3000 rpm; supernatant was discarded. Beads were resuspended in 1 mL 100 mM Tris/HCl to block unreacted —COOH sites, vortexed and mixed for 1 hour. Beads were recollected by centrifugation and resuspended in 100 μL 25 mM MES. At this point, the supernatant of several tubes were yellow in color and had significant absorbance at 440 nm; the beads were washed 6 times until absorbance was at baseline. Beads sat for an additional 2 days prior to fluorescence measurement, after sitting in solution for 2 days, the supernatant was again yellow in color and had measurable absorbance. Beads were washed 3 more times with 30 minute mixes in between until no absorbance was measurable. At 2 days following fluorescence measurements, the supernatant remained clear and free of measurable absorbance. Example 38: Preparation of Polymer-Dye Conjugates Example 38a: Preparation of Polymer-Dye Conjugate at Polymer Terminal 0.5 mg amine-terminated polymer was dissolved in 15 μL DMSO. The polymer solution was then exchanged into 50 mM NaHCO3/Na2CO3, pH 8 buffer and recovered in buffer at ˜5 mg/mL as determined by UV-VIS absorbance. 50 μg NETS-ester dye (DyLight 594) was dissolved at 10 mg/mL in anhydrous DMSO, which was then immediately added to 120 μg of polymer. The tube was mixed on shaker (600-800 rpm) for 1 h and subsequently diluted to 100 μL with 20% EtOH in water. The mixture was added to a 30 cm Superdex 200 SEC column in 0.6M NaCl and 20% EtOH to separate polymer-dye conjugate from unreacted dye. The addition of dye can be used to estimate the incorporation of linker on the polymer structure by measuring an absorbance ratio based on the relative extinction coefficients of the polymer and dye. Using the molecular weight of the polymer it is possible to estimate the number of polymer chains which contain a linker. In additional embodiments, polymers with a carboxylic acid side chain are modified with amine functional dyes using standard EDC conjugation procedures or by first converting to the NETS ester using the protocol similar to that described in Example 29. Thiol dyes conjugated to maleimide terminated polymers have also been demonstrated. Any range of chemistry pairs would be expected to work in similar fashion to conjugate a polymer and dye. Example 38b: Preparation of Polymer-Dye Conjugate at Internal Position In a glovebox, 100 mg polymer with internal amine functionalities was dissolved in 10 mL anhydrous DMSO in a 20 mL amber scintillation vial. 0.32 mL DIPEA was added to the polymer solution. 24 mg of NETS-ester dye (Cy3) was dissolved in 2.4 mL in anhydrous DMSO and added to the polymer solution. The vial was tightly sealed, then removed from the glovebox and stirred at room temperature for 48 hours. The reaction was then purified over Amicon Ultra centrifugal filtration units (MWCO=30 kDa) with 20% ethanol in water until all free dye was removed. Purity was verified by running a 0.15 mg sample over a 30 cm Superdex 200 SEC column in 0.6M NaCl and 20% ethanol. 90 mg yield (90%). The addition of dye can be used to estimate the incorporation of linker monomers in the polymer structure by measuring an absorbance ratio based on the relative extinction coefficients of the polymer and dye. For polymers described above, the ratio of linker monomers (or dye attachments) per fluorene monomer in the final polymer are in general agreement with the molar feed ratio of monomers used in the polymerization reaction. Polymers with a carboxylic acid side chain can also be modified with amine functional dyes using standard EDC conjugation procedures or by first converting to the NHS ester using the protocol similar to that described in Example 29. Analogous procedures can be used to conjugate a range of dyes including Cy3, DyLight 549, DyLight 633, FAM, FITC, Alexa633, Alexa647 and several others. Polymers with a carboxylic acid side chain can also be modified with amine functional dyes using standard EDC conjugation procedures. FIG. 21 (A) shows the polymer structure above conjugated to (from left to right) FITC, Cy3, DyLight 594 and DyLight633. The polymer alone is show for reference (far left). Note in each case the amount of residual donor (polymer) emission is minimal. The data highlight the capability of generating several diagnostic signals at different wavelengths for multiplex applications. In this embodiment a single light source is capable of generating five distinct emission wavelengths. Example 38c: Energy Transfer Evaluation for Polymer-Dye Conjugates Based on Polymer Excitation for Use in Polymer Tandem Conjugates FIG. 21 (B) depicts a comparison of the fluorescence of the dye (DyLight594) excited near its absorbance maximum (lower curve) and polymer-dye conjugate excited at 405 nm (upper curve). Dye emission around 620 nm was over 5 fold brighter from the polymer-dye conjugate at the same molar concentration of dye versus direct dye excitation. Such embodiments highlight the signal amplification afforded by the disclosed polymer donors in energy transfer processes. The picture in the upper left corner highlights the visual color change in the emission of the complex based on dye conjugation. The polymer solution emits blue in the absence of dye and red upon dye conjugation (post purification). FIG. 21 (C) compares the fluorescent signal of the base polymer (no dye, peak emission near 420 nm) to that of the polymer-dye conjugate (peak emission near 620 nm). The DyLight594 dye quenches >98% of the polymer emission when conjugated to the polymer above (Example 38b). This is a feature of the polymer materials as any remaining donor emission could manifest as background signal in multiplex assay formats. The ability to conjugate the dye directly to the polymer structure and vary the number of attachement sites provides for efficent transfer that can be regulated by chemical design. Example 39: Flow Testing of Monoclonal Antibody (antiCD4) Conjugates on Whole Lysed Blood Samples Polymer conjugates of primary antiCD4 antibody (RPA-T4 clone) were produced using 3 different conjugation routes as provided in Examples 45, 46 and 49. 1) Amine modified polymer converted to a maleimide reactive group using SMCC (maleimide/NHS crosslinker) reacted with thiol groups on the antibody introduced by reacting SATA (thiol/NHS cross linker) with lysine (amine) groups (CJ11-2, FIG. 22). 2) Same polymer modified with SMCC (malemide) but with thiol groups introduced on antibody using TCEP to partially reduce the disulfide linkages in the antibody (CJ13-2, FIG. 22 and FIG. 20D). 3) A carboxylic acid terminated polymer activated with TSTU to form the NHS ester was reacted directly with the lysine (amine) groups on the antibody (CJ04-2 FIG. 22). All conjugates were made from the same polymer structure and batch. The polymer was synthesized using the protocol depicted in Example 12 with an amine end capping unit in place of the carboxylic acid capping unit shown. The NHS/amine conjugation was done with the protocol described in Example 45. The maleimide/thiol conjugation reactions were done in lines with those protocols described in Examples 46 and 49. FIG. 22 depicts the performance of these conjugates in flow cytometry conduced as follows. 100 μl whole human blood from a healthy volunteer was aliquoted into FACS tubes (duplicates for each sample). Antibody conjugates were diluted in wash buffer (PBS with 0.5% BSA and 0.1% Sodium Azide) and added to the blood at specified concentrations. Samples were vortexed vigorously then incubated for 15-30 mins in the dark at room temperature. 2 ml of 1×BD FACS Lyse solution was added to each sample and mixed in by vigorous vortexing prior to a further 10 mins incubation in the dark at room temperature. Samples were centrifuged for 5 min at 500 g and the supernatant tipped off and discarded. Samples were vortexed and 3 ml of wash buffer (PBS with 0.5% BSA and 0.1% Sodium Azide) added. Centrifugation was repeated at 500 g for a further 5 min. The resulting supernatant was tipped off and discarded and the remaining cell pellet vortexed. Samples were run on a BD LSRII flow cytometer acquiring all violet channels equipped with a violet laser and 450/50 nm filter that had been set up and precalibrated against BD CST beads. All polymer conjugate samples (CJ04-2, CJ11-2 and CJ13-1 lines) showed minimal non specific binding compared to unstained cells. Further, all polymer conjugates produced significantly higher positive signals than a commercially available Pacific Blue control conjugate of the same antibody clone which is commonly used for flow cytometry at compatible wavelengths. The best performing conjugates from this set provided over 6 fold high stain index than the commercially available Pacific Blue control antibody. Example 40: Preparation of Polymer-Dye Conjugate The polymer is conjugated to a dye, Dylight 594, and purified in a manner similar to the methods as described in Example 36. FIG. 23 depicts a comparison of the florescence of the dye (DyLight594) and polymer-dye conjugate. The dye was excited at 594 nm and the polymer-dye conjugate at 380 nm. Example 41: Fluorescent Immunoassay (ELISA) with Streptavidin-Conjugated Polymer An immunoassay for human IgG was developed as a demonstrative system in 96 well plate format. In further embodiments, similar functionality would be equally applicable in other formats including suspended microspheres and protein chip microarrays. Step 1: Preparation of Reagents Wash concentrate was prepared by dissolving 79.2 g Tris base pre-set crystals (pH 7.7), 225 g sodium chloride and 0.5 g Thimerosol in 1000 mL deionised water. Wash solution was prepared by adding 100 mL wash concentrate to 2400 mL deionised water. Subsequently, 10 mL 10% Triton X-100 was added. The basic assay buffer was prepared by dissolving 14.8 g Tris base pre-set crystals (pH 7.7), 18 g sodium chloride and 0.5 g Thimerosol in 2000 mL Milli-Q water (conductivity 18.2 mΩcm). Subsequently, 2 mL 10% Tween 20 and 10 g Bovine Serum Albumin Fraction V, essentially gamma globulin free were added. The solution was filtered and stored at 4° C. Step 2: Preparation of Capture Antibody Coated Plates Capture antibody was coated onto the surface of Nunc white Maxisorp 96 well plates at a concentration of approximately 1 microgramme per well. The plates were sealed and stored overnight at 4° C. Subsequently, the plates were washed once with wash solution and tapped dry on absorbent paper. Unless otherwise stated all plate washing in this example was performed on an automated microtitre plate washer. Two hundred and fifty (250) microlitres of blocking buffer (0.1M PBS containing 2% BSA) were added to each well, the plates re-sealed and stored at 4° C. until use. Step 3: Immunoassay Capture antibody-coated microtitre plates were washed twice with wash solution and tapped dry on absorbent paper. Two hundred (200) μL of either assay standard or experimental unknown sample were added in quadruplicate to appropriate wells of the coated plate. The plates were incubated on a shaker for 2 hours at 18° C. Subsequently, the plates were washed three times with wash solution, tapped dry on absorbent paper, and 200 μL of biotinylated detection antibody at a previously determined optimal concentration (diluted in assay buffer and filtered before use) were added to each well. The plates were incubated on an orbital shaker at ambient temperature for a further 60 minutes. The plates were then washed three times and tapped dry on absorbent paper. Two hundred (200) μL of 0.2 micron syringe filtered Streptavidin-polymer conjugate as prepared in Example 30 diluted to a concentration previously determined as suitable in assay buffer. The polymer was a fluorene polymer with neutral PEG11 side chains and an amine conjugation site. The plates were incubated on an orbital shaker at ambient temperature for a further 2 hours. The plates were then washed six times, tapped dry, turned around 180o, and re-washed a further six times. The plates were again tapped dry on absorbent paper. Two hundred (200) μL of filtered release reagent (0.1M sodium hydroxide, 2% Triton X-100) were added using a multi-channel pipette, the plates shaken for 60 minutes at ambient temperature and the fluorescence measured with a Victor Fluorometer. The plate was then sealed, stored overnight at 4° C. and re-read in the Victor Fluorimeter the following morning. Fluorescence counts were analysed using the Multicalc Software from Perkin Elmer to determine lower limit of assay detection and assorted similar parameters. Alternative conditions were also evaluated to release the conjugate from the well plate surface to improve the fluorescent readout. A representative data set is shown in FIG. 24. Comparisons were also made to commercially available SA-dye conjugates. The polymer conjugates demonstrated superior detection limits relative to the dye conjugates as was expected due to the collective optical properties. Example 42: Synthesis, Conjugation and Application of Para-Phenylene Vinylene Co-Polymer with Active Functional Linker for Bioconjugation Poly(1,4-(di2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 2,5-dibromoterephthalate)-vinyl-alt-para(2-methoxy-5-2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl benzene)-vinylene) with phenylbutoxyamino termini. Di-2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 2,5-dibromoterephthalate (2.0 g, 1.52 mmol), 34-(4-methoxy-2,5-divinylphenoxy)-2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontane (1.11 g, 1.52 mmol), palladium acetate (13.6 mg, 0.061 mmol), tri-o-tolylphosphine (37 mg, 0.121 mmol), triethylamine (1 mL, 7.6 mmol) and 4 mL of DMF were combined in a small round bottom flask, equipped with a Teflon stribar, fitted with a needle valve and transferred to a Schlenk line. The solution was degassed via three freeze-pump-thaw cycles, put under nitrogen and heated to 100 C with constant stirring overnight. Next di-2,5,8,11,14,17,20,23,26,29,32-undecaoxatetratriacontan-34-yl 2,5-dibromoterephthalate (2.0 g, 1.52 mmol) (100 mg, 5 mol %), palladium acetate (5 mg), and tri-o-tolylphosphine and 0.5 mL DMF were combined in a small round bottom flask which is fitted with a needle valve and transferred to the Schlenk line. The solution was degassed via three cycles of freeze-pump-thaw and once warmed to room temperature was transferred to the polymerization reaction via cannula to exclude air and moisture. Allowed the mixture to react overnight. Next 4-(4-bromophenoxy)butan-1-amine (43 mg, 15 mol %) and 0.5 mL of DMF were combined in a small round bottom flask, equipped with a Teflon stribar, fitted with a needle valve and transferred to a Schlenk line. Once warmed to room temperature the solution was transferred to the polymerization reaction via cannula to exclude air and moisture. Allowed the mixture to react overnight. The next day the reaction was cooled to room temperature and the bulk of triethylamine was removed under vacuum. The reaction mixture was diluted with ˜30 mL of water and filtered through G 6 glass fiber filter paper. The filtrate was transferred to several Amicon filters (10 kDa cutoff) to concentrate the polymer and remove DMF. The remaining water is removed under vacuum and the residue is extracted into methylene chloride. The methylene chloride solution is dried over magnesium sulfate and filtered. The solvent is removed leaving behind a dark red thick oil, approximately 900 mg. The polymer was found to have a Mn of 20,400 g/mol as determined by GPC analysis relative to polystyrene standards. Incorporation of the amine linker was verified by conjugating a dye to the final polymer as described in Example 38. The polymer was then conjugated to streptavidin protein as follows: Amine polymer was dissolved at 50 mg/ml and desalted and buffer exchanged into 100 mM phosphate buffer pH 7.5. Polymer concentration was assessed by absorbance and 25 molar equivalents of SMCC (10 mg/ml in anhydrous DMSO) added. The reaction was mixed for 60 mins at room temperature and then desalted and buffer exchanged into PBS pH7.0+5 mM EDTA prior to repeat polymer concentration determination and confirmation of malemide functionality by SAMSA-fluorescein dye test. Streptavidin (5 mg/ml in 100 mM phosphate buffer pH7.5) was activated by addition of 20 molar equivalents of SATA (5 mg/ml in anhydrous DMSO). The reaction was mixed at room temperature for 60 mins prior to quenching (>15 mins room temp) with 10% (v/v) 50 mM EDTA, 2.5M hydroxylamine pH7.0. The activated protein was desalted and buffer exchanged into the same buffer as the activated polymer prior to an performance of an Ellman's assay to confirm and quantify thiol incorporation. Both the activated polymer and streptavidin were used as follows without delay. A greater than order of magnitude molar excess of SMCC activated polymer was added to the SATA activated streptavidin and the two mixed for 2 hours at room temperature prior to quenching with 20 molar equivalents of N-ethylmaleimide which was mixed in for 15 minutes at room temperature. Ion exchange and size exclusion chromatography were used to purify the bioconjugate of unreacted polymer and streptavidin. Appropriate fractions were pooled to maximize yield and performance and then concentrated by ultrafiltration. The conjugate was tested and its performance compared to a commercially available streptavidin-phycoerythrin (SA-PE) conjugate designed for purpose in a model Luminex xMap assay (FIG. 27, left). Donkey anti-mouse IgG antibody was covalently conjugated to xMap beads. A standard curve titration of Mouse IgG was then performed under standard Luminex xMap assay conditions (FIG. 27, right). Replicate samples were detected using either 4 μg/mL streptavidin-phycoerythrin or streptavidin conjugated polymer conjugate prepared as above (concentration not rigorously controlled). Samples were then read on a Luminex instrument. Absolute signals were found to be lower using the conjugated polymer. This is partially attributed to a non-ideal match between the polymer spectra and the excitation and emission optics in the instrument as well as the putative lower concentration of detection reagent used compared with the commercially available phycoerythrin product. However, the proportional background (non specific signal) from the polymer was also markedly lower resulting in a very comparable lower limit of detection for both detection formats (Fluorescence highest point in standard curve/fluorescence zero concentration of analyte (MFI/zero): 21.8 PE, 26.6 Polymer). Example 43: Synthesis of a Fluorene Co-Polymer with a DPP Band Gap Modifying Unit To a 25 mL round-bottomed flask were added: PEGylated dibromo-DPP monomer (110 mmol), PEGylated fluorene diboronicester (110 mmol), THF (2.4 mL) solvent, 2M K2CO3 (1.6 mL) and tetrakis(triphenylphosphine)palladium (3.3 mmol) catalyst. The mixture was degassed by three freeze-pump-thaw cycles and then stirred under argon at 80 C over night. The resulting mixture was allowed to r.t. and diluted with water. Polymer was collected after dichloromethane extraction. The resulting polymer was found to have an absorption maxima at 520 nm and emission maxima at 590 nm with quantum yield of 6% in water. The polymer had a MW estimated at 16,000 by GPC analysis relative to polystyrene standards and was soluble in water, methanol and dichloromethane. End linker incorporation can be performed using methods similar to those described above and including methods described in Examples 9, 10 and 11. Example 44: Synthesis of a Substituted Divinylbenzene Polymer Methods used to prepare the polymer above were similar to those provided in Example 38. General methods for the preparation of divinylbenzene polymers as disclosed herein may be derived from known reactions in the field as well as methods found herein, and the reactions may be modified by the use of appropriate reagents and conditions, as would be recognized by the skilled person, for the introduction of the various moieties found in the formulae as provided herein. Example 45: Conjugation of Polymer to an Amine on a Primary Antibody Procedure for Production of NHS Ester Polymer-Antibody Conjugate Primary monoclonal antibody, anti-CD4 (RPA-T4 clone) was desalted, and exchanged into 50 mM NaHCO3 buffer, pH 8.2 at 1 mg/mL. Enriched NHS functionalized polymer was dissolved into anhydrous dimethyl sulfoxide (DMSO) at 100 mg/mL. Polymer solution was added at 30 fold molar excess of antibody into the antibody solution and allowed to mix by agitation for 3 hours at RT. Protein concentration was adjusted with buffer prior to incubation to ensure the volume of organic solvent was <10% the total volume. Following ultrafiltration over a 10 KDa MWCO filter device, ion exchange and size exclusion chromatographic techniques were then used to purify the bioconjugate of unreacted polymer and antibody, respectively. Appropriate fractions were pooled to maximize yield and buffer exchanged into PBS+0.05% NaN3 and simultaneously concentrated by ultrafiltration as above. Degree of labeling (indicated as p above) was determined via absorbance at 405 nm and a corrected 280 nm value. The polymer conjugate (CJ04-02) provided in Example 39 (FIG. 22) had an F/P (# of polymers per antibody) of approximately 2.04. This conjugate demonstrated flow performance as determined by stain index measurements which were greater than 3 fold higher than a Pacific Blue control conjugate of the same antibody. Example 46: Conjugation of Polymer to an Antibody Using Malemide/Thiol Chemistry Malemide/Thiol Conjugation of Polymers to Partially Reduced Antibodies Secondary antibody, goat anti-mouse IgG (H+L) was reconstituted in PBS+10 mM acetic acid and desalted/exchanged into 50 mM Tris-HCl buffer, pH7.4 at 1.0 mg/mL. TCEP (tris(2-carboxyethyl)phosphine) was dissolved in 50 mM Tris-HCl buffer, pH7.4, added at 6 molar excess with a final TCEP concentration of 10 mM and mixed for 30 minutes at room temperature. The modified protein was purified over a PD-10 desalting column to remove excess TCEP and exchanged into reaction buffer, 100 mM NaPO4, pH 6.5 reaction buffer with 10 mM EDTA. Amine-activated polymer was dissolved in anhydrous DMSO at 10 mg/mL and mixed with succinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SMCC) linker. The linker was added at 50 mg/mL, 20 molar excess in DMSO to the polymer solution and activated by diisopropylethylamine (DIPEA). The reaction was purified over Amicon Ultra centrifugation filters and exchanged into reaction buffer, 100 mM NaPO4, pH 6.5 reaction buffer with 10 mM EDTA. Immediately following disulfide reduction, maleimide functionalized polymer in reaction buffer at 10 mg/mL was added in 20 molar excess of antibody and allowed to mix for 4 hours. Ion exchange and size exclusion chromatographic techniques were then used to purify the bioconjugate of unreacted polymer and antibody, respectively. Degree of labeling (indicated as p above) is determined via absorbance at 405 nm and a corrected 280 nm value. The polymer conjugate provided in Example 36 (FIG. 20B) had an F/P (# of polymers per antibody) of approximately 2. This conjugate demonstrated flow performance as determined by stain index measurements which were greater than 4 fold higher than a Pacific Blue control conjugate of the same antibody. Malemide/Thiol Conjugation of Polymers to Thiol Modified Antibodies Secondary antibody, goat anti-mouse IgG (H+L) was reconstituted in PBS+10 mM acetic acid and desalted/exchanged into 100 mM phosphate pH7.5 buffer. SATA (N-succinimidyl-S-acetylthioacetate) was dissolved anhydrous DMSO, added at 15 molar excess and mixed for 60 minutes at room temperature. After quenching with a hydroxylamine solution, the modified protein was desalted over a PD-10 column to remove excess SATA and exchanged into reaction buffer, 5 mM EDTA, PBS pH 7.0 buffer. Amine-activated polymer was dissolved in anhydrous DMSO at 10 mg/mL and mixed with succinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SMCC) linker. The linker was added at 50 mg/mL, 20 molar excess in DMSO to the polymer solution and activated by diisopropylethylamine (DIPEA). The reaction was purified over Amicon Ultra centrifugation filters and exchanged into reaction buffer, 5 mM EDTA, PBS pH 7.0 buffer. Immediately following activation of the antibody, maleimide functionalized polymer in reaction buffer at 10 mg/mL was added in 20 molar excess of antibody and allowed to mix for 4 hours. Ion exchange and size exclusion chromatographic techniques were then used to purify the bioconjugate of unreacted polymer and antibody, respectively. Degree of labeling (indicated as p above) is determined by absorbance at 405 nm and a corrected 280 nm value. The resulting purified conjugates were flow tested in similar fashion as those described in Example 36 for the conjugates prepared using TCEP reduction (data not provided). The polymer structures defined in Example 39 were used to prepare primary antiCD4 (RPA-T4) antibody conjugates in similar fashion to those described in the example above. 30 eq of polymer were reacted with the SATA modified antibody (CJ11-2, FIG. 22) and TCEP reduced antibody (CJ13-1, FIG. 20D and FIG. 22) to produce polymer conjugates for testing in flow cytometry assays after purification. SMCC modified polymers from Examples 23 and 26 were also successfully conjugated to antiCD4 (RPA-T4) and antiCD8 (RPA-T8) antibodies using the TCEP reduction method. DTT reduction was also successfully performed in place of TCEP. Performance in flow cytometry of the antiCD4 and antiCD8 conjugates were evaluated in similar fashion to those described in Example 39 (FIG. 22). Example 47: Polymer Conjugation to a DNA Oligomer Azide Polymer Synthesis for Click Conjugation to Alkyne Terminated DNA Oligo A solution of azidohexanoic acid NHS ester (2.5 mg) in anhydrous DMF (100 μL) was added to a solution of the amine-functional polymer (9.9 mg) in anhydrous DMF (100 μL) under argon. Diisopropylethylamine (2 μL) was then added. The reaction was agitated at room temperature for 15 hours. Water was then added (0.8 mL) and the azide-modified polymer was purified over a NAP-10 column. The eluent was freeze dried overnight. Yield 9.4 mg, 95%. Oligo Synthesis with Pendant Alkyne (Hexyne) for Click Conjugation to Azide Polymer The 3′ propanol oligo A8885 (sequence YATTTTACCCTCTGAAGGCTCCP, where Y=hexynyl group and P=propanol group (SEQ ID NO: 1)) was synthesized using 3′ spacer SynBase™ CPG 1000 column on an Applied Biosystems 394 automated DNA/RNA synthesizer. A standard 1.0 mole phosphoramidite cycle of acid-catalyzed detritylation, coupling, capping and iodine oxidation was used. The coupling time for the standards monomers was 40 s, and the coupling time for the 5′ alkyne monomer was 10 min. The oligo was cleaved from the solid support and deprotected by exposure to concentrated aqueous ammonia for 60 min at room temperature, followed by heating in a sealed tube for 5 h at 55° C. The oligo was then purified by RP-HPLC under standard conditions. Yield 34 OD. Solution Phase Click Conjugation: Probe Synthesis A solution of degassed copper sulphate pentahydrate (0.063 mg) in aqueous sodium chloride (0.2 M, 2.5 μL) was added to a degassed solution of tris-benzo triazole ligand (0.5 mg) and sodium ascorbate (0.5 mg) in aqueous sodium chloride (0.2 M, 12.5 μL). Subsequently, a degassed solution of oligo A8885 (50 nmole) in aqueous sodium chloride (0.2 M, 30 μL) and a degassed solution of azide polymer (4.5 mg) in anhydrous DMF (50 μL) were added, respectively. The reaction was degassed once more with argon for 30s prior to sealing the tube and incubating at 55° C. for 2 h. Water (0.9 mL) was then added and the modified oligo was purified over a NAP-10 column. The eluent was freeze-dried overnight. The conjugate was isolated as a distinct band using PAGE purification and characterized by mass spectrometry. Yield estimated at 10-20%. Fluorescence Studies The oligo-polymer conjugate was used as a probe in fluorescence studies. The probe was hybridized with the target A8090 (sequence GGAGCCTTCAGAGGGTAAAAT-Dabcyl (SEQ ID NO: 2)), which was labeled with dabcyl at the 3′ end to act as a fluorescence quencher. The target and probe were hybridized, and fluorescence monitored in a Peltier-controlled variable temperature fluorimeter. The fluorescence was scanned every 5° C. over a temperature range of 30° C. to 80° C. at a rate of 2° C./min. FIG. 25 shows increasing fluorescence intensity or emission with increasing temperature, indicating that as the probe-target pair melt, the polymer and quencher separate and fluorescence is recovered. Polymer conjugation to nucleic acids can also be performed using methods adapted from the protocols described in Examples 14, 45 and 46. Example 48: Purification of Polymer Antibody Conjugates Polymer antibody conjugates produced via the protocols described in Examples 45, 46 and 49 were purified using a two step method. First ion exchange is used to remove free, unreacted polymer. As the polymers described in this invention do not possess any formal charge they do not bind to the ion exchange media. Proteins (antibodies), however, do contain charged groups and are commonly bound to various ion exchange media for purification. In the examples provided the pH and conductivity of the conjugate solution (post reaction) was lowered to improve the binding of the free antibody and conjugate to the cationic exchange resin. After loading the conjugate, the resin is washed to baseline (measuring both 280 and 407 nm absorbance) to ensure all free polymer is removed. Bound antibody and polymer antibody conjugate are eluted by increasing the pH and ionic strength. A representative example of this separation is provided below in FIG. 26 (left) where the left peak represents the free polymer and the right peak the eluted conjugate and free protein. Removal of free polymer can also be achieved using affinity chromatograph methods in a similar fashion. Specific affinity resin can be used to bind the free protein and conjugate while removing polymer. After the polymer is removed, the conjugate solution is concentrated and loaded on a size exclusion column to separate any un-reacted or free antibody from the polymer. The polymer compositions described in Examples 43 and 44 elute much earlier than then antibodies despite having a lower molecular weight. This is expected to be a result of the rigid polymer structure. The conjugates thus elute well before any free antibody providing near base line separation of the desired conjugate. Isolating fractions near the center of the distribution also ensures no free antibody is included. A representative example of this separation is provided below in FIG. 26 (right) where the left peak represents the conjugate and the small peak on the far right the free antibody. Retention times of the individual components was verified in an independent experiment. Taken together the purification ensures that both free antibody and free polymer are removed. Purity of the resulting conjugates is reasonably estimated at >95%. Pooled samples can be concentrated and concentration measured by absorbance at 280 and 407 nm, being sure to correct for the polymer absorbance at 280 nm. Such measurements also allow for the determination of polymer to antibody labelling ratios (F/P). Example 49: Dye Labeling and Linker Activation of Tandem Polymer Tandem Dye Conjugation In a glovebox, 93 mg tandem polymer (from Example 26) was dissolved at 15 mg/mL in anhydrous DMSO in a glass vial with stir bar. 22.5 mg Cy3-NHS ester was also dissolved at 15 mg/mL in anhydrous DMSO and added to the polymer solution, followed by 0.3 mL diisopropylethylamine. After stirring for 48 h at room temperature, the solution was diluted to 90 mL with 20% EtOH in water and concentrated over Amicon Ultra-15 filters. The retentate was repeatedly diluted and concentrated over the filters until excess Cy3 was removed. 90% yield. Labeling and linker content were validated by measuring and taking the ratio of polymer and dye absorbance as described in Example 38. Amine Modification of Tandem (Aqueous Conditions) 100 mg of polymer-dye conjugate was dissolved at 150 mg/mL in ethanol. This was added dropwise to 6 mL 50 mM MES buffer (pH 5) at 4° C. 38 mg N-hydroxy succinimide was added in one portion, and the solution was stirred to dissolve the solids. After dissolution, 192 mg of N-(3-dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride was added in portions while stirring. After stirring the solution for 30 minutes, 33 μL of ethylene diamine was added. After stirring overnight at room temperature, the solution was diluted to 90 mL with 20% EtOH in water and concentrated over Amicon Ultra-15 filters. The retentate was repeatedly diluted and concentrated over the filters a total of four times to remove impurities. 90% yield, 60% conversion. Linker conversion was verified by conjugating a second dye to the terminal amine as described in Example 38. Tandem Conjugation to a Primary Antibody Primary monoclonal antibody, anti-CD8 (RPA-T8 clone) was desalted/exchanged into 5 mM EDTA, 50 mM phosphate 150 mM NaCl pH 7.0 buffer. TCEP (tris(2-carboxyethyl)phosphine) was dissolved water and added at 12 molar excess and mixed for 90 minutes at 30° C. The modified protein was purified over a PD-10 desalting column to remove excess TCEP and exchanged into 5 mM EDTA, 50 mM phosphate 150 mM NaCl pH 7.0 buffer. Amine-activated tandem polymer was dissolved in ethanol at 50 mg/mL and this solution was mixed with two volumes of 100 mM phosphate pH 7.5 buffer. This solution was then desalted/exchanged into 100 mM phosphate pH 7.5 buffer using a PD-10 desalting column. To this solution was added 25 molar excess of succinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SMCC) linker (prepared as a 10 mg/ml solution in anhydrous DMSO). The resulting solution was roller mixed at 20° C. for 60 minutes before being desalted/exchanged into 5 mM EDTA, 50 mM phosphate 150 mM NaCl pH 7.0 buffer using a PD-10 desalting column. Immediately following disulfide reduction, the maleimide functionalized polymer was added in 25 molar excess of antibody and allowed to mix for 2 hours at 20° C. Ion exchange and size exclusion chromatographic techniques were then used to purify the bioconjugate of unreacted polymer and antibody, respectively. Degree of labeling (indicated as p below) is determined via absorbance and a corrected 280 nm value. Flow Cytometry Analysis of Polymer Tandem Conjugate in Multicolor Experiment The resulting antiCD8 Tandem conjugate was evaluated on both compensation beads and whole blood samples on a flow cytometer. Anti mouse IgG compensation beads were used to capture the antibody and quantify signal spill over into detection channels (detectors with unique emission filters) other than that intended for the conjugate. FIG. 28 (left) shows the signal measured when the tandem conjugate was excited with a violet laser with emission detected using a 610 nm filter matched to the conjugates emission (labeled QDotA). Crosstalk into the flow cytometer's other channels paired with the violet excitation laser (DAPI-A and AmCyan-A) and two channels off the 488 nm laser (FITC-A and PE-A) are also shown in this panel of the figure. The data show minimal crosstalk in the 450/50 nm filter (DAPI-A) which specifically detects residual polymer (donor) emission. The significantly higher signal from the Cy3 reporter on the Tandem (610 nm filter) relative to the other channels above illustrates that minimal compensation (maximally no more than 6% in this example and case by case often much lower) is required. The Tandem anti CD8 conjugate was subsequently evaluated in a 4 color flow assay with other labeled antibodies (anti CD3 Pacific Blue, anti CD45 Phycoerythrin and anti CD4 fluorescein) on whole human blood from a healthy volunteer using staining and analysis protocols in accord and developed from Example 39. The data in FIG. 28 (right) clearly show the compatibility of the Tandem label with common multicolour flow cytometry instrumentation, reagents and protocols. Specifically, intense and specific staining of CD8 positive lymphocytes is observed and within the CD4 positive subset ready discrimination of CD8 expressive and non expressive cells is clear Collectively the data highlight the viability of the polymer-dye Tandem conjugates in multicolor flow assays as described in the disclosed invention (See, e.g., FIG. 20 and FIG. 22). Example 50: Validation of Non-Ionic Polymer Side Chains for Water Solubility and Flow Cytometry Application A series of different polyfluorene polymers were produced to investigate the interaction of water soluble conjugated polymers with cells. This was done by first synthesizing a range of monomers substituted with different solubilizing side chains (e.g., PEG-, sulfonate-, quaternary amine-, zwitterion- substituted) which were then polymerized using Suzuki coupling. The purpose was to determine what influence the side chains had on both non-specific cell binding and polymer solubility in typical buffers used in biological assays, particularly those used in flow cytometry (e.g. PBS and DPBS). The number and property diversity of polymer candidates synthesized made it impractical to produce purified conjugates of each for flow cytometry testing. Thus, a system was developed to score each candidate polymer based on its contribution to non-specific binding to cells. Such a system enabled ranking of polymers, with predictive value on whether they would perform sufficiently once conjugated. A Non-specific Binding (NSB) “Index” was developed around a Jurkat cell model (lymphocyte cell line). In this, cells were incubated with a fixed concentration of each polymer, washed, and analyzed by flow. FIG. 33 displays the outcome following such analysis, and illustrates the wide variation in signal generated by each polymer type. The polymers in FIG. 33 were evaluated with a phthalamide protecting group on the pendant amine with the exception of P9. The data ranks these polymers in terms of signal generated purely by NSB. More accurate assessment of relative NSB was enabled by adjusting further normalizing the flow signal by differences in fluorescence efficiency (crude assessment of quantum yield) of each form of polymer when assayed independently in stain buffer using 405 nm excitation on a fluorometer and monitoring emission in the range of 420-460 nm (to estimate a 440/40 nm filter in the cytometer). Representative polymers P5, P2, P9 and P12 showed increasing NSB relative to unstained cells (far left curve, intensity represented on x-axis). The data in FIG. 34 go on to highlight the difference in polymers produced with neutral, non-ionic PEG side chains (designated P20) verses those which also incorporate anionic side chains (designated P4). The data are histograms collected from flow cytometry analysis (405 nm excitation in a BD LSR-II cytometer) using a Jurkat cell line as in FIG. 33. The panel on the left shows unstained cells and a negative control (cells treated with a non-specific Pacific Blue labeled conjugate) which are the two curves on the far left. Little if any non-specific staining is observed for the Pacific Blue control. In this same panel, however, curve on the right represents cells treated with the anionic P4 polymer and has a clear off set in signal (x-axis) as shown. Conversely the neutral polymer P20 showed almost no off set from the untreated cells which is in line with the Pacific Blue control. The panel in the middle represents a range of different polymer and polymer side chain combinations tested on the same cells. The data highlighted the advantage of neutral side chains. This advantage has also translated to other assay formats including plate based immunoassays and cytometric bead arrays (data not shown). The neutral side chains also unexpectedly resulted in a significant increase in the solubility of the conjugated polymers in aqueous solutions relative to those made previously with ionic side chains. This was particularly true in buffers containing even moderate ionic strength (such as those used in basic cell protocols). The solution quantum yields were also seen to increase, possibly due to the higher aqueous solubility (and less aggregation). The poor solubility in buffers also made protein conjugation more difficult and streptavidin conjugates produced from P4 showed signs of aggregation in typical assay buffers such as phosphate buffered saline (PBS). This was not true of polymers and conjugates produced in other examples disclosed herein. Example 51: Purification and Characterization of Polymer-Avidin Conjugates Gel Analysis of Polymer-Avidin Conjugates To verify successful conjugation to avidin (AvDN), an agarose gel electrophoresis method was developed and used to assess the relative mobility of AvDN as a function of the degree of conjugation with polymer (FIG. 35). Prior to gel loading, the conjugation reaction was stained with biotinyl-fluorescein, which bound polymer-AvDN conjugate and free AvDN. Electrophoresis was performed in 0.8% agarose gels, poured and run in a buffer of 10 mM Sodium Borate, pH 11. The gel was visualized under UV illumination (to visualize the polymer) and by 532 nm excitation (to visualize fluorescein) to assess the degree of conjugation. Under UV illumination, a single band was observed for polymer. Under 532 nm excitation, bands were observed for unbound biotinyl-fluorescein, unreacted AvDN, and polymer-AvDN conjugate which coincided with the free polymer band, indicating that unreacted polymer co-eluted with polymer-AvDN conjugate (FIG. 35). Conjugation was confirmed by the intensity of the conjugate band. The key at the top of the gel images (FIG. 35) indicates which components were included in the conjugation reaction, as well as whether the samples were pre-incubated with biotinyl fluorescein prior to loading and electrophoresis. The image on left visualizes polymer by UV-excitation, whereas the image on right captures the result of fluorescein excitation. On the right image, biotinylated fluorescein can be seen associating with polymer when conjugation was performed in the presence, but not in the absence, of hetero-bifunctional NHS-ethoxy-maleimide linkers (linkers were used to functionalize the polymer amine, while protein amines were partially converted to thiols using Traut's reagent, prior to the maleimide-thiol coupling). Abbreviations: AvDN=avidin DN, AA1=polymer, Linker=hetero-bifunctional NHS-Maleimide linker included in the reaction, Biot-F=biotinyl fluorescein pre-staining before electrophoresis. Purification: Removal of Unreacted Avidin by SEC Chromatography The crude conjugate mixture was fractionated on a Superdex 200 size exclusion column, while fractions were monitored by UV absorbance (FIG. 36, top). To validate the method, fractions were analyzed by agarose gel electrophoresis. As described above, this method of electrophoresis made it possible to visualize the degree to which avidin was attached to polymer, and in this case to analyze the composition of each fraction from the column. Selected fractions were incubated with biotinyl-fluorescein (1 molar equivalent relative to avidin) prior to gel loading, with biotinyl-fluorescein loaded separately as a marker (leftmost lane, FIG. 36, bottom). Electrophoresis was performed in 0.8% agarose gels, poured and run in a buffer of 10 mM Sodium Borate, pH 11. The gel was visualized by 532 nm excitation. Retardation of fluorescein-visualized bands for fractions C2-C6 indicates purified polymer-avidin conjugate, while the two bands observed for fraction C8 indicate a mixture of polymer-avidin conjugate and free avidin. Fractions C10-D2 show only free avidin. Evaluation of Conjugation Efficiency by Gel Analysis In order to determine the best ratio of polymer to streptavidin in conjugation reactions, the molar equivalents of polymer to streptavidin were varied from 0-24 equivalents. Post conjugation, the conjugation products were incubated with biotinyl-fluorescein prior to electrophoresis. The gel was visualized by UV illumination and 532 nm excitation (FIG. 37). At 0 molar equivalents of polymer to streptavidin, free streptavidin is observed as a band with relatively high mobility. As the molar equivalents for polymer are increased from 3 equivalents to 12 equivalents, the free streptavidin band decreases in intensity while the polymer-streptavidin conjugate band increases in intensity. At 24 equivalents of polymer, only the conjugate band is observed by 532 nm excitation. Impact of Purification on Conjugate Performance on Cell Analysis by Flow Cytometry Purification of polymer streptavidin conjugates (polymer structure exemplified in Example 9, denoted P30 in FIG. 38) was performed to determine the impact on flow cytometry performance. Cation-exchange chromatography was implemented in purification to improve removal of excess free polymer. Uncharged polymer eluted in the flow-through while protonated amines on proteins were retained by the media. Thus, streptavidin, whether conjugated to polymer or unreacted, was retained. This ion exchange phase of purification was kept simple with a step gradient, which resulted in co-elution of conjugated and unreacted SA. Further fractionation was enabled by subsequent size-exclusion chromatography, which provided better resolution of conjugate from free SA. Performance benefits in flow cytometry of this new purification method were observed using Jurkat cells incubated with polymer-streptavidin conjugate which were analyzed by flow cytometry. Comparisons were made between crude samples (FIG. 38—top) and purified conjugates (FIG. 38 bottom). Commercially available Pacific Blue-streptavidin conjugates were used as a comparator for brightness, nonspecific binding, and stain index. An improvement in overall Stain Index of approximately 3-fold was shown for Jurkat cells, with similar NSB for both Polymer conjugates and PB-SA based on the histograms shown in FIG. 38. Testing in blood (data not shown) indicated a significant reduction in NSB to levels similar to PB-SA upon conjugate purification. In a separate experiment with a similar polymer (exemplified in Example 11), conjugates with varying polymer to streptavidin ratios were obtained by SEC. Those with the higher ratio provided flow performance relative to those with lower labeling. Ratios were determined based on a ratio of absorbance at 385 nm/280 nm. Relative performance to a Pacific Blue control showed an increase from 10.9 times higher stain index (385/280 ratio of 3.6) to a stain index 13.8 times that of Pacific Blue (A385/280 ratio of 4.7). While preferred embodiments of the present invention have been shown and described herein, it will be obvious to those skilled in the art that such embodiments are provided by way of example only. Numerous variations, changes, and substitutions will now occur to those skilled in the art without departing from the invention. It should be understood that various alternatives to the embodiments of the invention described herein may be employed in practicing the invention. It is intended that the following claims define the scope of the invention and that methods and structures within the scope of these claims and their equivalents be covered thereby."},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE INVENTION <EOH>Fluorescent hybridization probes have developed into an important tool in the sequence-specific detection of DNA and RNA. The signals generated by the appended fluorescent labels (or dyes) can be monitored in real time and provide simple, rapid, and robust methods for the detection of biological targets and events. Utility has been seen in applications ranging from microarrays and real time PCR to fluorescence in situ hybridization (FISH). Recent work in the area of multichromophores, particularly regarding conjugated polymers (CPs) has highlighted the potential these materials have in significantly improving the detection sensitivity of such methods (Liu and Bazan, Chem. Mater., 2004). The light harvesting structures of these materials can be made water soluble and adapted to amplify the fluorescent output of various probe labels (See U.S. patent application Ser. No. 10/600,286, filed Jun. 20, 2003 and Gaylord, Heeger, and Bazan, Proc. Natl. Acad. Sci., 2002, both of which are incorporated herein by reference in their entirety). Results such as these indicate CPs to be highly promising in the field of nucleic acid diagnostics, particularly where sample quantities are scarce. However, there exist methods for the amplification (or replication) of nucleic acid targets, i.e., PCR. Comparatively, in the field of protein recognition, there are no such simple methods for amplifying the targeted materials. As such, signal enhancement arising from CP application is of high consequence in this area. Dye-labeled antibodies are regularly used for the detection of protein targets in applications such as immunohistochemistry, protein arrays, ELISA tests, and flow cytometry. Integrating CP materials into such methodologies promises to provide a dramatic boost in the performance of such assays, enabling detection levels previously unattainable with conventional fluorescent reporters (e.g., dyes). Beyond addition signal, one of the other key drivers in biological detection formats is the ability to detect multiple analytes in the same test or multiplexing. This is commonly achieved by using fluorescent reporters with operate at different, discernable wavelengths. CP materials are ideally suited to provide a platform for expanded multiplexing. This can be achieved by tuning the structure of different CPs to operate at different wavelengths or by incorporating a dye within the polymer-biomolecule conjugate. The material and methods to produce higher sensitivity biological assays and increase multiplexing are highly desired in both molecular (nucleic acid) and immunoassay formats."},"summary":{"kind":"string","value":"<SOH> SUMMARY OF THE INVENTION <EOH>Provided herein are water soluble conjugated polymers of Formula (I): wherein: each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 1 -C 12 alkoxy, C 2 -C 18 (hetero)aryloxy, C 2 -C 18 (hetero)arylamino, (CH 2 ) x′ (OCH 2 CH 2 ) y′ OCH 3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C 2 -C 18 (hetero)aryl group; each optional linker L 1 and L 2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another substrate, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G 1 and G 2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, and thiols within G 1 , G 2 , L 1 or L 2 that allows, for functional conjugation to another molecule, substrate or biomolecule; each dashed bond, , is independently a single bond, triple bond or optionally substituted vinylene (—CR 5 ═CR 5 —) wherein each R 5 is independently hydrogen, cyano, C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl or a C 2 -C 18 (hetero)aryl group, wherein each C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl or a C 2 -C 18 (hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkenyl, C 2 -C 12 alkynyl group, C 1 -C 12 alkoxy, or C 1 -C 12 haloalkyl; and n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. In one aspect, water soluble conjugated polymers of Formula (I) have the structure of Formula (Ia): wherein R, L 1 , L 2 , G 1 , G 2 , MU, a, b, c, d and n are described previously for formula (I). In some embodiments, each R is independently (CH 2 ) x (OCH 2 CH 2 ) y OCH 3 where each x is independently an integer from 0-20, each y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkoxy, or (OCH 2 CH 2 ) z OCH 3 where each z is independently an integer from 0 to 50. In some instances, each R is (CH 2 ) 3 (OCH 2 CH 2 ) 11 CH 3 . In other embodiments, each R is a benzyl substituted with at least one (OCH 2 CH 2 ) 10 OCH 3 group. In some instances, the benzyl is substituted with two (OCH 2 CH 2 ) 10 OCH 3 groups. In other instances, the benzyl is substituted with three (OCH 2 CH 2 ) 10 OCH 3 groups. In some embodiments, optional linkers L 1 or L 2 have the structure: *=site for covalent attachment to unsaturated backbone; wherein R 3 is independently hydrogen, halogen, alkoxy(C 1 -C 12 ), C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl or a C 2 -C 18 (hetero)aryl group, wherein each C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl or a C 2 -C 18 (hetero)aryl group is optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkenyl, C 2 -C 12 alkynyl group, C 1 -C 12 alkoxy, or C 1 -C 12 haloalkyl; and q is an integer from 0 to 4. In other embodiments, optional linkers L 1 or L 2 have the structure: *=site for covalent attachment to unsaturated backbone wherein A is a site for conjugation, chain extension or crosslinking and is [O—CH 2 —CH 2 ] q —W, or (C 1 -C 12 )alkoxy-X or C 2 -C 18 (hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; W is —OH or —COOH; X is —NH 2 , —NHCOOH, —NHCOOC(CH 3 ) 3 , —NHCO(C 3 -C 12 )cycloalkyl(C 1 -C 4 )alkyl-N-maleimide; or —NHCO[CH 2 —CH 2 —O] t NH 2 ; q is an integer from 1 to 20; and t is an integer from 1 to 8. In yet other embodiments, optional linkers L 1 or L 2 have the structure: *=site for covalent attachment to backbone wherein R 25 are each independently any one of or a combination of a bond, C 1 -C 20 alkyl, C 1 -C 20 alkoxy, C 2 -C 20 alkene, C 2 -C 20 alkyne, C 3 -C 20 cycloalkyl, C 1 -C 20 haloalkyl, (CH 2 ) x (OCH 2 CH 2 ) p (CH 2 ) x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C 2 -C 18 (hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups; wherein at least one R 25 is terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In further embodiments, optional linkers L 1 or L 2 have the structure: *=site for covalent attachment to unsaturated backbone; wherein R35 is any one of or a combination of a bond, C1-C20 alkyl, C1-C20 alkoxy, C2-C20 alkene, C2-C20 alkyne, C3-C20 cycloalkyl, C1-C20 haloalkyl, (CH2)x(OCH2CH2)p(CH2)x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C2-C18(hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In further embodiments, optional linkers L 1 or L 2 are selected from the group consisting of a-h having the structures: *=site for covalent attachment to unsaturated backbone; wherein R′ is independently H, halogen, C 1 -C 12 alkyl, (C 1 -C 12 alkyl)NH 2 , C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 2 -C 18 (hetero)aryl, C 2 -C 18 (hetero)arylamino, —[CH 2 —CH 2 ] r′ —Z 1 , or (C 1 -C 12 )alkoxy-X 1 ; and wherein Z 1 is —OH or —COOH; X 1 is —NH 2 , —NHCOOH, —NHCOOC(CH 3 ) 3 , —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH 2 —CH 2 —O] s′ (CH 2 ) s′ NH 2 ; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH 2 ) 3 (OCH 2 CH 2 ) x″ OCH 3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkoxy, or (OCH 2 CH 2 ) y —OCH 3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein k is 2, 4, 8, 12 or 24; wherein R 15 is selected from the group consisting of l-t having the structure: *=site for covalent attachment to backbone. In yet further embodiments, optional linkers L 1 or L 2 are In some embodiments, G 1 and G 2 are each independently selected from hydrogen, halogen, alkyne, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorine and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group, molecule or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In some embodiments, G 1 and G 2 each independently have the structure wherein R 11 is any one of or a combination of a bond, C 1 -C 20 alkyl, C 1 -C 20 alkoxy, C 2 -C 20 alkene, C 2 -C 20 alkyne, C 3 -C 20 cycloalkyl, C 1 -C 20 haloalkyl, (CH 2 ) x (OCH 2 CH 2 ) p (CH 2 ) x where each x is independently an integer from 0-20, p is independently an integer from 0 to 50, aryl, C 2 -C 18 (hetero)aryl, phenoxy, amido, amino, carbamate, carboxylate, carbonates, sulfide, disulfide, or imido groups terminated with a functional group selected from amine, carbamate, carboxylate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule. In other embodiments, G 1 and G 2 are each independently selected from the group consisting of 1-31 having the structures: *=site for covalent attachment to backbone wherein R 15 is selected from the group consisting of l-t having the structure: and k is 2, 4, 8, 12 or 24. In further embodiments, G 1 and G 2 are optionally substituted aryl or heteroaryl wherein the optional substituent is selected from halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiol, boronic acid, boronate radical, boronic esters and optionally substituted fluorene. In some embodiments, G 1 and G 2 are the same. In other embodiments, G 1 and G 2 are different. In further embodiments, the polymer contains a single conjugation site at only one terminus of the polymer chain G 1 or G 2 . In yet further embodiments, G 1 and G 2 is In some embodiments, MU is selected from the group consisting of a′-k′ having the structure: *=site for covalent attachment to unsaturated backbone wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein at least one of G 1 or G 2 comprises a functional conjugation site. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein L 1 comprises a functional conjugation site. In some embodiments, the water soluble conjugated polymer has the structure of formula: wherein at least one of G 1 or G 2 comprises a functional conjugation site. In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In other embodiments, the polymer has the structure of formula: In some instances, a signaling chromophore is attached to the polymer via the NH 2 group. In certain instances, the signaling chromophore is Cy3 or Dylight 594 dye. In certain instances, the linker, is about 10% of the entire polymer. In other instances, the polymer is conjugated to a secondary dye reporter and an antibody. In some embodiments of conjugated polymers described herein, the polymer is further conjugated to additional molecules. In some embodiments, the polymer is conjugated to a streptavidin, antibody or nucleic acid and used as a direct fluorescent reporter. In certain embodiments, the polymer is conjugated to a streptavidin. In other embodiments, the polymer is conjugated to thiol groups at the hinge region of an antibody. In yet other embodiments, the polymer is conjugated to an amine group on a protein which is modified with a heterobifunctional linker. In further embodiments, the polymer is conjugated to a nucleic acid. In yet further embodiments, the polymer is conjugated to an antibody. In certain instances, the polymer is conjugated to a monoclonal antibody, a secondary antibody or a primary antibody. In other instances, a polymer antibody conjugate is excited at about 405 nm in a flow cytometry assay where the specific signal is at least 3 fold greater than the same antibody conjugated to Pacific Blue. In some embodiments of conjugated polymers described herein, the polymer is purified by ion exchange chromatography. In other embodiments, the polymer is >95% pure. In some embodiments of conjugated polymers described herein, the polymer is used in flow cytometry assays to identify different cell markers or cell types. In other embodiments, the polymer is used to sort cells. In yet other embodiments, the polymer is used to sort cells for use in therapeutics. In some embodiments of conjugated polymers described herein, the polymer is used for intracellular staining. In certain instances, the polymer is used in flow cytometry assays to identify different cell markers or cell types. In some embodiments of conjugated polymers described herein, the polymer comprises a minimum number average molecular weight of greater than 40,000 g/mol and a water solubility of greater than 50 mg/mL in pure water or a phosphate buffered saline solution. In some embodiments of conjugated polymers described herein, the polymer comprises at least two unique conjugation linkers which can conjugated to two unique materials. Also provided herein are assay methods comprising providing a sample that is suspected of containing a target biomolecule; providing a sensor protein conjugated to at least one signaling chromophore and is capable of interacting with the target biomolecule or a target-associated biomolecule; providing a water soluble conjugated polymer described herein; contacting the sample with the sensor protein and the conjugated polymer in a solution under conditions in which the sensor protein can bind to the target biomolecule or a target-associated biomolecule if present; applying a light source to the sample that can excite the conjugated polymer; and detecting whether light is emitted from the signaling chromophore. In some embodiments, the sensor protein is an antibody. In other embodiments, the sensor protein comprises a plurality of sensor proteins conjugated to a plurality of signaling chromophores, wherein at least two of the plurality of chromophores emit different wavelengths of light upon energy transfer from the multichromophore. Also provided herein are conjugated polymer complexes comprising a polymer coupled to at least one biomolecule selected from the group consisting of a sensor biomolecule, a bioconjugate and a target biomolecule wherein the polymer is covalently bound by at least one bioconjugation site pendant thereto, and the polymer comprises a signaling chromophore or a signaling chromophore optionally is covalently bound to the polymer or the sensor biomolecule; wherein the polymer comprises the structure of formula: wherein: each R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along the polymer main chain and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 1 -C 12 alkoxy, C 2 -C 18 (hetero)aryloxy, C 2 -C 18 (hetero)arylamino, (CH 2 ) x′ (OCH 2 CH 2 ) y′ OCH 3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50, or a C 2 -C 18 (hetero)aryl group; each optional linker L 1 and L 2 are aryl or heteroaryl groups evenly or randomly distributed along the polymer main chain and are substituted with one or more pendant chains terminated with a functional group for conjugation to another molecule, substrate or biomolecule selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof; G 1 and G 2 are each independently selected from hydrogen, halogen, amine, carbamate, carboxylic acid, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiol, optionally substituted aryl, optionally substituted heteroaryl, halogen substituted aryl, boronic acid substituted aryl, boronic ester substituted aryl, boronic esters, boronic acids, optionally substituted fluorene and aryl or heteroaryl substituted with one or more pendant chains terminated with a functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, thiols, and protected groups thereof for conjugation to another substrate, molecule or biomolecule; wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, and thiols within G 1 , G 2 , L 1 or L 2 that allows, for functional conjugation to another molecule, substrate or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. In some embodiments, the sensor biomolecule is selected from the group consisting of an avidin, streptavidin, neutravidin, avidinDN, and avidinD. In other embodiments, the conjugated polymer complex is further configured to bind to a complex selected from the group consisting of a biotin-labeled antibody, biotin-labeled protein, and biotin-labeled target biomolecule. In further embodiments, the sensor biomolecule is an antibody. In yet further embodiments, both the signaling chromophore and the sensor biomolecule are covalently linked to the multichromophore through a plurality of linkers. In some other embodiments, both the signaling chromophore and the sensor biomolecule are covalently linked to the polymer through a central linking site that covalently binds the polymer, the signaling chromophore and the sensor biomolecule. In yet other embodiments, the signaling chromophore, when covalently bound to the polymer or the sensor biomolecule, is an organic dye. Also provided herein are water soluble conjugated polymer having the structure of Formula (Ia): wherein: each R is independently (CH 2 ) x (OCH 2 CH 2 ) y OCH 3 where each x is independently an integer from 0-20, y is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkoxy, or (OCH 2 CH 2 ) z OCH 3 where each z is independently an integer from 0 to 50; each optional linker L 1 or L 2 is selected from the group consisting of a-i having the structure *=site for covalent attachment to unsaturated backbone wherein R′ is independently H, halogen, C 1 -C 12 alkyl, (C 1 -C 12 alkyl)NH 2 , C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 2 -C 18 (hetero)aryl, C 2 -C 18 (hetero)arylamino, —[CH 2 —CH 2 ] r′ —Z 1 , or (C 1 -C 12 )alkoxy-X 1 ; and wherein Z 1 is —OH or —COOH; X 1 is —NH 2 , —NHCOOH, —NHCOOC(CH 3 ) 3 , —NHCO(C3-C12)cycloalkyl(C1-C4)alkyl-N-maleimide; or —NHCO[CH 2 —CH 2 —O] s′ (CH 2 ) s′ NH 2 ; r′ is an integer from 1 to 20; and each s′ is independently an integer from 1 to 20, (CH 2 ) 3 (OCH 2 CH 2 ) x″ OCH 3 where x″ is independently an integer from 0 to 50, or a benzyl optionally substituted with one or more halogen, hydroxyl, C 1 -C 12 alkoxy, or (OCH 2 CH 2 ) y″ OCH 3 where each y″ is independently an integer from 0 to 50 and R′ is different from R; wherein R 15 is selected from the group consisting of l-t having the structure: and k is 2, 4, 8, 12 or 24; *=site for covalent attachment to backbone MU is a polymer modifying unit or band gap modifying unit that is selected from the group consisting of a′-k′ having the structure: *=site for covalent attachment to unsaturated backbone; wherein R is a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; G 1 and G 2 are each independently selected from the group consisting of 1-31 having the structures: wherein the polymer comprises at least 1 functional group selected from amine, carbamate, carboxylic acid, carboxylate, maleimide, activated esters, N-hydroxysuccinimidyl, hydrazines, hydrazides, hydrazones, azide, alkyne, aldehydes, and thiols within G 1 , G 2 , L 1 or L 2 that allows, for functional conjugation to another molecule, substrate or biomolecule; n is an integer from 1 to about 10,000; and a, b, c and d define the mol % of each unit within the structure which each can be evenly or randomly repeated and where a is a mol % from 10 to 100%, b is a mol % from 0 to 90%, and each c and d are mol % from 0 to 25%. Also provided herein are water soluble conjugated polymer having the structure of Formula: wherein Ar is an aryl or heteroaryl and is optionally substituted with one or more optionally substituted substituents selected from halogen, hydroxyl, C 1 -C 12 alkyl, C 2 -C 12 alkene, C 2 -C 12 alkyne, C 3 -C 12 cycloalkyl, C 1 -C 12 haloalkyl, C 1 -C 12 alkoxy, C 2 -C 18 (hetero)aryloxy, C 2 -C 18 (hetero)arylamino, (CH 2 ) x′ (OCH 2 CH 2 ) y′ OCH 3 where each x′ is independently an integer from 0-20, y′ is independently an integer from 0 to 50; and dashed bonds, L 1 , L 2 , G 1 , G 2 , MU, a, b, c, d and n are described previously for formula (I)."},"cpc_label":{"kind":"string","value":"G01N3358"},"filing_date":{"kind":"string","value":"20170927"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180315"},"examiner_id":{"kind":"string","value":"86750.0"},"ipc_label":{"kind":"string","value":"G01N3358"},"npe_litigated_count":{"kind":"number","value":1,"string":"1"},"examiner_full_name":{"kind":"string","value":"TRUONG, DUC"},"invention_title":{"kind":"string","value":"NOVEL REAGENTS FOR DIRECTED BIOMARKER SIGNAL AMPLIFICATION"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"G01N"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32890,"cells":{"application_number":{"kind":"number","value":15719560,"string":"15,719,560"},"decision":{"kind":"string","value":"ACCEPTED"},"title":{"kind":"string","value":"FLOOR DRAIN FOR SAME FLOOR DRAINAGE WITHOUT DESCENDING FLOOR OF BUILDING"},"abstract":{"kind":"string","value":"A floor drain for same floor drainage of a building consists of a floor drain body and a floor drain cover The floor drain body consists of a lower accumulated water collection tank, a lateral accumulated water collection tank and an accumulated water discharge port. A bottom of the lower accumulated water collection tank is sealed, and has an angle of 70° to 120° with the lateral accumulated water collection tank. The floor drain cover is a plate with holes, and is divided into a lower upstream face and a lateral upstream face. The lower upstream face of the floor drain cover is located above the lower accumulated water collection tank, and the lateral upstream face of the floor drain cover is located outside the lateral accumulated water collection tank."},"claims":{"kind":"string","value":"1. A floor drain for same floor drainage without descending floor of a building, consisting of a floor drain body (1) and a floor drain cover (2), wherein the floor drain cover (2) and the floor drain body (1) are separable; the floor drain body (1) consists of a lower accumulated water collection tank (3), a lateral accumulated water collection tank (4) and an accumulated water discharge port (5); a bottom of the lower accumulated water collection tank (3) is closed, and the lower accumulated water collection tank (3) has an angle of 70° to 120° with the lateral accumulated water collection tank (4); the accumulated water discharge port (5) is located at the rear of the lateral accumulated water collection tank (4); the floor drain cover (2) is a plate with holes, and is divided into a lower upstream face (6) and a lateral upstream face (7); an angle between the lower upstream face (6) and the lateral upstream face (7) is 70° to 120°; the lower upstream face (6) of the floor drain cover (2) is located above the lower accumulated water collection tank (3); and the lateral upstream face (7) of the floor drain cover (2) is located outside the lateral accumulated water collection tank (4). 2. The floor drain for same floor drainage without descending floor of a building according to claim 1, wherein an inner wall of the bottom of the lower accumulated water collection tank (3) of the floor drain body (1) is higher than or level with an inner wall of a bottom of the accumulated water discharge port (5), and an area of a drainage section of the accumulated water discharge port (5) level with a horizontal section of a top surface of the lower accumulated water collection tank (3) of the floor drain body (1) is greater than or equal to 450 mm2 and less than 3500 mm2. 3. The floor drain for same floor drainage without descending floor of a building according to claim 2, wherein a support (8) protruding from an outer wall is arranged at the bottom of the lower accumulated water collection tank (3), and when the accumulated water discharge port (5) is horizontal, a bottom of the support (8) is above 5 mm lower than a bottom of the accumulated water discharge port (5), and a distance from the bottom of the support (8) to a top surface of the lower upstream face of the floor drain cover (2) is greater than 10 mm and less than 70 mm. 4. The floor drain for same floor drainage without descending floor of a building according to claim 3, wherein a distance from the closed bottom of the lower accumulated water collection tank (3) of the floor drain body (1) to a top surface of the lower upstream face (6) of the floor drain cover (2) is greater than 10 mm and less than 60 mm. 5. The floor drain for same floor drainage without descending floor of a building according to claim 4, wherein when the inner wall of the closed bottom of the lower accumulated water collection tank (3) centers on the accumulated water discharge port (5), a middle is lower and two sides are high. 6. The floor drain for same floor drainage without descending floor of a building according to claim 1, wherein more than one slot (9) is arranged on the lower accumulated water collection tank (3); more than one clamping groove (10) is arranged on the lateral accumulated water collection tank (4); more than one convex point (11) corresponding to the slot (9) is arranged on the lower upstream face (6) of the floor drain cover; or more than one slot (9) is arranged on the lateral accumulated water collection tank (4); more than one clamping groove (10) is arranged on the lower accumulated water collection tank (3); and a convex point (11) corresponding to the slot (9) is formed on the lateral upstream face (7) of the floor drain cover. 7. The floor drain for same floor drainage without descending floor of a building according to claim 2, wherein more than one slot (9) is arranged on the lower accumulated water collection tank (3); more than one clamping groove (10) is arranged on the lateral accumulated water collection tank (4); more than one convex point (11) corresponding to the slot (9) is arranged on the lower upstream face (6) of the floor drain cover; or more than one slot (9) is arranged on the lateral accumulated water collection tank (4); more than one clamping groove (10) is arranged on the lower accumulated water collection tank (3); and a convex point (11) corresponding to the slot (9) is formed on the lateral upstream face (7) of the floor drain cover. 8. The floor drain for same floor drainage without descending floor of a building according to claim 3, wherein more than one slot (9) is arranged on the lower accumulated water collection tank (3); more than one clamping groove (10) is arranged on the lateral accumulated water collection tank (4); more than one convex point (11) corresponding to the slot (9) is arranged on the lower upstream face (6) of the floor drain cover; or more than one slot (9) is arranged on the lateral accumulated water collection tank (4); more than one clamping groove (10) is arranged on the lower accumulated water collection tank (3); and a convex point (11) corresponding to the slot (9) is formed on the lateral upstream face (7) of the floor drain cover. 9. The floor drain for same floor drainage without descending floor of a building according to claim 4, wherein more than one slot (9) is arranged on the lower accumulated water collection tank (3); more than one clamping groove (10) is arranged on the lateral accumulated water collection tank (4); more than one convex point (11) corresponding to the slot (9) is arranged on the lower upstream face (6) of the floor drain cover; or more than one slot (9) is arranged on the lateral accumulated water collection tank (4); more than one clamping groove (10) is arranged on the lower accumulated water collection tank (3); and a convex point (11) corresponding to the slot (9) is formed on the lateral upstream face (7) of the floor drain cover. 10. The floor drain for same floor drainage without descending floor of a building according to claim 5, wherein more than one slot (9) is arranged on the lower accumulated water collection tank (3); more than one clamping groove (10) is arranged on the lateral accumulated water collection tank (4); more than one convex point (11) corresponding to the slot (9) is arranged on the lower upstream face (6) of the floor drain cover; or more than one slot (9) is arranged on the lateral accumulated water collection tank (4); more than one clamping groove (10) is arranged on the lower accumulated water collection tank (3); and a convex point (11) corresponding to the slot (9) is formed on the lateral upstream face (7) of the floor drain cover. 11. The floor drain for same floor drainage without descending floor of a building according to claim 6, wherein a plane greater than 50 mm is formed at the bottom of the support (8). 12. The floor drain for same floor drainage without descending floor of a building according to claim 7, wherein a plane greater than 50 mm is formed at the bottom of the support (8). 13. The floor drain for same floor drainage without descending floor of a building according to claim 8, wherein a plane greater than 50 mm is formed at the bottom of the support (8). 14. The floor drain for same floor drainage without descending floor of a building according to claim 9, wherein a plane greater than 50 mm is formed at the bottom of the support (8). 15. The floor drain for same floor drainage without descending floor of a building according to claim 10, wherein a plane greater than 50 mm is formed at the bottom of the support (8)."},"description":{"kind":"string","value":"TECHNICAL FIELD The present invention relates to a floor drain for same floor drainage, and more specifically, to a floor drain for same floor drainage without descending floor of a building. BACKGROUND Currently, if same floor drainage needs to be realized in a building toilet, a floor of the toilet is required to be descended entirely or locally. To reduce the height of descending the floor, the width of a flow path of a floor drain and an area of a drainage section are also reduced, thereby easily causing blockage or impeded drainage of the floor drain and a drainage pipeline. SUMMARY The purpose of the present invention is to overcome existing technical defects, so as to provide a floor drain for same floor drainage used in the same floor drainage without descending floor of a building, thereby improving the unobstruction and difficult blocking of the drainage, being easy to maintain, and improving human life and sanitary environments. A floor drain for same floor drainage without descending floor of a building in the present invention comprises a floor drain body and a floor drain cover. The floor drain cover and the floor drain body are separable. The floor drain body comprises a lower accumulated water collection tank, a lateral accumulated water collection tank and an accumulated water discharge port. A bottom of the lower accumulated water collection tank is closed, and the lower accumulated water collection tank has an angle of 70° to 120° with the lateral accumulated water collection tank. The accumulated water discharge port is located at the rear of the lateral accumulated water collection tank. The floor drain cover is a plate with holes, and is divided into a lower upstream face and a lateral upstream face. An angle between the lower upstream face and the lateral upstream face is 70° to 120°. The lower upstream face of the floor drain cover is located above the lower accumulated water collection tank. The lateral upstream face of the floor drain cover is located outside the lateral accumulated water collection tank. The floor drain can drain surface water from the lower upstream face and the lateral upstream face simultaneously, thereby increasing the area of a water inlet section and accelerating the drainage of the surface water. According to the floor drain for same floor drainage without descending floor of the building in the present invention, an inner wall of the bottom of the lower accumulated water collection tank of the floor drain body is higher than or level with an inner wall of a bottom of the accumulated water discharge port, so that when surface water enters the accumulated water discharge port, a certain level difference can be formed, and the surface water can directly flow into a drainage concentrator having a water sealing function and a maintenance function without passing through a water seal, thereby greatly improving the unobstruction of drainage. An area of a drainage section of the accumulated water discharge port level with a horizontal section of a top surface of the lower accumulated water collection tank of the floor drain body is greater than or equal to 450 mm2 and less than 3500 mm2, thereby guaranteeing that the floor drain has relatively large drainage discharge. According to the floor drain for same floor drainage without descending floor of the building in the present invention, a support protruding from an outer wall is arranged at the bottom of the lower accumulated water collection tank, and when the accumulated water discharge port is horizontal, a bottom of the support is above 5 mm lower than a bottom of the accumulated water discharge port, thereby guaranteeing that a certain slope is formed by the accumulated water discharge port and a pipeline connecting the accumulated water discharge port so that accumulated water is not retained in the pipeline, and guaranteeing that a water flow has a certain speed. A distance from the bottom of the support to a top surface of the lower upstream face of the floor drain cover is greater than 10 mm and less than 70 mm, so that the floor drain for same floor drainage can be directly embedded in a cushion, a leveling layer and a decorative layer of the building, thereby achieving a using effect of not descending the floor. According to the floor drain for same floor drainage without descending floor of the building in the present invention, a distance from the closed bottom of the lower accumulated water collection tank of the floor drain body to a top surface of the lower attaining surface of the floor drain cover is greater than 10 mm and less than 60 mm, and thus, the area of a flowing section of the accumulated water discharge port can be increased on the premise of applying to a condition of not descending the floor. According to the floor drain for same floor drainage without descending floor of the building in the present invention, when the inner wall of the closed bottom of the lower accumulated water collection tank centers on the accumulated water discharge port, a middle is lower and two sides are higher, so that a water flow having certain kinetic energy can be rapidly formed when only a little quantity of accumulated water enters the lower accumulated water collection tank on the ground, so that the lower accumulated water collection tank is not deposited, thereby improving a drainage effect. According to the floor drain for same floor drainage without descending floor of the building in the present invention, more than one slot is arranged on the lower accumulated water collection tank; more than one clamping groove is arranged on the lateral accumulated water collection tank; more than one convex point corresponding to the slot is formed on the lower attaining surface of the floor drain cover; or more than one slot is arranged on the lateral accumulated water collection tank; more than one clamping groove is arranged on the lower accumulated water collection tank; and a convex point corresponding to the slot is formed on the lateral attaining surface of the floor drain cover. Therefore, when the convex point is inserted into the slot, the floor drain cover can be fixed to the floor drain body or separated from the floor drain body for blockage removal and maintenance by applying a certain force to the floor drain cover in a position of the clamping groove. According to floor drain for same floor drainage without descending floor of the building in the present invention, a plane greater than 50 mm is formed at the bottom of the support, and when the floor drain for same floor drainage is installed, the floor drain for same floor drainage placed on the ground can be guaranteed not to fall toward one side when the lower accumulated water collection tank has a lower middle and two higher sides. BRIEF DESCRIPTION OF DRAWINGS FIG. 1 is a top view of the present invention; FIG. 2 is a sectional view of a section A-A of FIG. 1; FIG. 3 is a side view of FIG. 1; FIG. 4 is a front view of FIG. 1; FIG. 5 is a rear view of FIG. 1; FIG. 6 is a sectional view of a section B-B of FIG. 1; and FIG. 7 is a diagram of separation of a floor drain body and a floor drain cover of the present invention. DETAILED DESCRIPTION The present invention is further described below in combination with drawings, but is not limited to embodiments. Embodiment 1 As shown in FIGS. 1, 2 and 7, a floor drain for same floor drainage without descending floor of a building in the present invention consists of a floor drain body 1 and a floor drain cover 2. The floor drain body 1 and the floor drain cover 2 are separable. The floor drain body 1 consists of a lower accumulated water collection tank 3, a lateral accumulated water collection tank 4 and an accumulated water discharge port 5. A bottom of the lower accumulated water collection tank 3 is closed, and the lower accumulated water collection tank 3 has an angle of 90° with the lateral accumulated water collection tank 4. The accumulated water discharge port 5 is located at the rear of the lateral accumulated water collection tank 4. The floor drain cover 2 is a plate with holes, and is divided into a lower upstream face 6 and a lateral upstream face 7. An angle between the lower upstream face 6 and the lateral upstream face 7 is 90°. The lower upstream face 6 of the floor drain cover 2 is located above the lower accumulated water collection tank 3 of the floor drain body 1. The lateral upstream face 7 of the floor drain cover 2 is located outside the lateral accumulated water collection tank 4 of the floor drain body 1. Embodiment 2 As shown in FIGS. 2 and 5, an inner wall of the bottom of the lower accumulated water collection tank 3 of the floor drain body 1 of the floor drain for same floor drainage without descending floor of the building in the present invention is higher than or level with an inner wall of a bottom of the accumulated water discharge port 5. An area of a drainage section of the accumulated water discharge port 5 level with a horizontal section of a top surface of the lower accumulated water collection tank of the floor drain body 1 is greater than or equal to 450 mm2 and less than 3500 mm2, preferably 1080 mm2. Others are the same as those of Embodiment 1. Embodiment 3 As shown in FIGS. 2, 3 and 4, a distance from the inner wall of the closed bottom of the lower accumulated water collection tank 3 of the floor drain body 1 of the floor drain for same floor drainage without descending floor of the building in the present invention to the lower attaining surface of the floor drain cover 2 is 20 mm. A support 8 protruding from an outer wall is arranged at the bottom of the lower accumulated water collection tank 3, and when the accumulated water discharge port 5 is horizontal, a bottom of the support 8 is 8 mm lower than a bottom of the accumulated water discharge port 5, and a distance from the bottom of the support 8 to a top surface of the lower upstream face of the floor drain cover 2 is 35 mm. Others are the same as those of Embodiment 2. Embodiment 4 As shown in FIGS. 5 and 6, when the inner wall of the closed bottom of the lower accumulated water collection tank 3 of the floor drain for same floor drainage without descending floor of the building in the present invention centers on the accumulated water discharge port 5, a middle is lower and two sides are higher. Others are the same as those of Embodiment 3. Embodiment 5 As shown in FIGS. 1 and 4, two slots 9 are formed on the lower accumulated water collection tank 3 of the floor drain for same floor drainage without descending floor of the building in the present invention. One clamping groove 10 is formed in a lateral accumulated water collection tank 4. Two convex points 11 corresponding to the slot 9 are formed on the lower upstream face 6 of the floor drain cover. Others are the same as those of Embodiment 4. Embodiment 6 As shown in FIGS. 2, 3, 4 and 5, the bottom of the support 8 of the floor drain for same floor drainage without descending floor of the building in the present invention is a rectangular plane, and a long side is 90 mm. The above only describes preferred embodiments of the present invention, and is only used for describing the technical solution of the present invention, rather than liming the present invention. Although the present invention is described in detail by referring to better embodiments, those ordinary skilled in the art should understand that any amendment, equivalent replacement, improvement and the like made within spirits and principles of the present invention should be included in a protection scope of the present invention."},"background":{"kind":"string","value":"<SOH> BACKGROUND <EOH>Currently, if same floor drainage needs to be realized in a building toilet, a floor of the toilet is required to be descended entirely or locally. To reduce the height of descending the floor, the width of a flow path of a floor drain and an area of a drainage section are also reduced, thereby easily causing blockage or impeded drainage of the floor drain and a drainage pipeline."},"summary":{"kind":"string","value":"<SOH> SUMMARY <EOH>The purpose of the present invention is to overcome existing technical defects, so as to provide a floor drain for same floor drainage used in the same floor drainage without descending floor of a building, thereby improving the unobstruction and difficult blocking of the drainage, being easy to maintain, and improving human life and sanitary environments. A floor drain for same floor drainage without descending floor of a building in the present invention comprises a floor drain body and a floor drain cover. The floor drain cover and the floor drain body are separable. The floor drain body comprises a lower accumulated water collection tank, a lateral accumulated water collection tank and an accumulated water discharge port. A bottom of the lower accumulated water collection tank is closed, and the lower accumulated water collection tank has an angle of 70° to 120° with the lateral accumulated water collection tank. The accumulated water discharge port is located at the rear of the lateral accumulated water collection tank. The floor drain cover is a plate with holes, and is divided into a lower upstream face and a lateral upstream face. An angle between the lower upstream face and the lateral upstream face is 70° to 120°. The lower upstream face of the floor drain cover is located above the lower accumulated water collection tank. The lateral upstream face of the floor drain cover is located outside the lateral accumulated water collection tank. The floor drain can drain surface water from the lower upstream face and the lateral upstream face simultaneously, thereby increasing the area of a water inlet section and accelerating the drainage of the surface water. According to the floor drain for same floor drainage without descending floor of the building in the present invention, an inner wall of the bottom of the lower accumulated water collection tank of the floor drain body is higher than or level with an inner wall of a bottom of the accumulated water discharge port, so that when surface water enters the accumulated water discharge port, a certain level difference can be formed, and the surface water can directly flow into a drainage concentrator having a water sealing function and a maintenance function without passing through a water seal, thereby greatly improving the unobstruction of drainage. An area of a drainage section of the accumulated water discharge port level with a horizontal section of a top surface of the lower accumulated water collection tank of the floor drain body is greater than or equal to 450 mm 2 and less than 3500 mm 2 , thereby guaranteeing that the floor drain has relatively large drainage discharge. According to the floor drain for same floor drainage without descending floor of the building in the present invention, a support protruding from an outer wall is arranged at the bottom of the lower accumulated water collection tank, and when the accumulated water discharge port is horizontal, a bottom of the support is above 5 mm lower than a bottom of the accumulated water discharge port, thereby guaranteeing that a certain slope is formed by the accumulated water discharge port and a pipeline connecting the accumulated water discharge port so that accumulated water is not retained in the pipeline, and guaranteeing that a water flow has a certain speed. A distance from the bottom of the support to a top surface of the lower upstream face of the floor drain cover is greater than 10 mm and less than 70 mm, so that the floor drain for same floor drainage can be directly embedded in a cushion, a leveling layer and a decorative layer of the building, thereby achieving a using effect of not descending the floor. According to the floor drain for same floor drainage without descending floor of the building in the present invention, a distance from the closed bottom of the lower accumulated water collection tank of the floor drain body to a top surface of the lower attaining surface of the floor drain cover is greater than 10 mm and less than 60 mm, and thus, the area of a flowing section of the accumulated water discharge port can be increased on the premise of applying to a condition of not descending the floor. According to the floor drain for same floor drainage without descending floor of the building in the present invention, when the inner wall of the closed bottom of the lower accumulated water collection tank centers on the accumulated water discharge port, a middle is lower and two sides are higher, so that a water flow having certain kinetic energy can be rapidly formed when only a little quantity of accumulated water enters the lower accumulated water collection tank on the ground, so that the lower accumulated water collection tank is not deposited, thereby improving a drainage effect. According to the floor drain for same floor drainage without descending floor of the building in the present invention, more than one slot is arranged on the lower accumulated water collection tank; more than one clamping groove is arranged on the lateral accumulated water collection tank; more than one convex point corresponding to the slot is formed on the lower attaining surface of the floor drain cover; or more than one slot is arranged on the lateral accumulated water collection tank; more than one clamping groove is arranged on the lower accumulated water collection tank; and a convex point corresponding to the slot is formed on the lateral attaining surface of the floor drain cover. Therefore, when the convex point is inserted into the slot, the floor drain cover can be fixed to the floor drain body or separated from the floor drain body for blockage removal and maintenance by applying a certain force to the floor drain cover in a position of the clamping groove. According to floor drain for same floor drainage without descending floor of the building in the present invention, a plane greater than 50 mm is formed at the bottom of the support, and when the floor drain for same floor drainage is installed, the floor drain for same floor drainage placed on the ground can be guaranteed not to fall toward one side when the lower accumulated water collection tank has a lower middle and two higher sides."},"cpc_label":{"kind":"string","value":"E03F50407"},"filing_date":{"kind":"string","value":"20170929"},"patent_issue_date":{"kind":"string","value":"20180605"},"date_published":{"kind":"string","value":"20180125"},"examiner_id":{"kind":"string","value":"80742.0"},"ipc_label":{"kind":"string","value":"E03F504"},"npe_litigated_count":{"kind":"number","value":0,"string":"0"},"examiner_full_name":{"kind":"string","value":"SCHNEIDER, CRAIG M"},"invention_title":{"kind":"string","value":"FLOOR DRAIN FOR SAME FLOOR DRAINAGE WITHOUT DESCENDING FLOOR OF BUILDING"},"small_entity_indicator":{"kind":"string","value":"SMALL"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"E03F"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32891,"cells":{"application_number":{"kind":"number","value":15721589,"string":"15,721,589"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"OUTLET BOX"},"abstract":{"kind":"string","value":"A utility box for mounting at least in part within a wall for use with a fluid carrying supply pipe, the box comprising, a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls, a bottom wall aperture in the bottom wall sized for extending the pipe through the bottom wall aperture with the pipe terminating in a free end portion positioned within the interior of the housing at a location above the bottom wall, a valve attachable to the free end portion of the pipe, the junction of the valve and the pipe being within the interior of the housing above the bottom wall, and a first seal positioned to provide a fluid-tight seal between the bottom wall and the pipe to prevent fluid within the interior of the housing from passing out of the interior of the housing through the bottom wall aperture."},"claims":{"kind":"string","value":"1. A utility box for mounting at least in part within a wall for use with a fluid carrying supply pipe, the box comprising: a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls; a bottom wall aperture in the bottom wall sized for extending the pipe through the bottom wall aperture with the pipe terminating in a free end portion positioned within the interior of the housing at a location above the bottom wall; a valve attachable to the free end portion of the pipe, the junction of the valve and the pipe being within the interior of the housing above the bottom wall; and a first seal positioned to provide a fluid-tight seal between the bottom wall and the pipe to prevent fluid within the interior of the housing from passing out of the interior of the housing through the bottom wall aperture. 2. A utility box mounted at least in part within a wall, the box comprising: a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls; a bottom wall aperture in the bottom wall; a fluid carrying supply pipe extending through the bottom wall aperture and terminating in a free end portion within the interior of the housing at a location above the bottom wall; a valve attached to the free end portion of the pipe, the junction of the valve and the pipe being within the interior of the housing above the bottom wall; a first seal providing a fluid-tight seal between the bottom wall and the pipe to prevent fluid within the interior of the housing from passing out of the interior of the housing through the bottom wall aperture; and a second seal providing a fluid-tight seal between the free end portion of the pipe and the valve. 3. The utility box of claim 2, further comprising: a manifold positioned to provide a fluid path between the free end portion of the pipe and the valve, the manifold having a lower connecting portion, an upper connecting portion and a side connecting portion positioned between the lower and upper connecting portions, with the lower connecting portion being connected in a fluid-tight arrangement to the free end portion of the pipe and one of the upper and side connecting portions being connected in a fluid-tight arrangement to the valve. 4. The utility box of claim 3 for use with a fitting having a push-fit connector, wherein one of the upper and side connecting portions is a tube sized for having the push-fit connector pressed thereon. 5. The utility box of claim 4, wherein the lower connecting portion comprises a push-fit connector sized for being pressed onto the free end portion of the pipe. 6. The utility box of claim 3 for use with an arrestor assembly, wherein valve is connected to the side connecting portion and the upper connection portion is configured for connection to the arrestor assembly. 7. The utility box of claim 2, further comprising: a manifold positioned to provide a fluid path between the free end portion of the pipe and the valve, the manifold having a lower connecting portion and an upper connecting portion, with the lower connecting portion being connected in a fluid-tight arrangement to the free end portion of the pipe and the upper connecting portions being connected in a fluid-tight arrangement to the valve. 8. A utility box for mounting at least in part within a wall for use with an in-wall drain pipe and a drain-fluid source conduit transporting a drain fluid for entry into the drain pipe, the box comprising: a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls; a bottom wall aperture in the bottom wall sized to be placed in fluid communication with the drain pipe; a drain including a drain base positioned within the bottom wall aperture and in fluid-tight communication with the drain pipe, and a retaining member for removable attachment to the drain base for retaining the drain-fluid source conduit in place relative to the drain base for communication of the drain fluid into the drain base. 9. A method of mounting a utility box at least in part within a wall, the method comprising: providing a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls, the bottom wall having a bottom wall aperture; extending a fluid carrying supply pipe through the bottom wall aperture and an positioning a free end portion of the pipe within the interior of the housing at a location above the bottom wall; attaching a valve to the free end portion of the pipe with the junction of the valve and the pipe being within the interior of the housing above the bottom wall; positioning a first seal between the bottom wall and the pipe to provide a fluid-tight seal prevent fluid therebetween to prevent fluid within the interior of the housing from passing out of the interior of the housing through the bottom wall aperture; and positioning a second seal between the free end portion of the pipe and the valve to provide a fluid-tight seal therebetween."},"description":{"kind":"string","value":"RELATED APPLICATIONS This application claims benefit of U.S. Provisional Application No. 62/402,896, filed on Sep. 30, 2016, the entire disclosures and content of which are hereby incorporated by reference in their entirety. FIELD OF INVENTION The invention relates to outlet boxes for mounting in a wall, and more particularly, to outlet boxes having a housing with one or more apertures for installing fixtures for utilities, such as water. BACKGROUND Utility outlet boxes may be installed in building walls to provide access and/or disposal points for utilities, such as water. In one application, outlet boxes may be installed within building walls during the construction or renovation, and pipes and/or fixtures may be connected to the outlet boxes. Leaks that develop in the outlet box, such as in the connected pipes and/or fixtures connected thereto, may be difficult to discover because water drains out of the outlet box. Water leaking in the outlet box may drain or otherwise intrude into interior portions of the surrounding wall potentially causing mold or water damage. Additionally, even if the leak is discovered, removal of a portion of the wall or removal of the outlet box from the wall or may be required to repair or discover the offending leak. Accordingly, there is a need for an outlet box that prevents water leaks from intruding into the surrounding building walls, that increases detectability of leaks, and that improves ease of repair of leaky fixtures and/or pipes connected to the outlet box. Previously-implemented outlet boxes may also be difficult to mount to building walls and may not be securely attached when mounted thereto. For example, some currently existing methods for attachment of outlet boxes include securing the outlet boxes using straps. However, straps may require access to the rear of the outlet box during installation, and not provide adequate structural support for the outlet box alone. There is therefore the need for an apparatus that facilitates an easier and more secure means of mounting the outlet boxes within building walls. Previously-implemented outlet boxes are also configured for use in a single application, such as installing a water fixture for supplying water to an appliance. Installation of additional boxes may be necessary to provide additional drains, an air admittance valve, or additional water supply valves, for example. Therefore, currently existing outlet boxes do not provide sufficient versatility for installing different combinations of fixtures. Further, previously-implemented outlet boxes do not easily accommodate attachment of differently sized pipes or different fixtures, and do not allow for pipes and/or fixtures to be connected to the outlet boxes at different positions. For example, a pipe above an outlet box may need to be routed to the underside of the utility box because the top of the utility box does not include an appropriate receptacle for receiving the pipe. Even when the previously-implemented outlet box installed in the building wall has an appropriately located receptacle for receiving a pipe (e.g., at the bottom), the receptacle may not be appropriately sized for connecting the pipe. The previously-implemented may not allow for installation of fixtures having differently sized attachment portions. BRIEF DESCRIPTION OF THE DRAWINGS FIG. 1 illustrates a perspective view of a utility box according to a first embodiment. FIG. 2 illustrates a first exploded view of the utility box of FIG. 1. FIG. 3 illustrates a second exploded view of the utility box of FIG. 1. FIG. 4 illustrates a third exploded view of the utility box of FIG. 1. FIG. 5 illustrates a front view of a box main housing of the utility box of FIG. 1. FIG. 6 illustrates a top plan view of the box main housing of FIG. 5. FIG. 7 illustrates a bottom plan view of the box main housing of FIG. 5. FIG. 8A illustrates an enlarged cross-sectional view substantially along line 1A-1A of the box main housing of FIG. 5. FIG. 8B illustrates an enlarged cross-sectional view substantially along line 1B-1B of the box main housing of FIG. 5. FIG. 9 illustrates an enlarged cross-sectional view substantially along line 1A-1A of a support receptacle of the box main housing of FIG. 5. FIG. 10 illustrates a right side view of the box main housing of FIG. 5. FIG. 11 illustrates a rear view of the box main housing of FIG. 5. FIG. 12 illustrates an enlarged cross-sectional view substantially along line 1A-1A of a second upper receptacle of the box main housing of FIG. 5. FIG. 13A illustrates a bottom perspective view of a box main housing according to a second embodiment. FIG. 13B illustrates a front view of a box main housing according to a third embodiment. FIG. 13C illustrates a bottom perspective view of the box main housing of FIG. 13B. FIG. 14A illustrates a bottom perspective view of the box main housing of FIG. 5 positioned against an interior side of a building wall and having a pipe inserted into a second lower receptacle thereof. FIG. 14B illustrates a cross-sectional view of a lower wall of the box main housing of FIG. 14A taken along line 1-1 of FIG. 5. FIG. 15 illustrates a front perspective view of the lower wall of the box main housing of FIG. 5. FIG. 16A illustrates a front view of a first manifold body of a valve assembly. FIG. 16B illustrates a left side view of the first manifold body of FIG. 16A. FIG. 17 illustrates a cross-sectional view of the first manifold body of FIG. 16A substantially along line 2-2. FIG. 18 illustrates a bottom view of a manifold spacer. FIG. 19 illustrates a cross-sectional view of the manifold spacer of FIG. 18 substantially along line 3-3. FIG. 20A illustrates a front view of a second manifold body of the valve assembly. FIG. 20B illustrates a left side view of the second manifold body of FIG. 20A. FIG. 21 illustrates a cross-sectional view of the second manifold body of FIG. 20A substantially along line 4-4. FIG. 22 illustrates a cross-sectional view of a liquid flow switch and a bushing assembly installed in the second manifold body of FIG. 20A substantially along line 4-4, and having a port interface and a C-clip attached to the second manifold body. FIG. 23 illustrates a bottom plan view of an end bushing of the bushing assembly of FIG. 22. FIG. 24 illustrates a side view of the end bushing of FIG. 23. FIG. 25 illustrates a cross-sectional view of the end bushing of FIG. 23 along the line 5-5. FIG. 26 illustrates a side view of a port of the second manifold body of FIG. 20A. FIG. 27 illustrates a side view of the port interface of FIG. 22. FIG. 28 illustrates a cross-sectional view of the port interface of FIG. 27. FIG. 29 illustrates a plan view of the C-clip of FIG. 22. FIG. 30A illustrates a top plan view of a manifold support ferrule. FIG. 30B illustrates a cross-sectional view of the manifold support ferrule of FIG. 30B along the line 6-6. FIG. 31 illustrates the utility box of FIG. 1 equipped with a pair of valve assemblies and a drain assembly. FIG. 32 illustrates a front view of a drain base of the drain assembly of FIG. 31. FIG. 33 illustrates a right side view of the drain base. FIG. 34 illustrates a cross-sectional view of the drain base of FIG. 32 substantially along line 7-7. FIG. 35 illustrates a top perspective view of a retaining member of the drain assembly of FIG. 31. FIG. 36 illustrates a top rear perspective view of a mounting bracket and a pipe supportably attaching the utility box of FIG. 1 to wall studs and an adjacent second utility box. FIG. 37 illustrates a top rear perspective view of the mounting bracket and the pipe of FIG. 36 supportably attaching a utility box according to a second embodiment to wall studs. FIG. 38 illustrates a perspective view of the mounting bracket of FIG. 36. FIG. 39 illustrates a front view of the mounting bracket of FIG. 36. FIG. 40 illustrates a side view of the mounting bracket of FIG. 36. FIG. 41 illustrates a perspective view of a pipe support bracket attached to a pipe according to a first embodiment. FIG. 42 illustrates a perspective view of a collar of the pipe support bracket of FIG. 41. FIG. 43 illustrates a rear perspective view of a brace of the pipe support bracket of FIG. 41. FIG. 44 illustrates a front perspective view of a brace of the pipe support bracket of FIG. 41. FIG. 45 illustrates a perspective view of a second collar of a pipe support bracket according to a second embodiment of the pipe support bracket. FIG. 46 illustrates a cross-sectional view of the pipe support bracket of FIG. 45. FIG. 47 illustrates a perspective view of the pipe support bracket of FIG. 45. FIG. 48 illustrates a front view of a utility box having a plurality of valve assemblies installed therein, and provided with partially transparent and partial sectional views of some of the valve assemblies. FIG. 49 illustrates a cross-sectional view of the utility box of FIG. 48 taken substantially along line 8-8. FIG. 50 illustrates an enlarged cross-sectional view of a water valve assembly installed in the utility box of FIG. 48 taken substantially along line 8-8. FIGS. 51-93 illustrate additional embodiment of the utility box and its component parts similar to those shown in FIGS. 1-50. DETAILED DESCRIPTION A utility box 10 according to a first embodiment is shown in FIG. 1. The utility box 10 is configured to be installed in the wall of a residential or commercial building to provide one or more access and/or disposal points for utilities. The utility box 10 may be comprised of a rigid waterproof material, such as plastics, polymers, or polyvinyl chloride (PVC); however, other similar materials are contemplated. In this first embodiment, the utility box 10 is configured to provide water access and disposal points for appliances, such as washing machines, dishwashers and ice makers; however, those of ordinary skill in the art will recognize that the configuration of the utility box may be suitable for other applications. The utility box 10 includes a box main housing 12 having a generally three-dimensional square or rectangular outer shape, as shown in FIGS. 5, 6, 7, 8A, 10 and 11. A forwardly opening cavity portion 14 is defined by housing walls 16 extending rearwardly from an opening 18 and terminating at a rear wall 20. The housing walls 16 are comprised of a lower wall 22, an upper wall 24 opposite to the lower wall, and opposing left and right sidewalls 26L and 26R, as shown in FIG. 5. The opening 18 is sized to allow a user's hand to reach into the cavity portion 14 for operation, installation and removal of water valves and drains therein, as described below. The utility box 10 includes one or more receptacles for connecting a water pipe to the utility box, and for installation of a water supply valve or drain, such as a valve assembly 28 shown in FIGS. 1, 2, 3, and 4. A pair of laterally offset first lower receptacles 30 is disposed on the lower wall 22, as shown in FIGS. 5, 7, 8B, and 11. The lower receptacles 30 each include an annular wall 32 circumferentially extending around a removable circular knockout portion 34, as shown in FIGS. 7 and 8B. The knockout portion 34 is at least partially joined or connected to the lower wall 22 by two narrow bridge portions 36 extending radially inward from the annular ring to the knockout portion, as shown in FIGS. 3 and 9. The bridge portions 36 are located at 180° from one another around the knockout portion 34. The knockout portion 34 may include an outer portion 37 having a thickness less than the annular wall 32, the outer portion extending around the circumference of the knockout portion 34 between the bridge portions 36 and connecting the knockout portion to the annular wall 32. The outer portion 37 may have a tapered or angular cross-sectional shape that tapers radially inward from an upper surface to a lower surface of the knockout portion 34. The knockout portion 34 may be removed by cutting through all or most of the outer portion 37, using a utility knife or blade for example, without severing the bridge portions 36. The remaining bridge portions 36 may be broken after severing the outer portion to prevent unintentional loss of the knockout portion within the wall or a pipe. The bridge portions 36 may act as pivot points about which the knockout portion 34 may be rotated to increase strain in, and thereby weaken, the bridge portions. After rotating the knockout portion 34 about the bridge portions 36, the user may grip the knockout portion and sever the bridge portions 36 to remove the knockout portion from the utility box 10 without the dropping it into a wall or pipe below. Removal of the knockout portion 34 creates an aperture 33 defined by the surrounding annular wall 32, the aperture being sized and shaped to receive a corresponding part, such as a pipe, having a known size and shape. In other embodiments, an air gap may space the annular wall 32 apart from the knockout portion 34 instead of having the outer portion 37 therebetween. A pilot guide 38 is provided to guide a drill bit through a center the bottom side of the knockout portion to create an aperture of a desired size therein for receiving a pipe or hose, as shown in FIG. 8B. The pilot guide 38 may be a hole or divot extending partially or completely through the center of the knockout portion 34. The lower receptacles 30 include a cylindrical sidewall portion 40 extending downwardly from a lower surface 42 of the lower wall 22 around the annular wall 32 and defining a cavity 44 therein. The design of the receptacles (e.g., lower receptacles 30) and associated components prevents water from leaking therethrough and into the wall containing the utility box 10. Installation of the pipe and associated components are now described with reference to FIGS. 48, 49, and 50. First, an upper end of a pipe 35 is inserted through the aperture 33 of the lower receptacle 30 to extend between the cavity portion 14 and a lower side of the lower wall 22. An O-ring 46 may be positioned around the pipe 35 below the lower wall 22 and against or abutting the annular wall 32. The O-ring 46 is sized and shaped to resiliently and radially compress between the outer diameter of the pipe 35 and the inner diameter of the cylindrical sidewall portion 40, thereby forming a fluid-tight seal around the pipe 35 at the lower surface of the annular wall 32. A metallic gripper ring 48 having circumferentially spaced axially and radially inwardly protruding teeth (described in U.S. Pat. No. 6,464,266, which is incorporated herein in its entirety by reference) may be installed around the pipe 35 beneath the O-ring 46 to help retain the O-ring within the cavity 44. When the pipe 35 is inserted through the gripper ring 48, the inwardly protruding teeth of the gripper ring 48 bend in the direction of insertion, and dig into or press inwardly against the outer diameter of the pipe 35. For instance, the teeth of the gripper ring 48 may bend downwardly when the pipe 35 is inserted downwardly through the aperture 33. The pipe 35 may be rotated in a first direction (e.g., clockwise) relative to the gripper ring 48 to score the outer diameter of the pipe 35 and prevent further movement of the pipe 35 through the gripper ring 48. The gripper ring 48 may have a larger diameter than the inner diameter of the sidewall portion 40 so as to abut a lower side of the sidewall portion 40. In some embodiments, the gripper ring 48 may be fixed to the bottom of the sidewall portion 40 using adhesives or sonic welding, by way of non-limiting example. When the pipe 35 is inserted through the aperture 33, the O-ring 46, and the gripper ring 48, as described above, the pipe 35 is maintained in fluid-tight attachment to the box main housing 12. Thereafter, a valve assembly 28 or other assembly may be installed over the upper end of the pipe 35 within the cavity portion 14, as described below. If the valve assembly 28 leaks or breaks, or water otherwise accumulates within the cavity portion 14, the O-ring 46 sealed around the pipe 35 prevents liquid from leaking through the aperture 33 and into the wall. The inside of the building walls is thereby protected from leaks within or around the utility box 10, and leaking water will pool within the cavity portion 14 providing a visual indication of a leak. Moreover, a leaky valve assembly 28 may be removed and replaced without removal of the building wall or the box main housing 12 from the wall. Thus, the valve assembly 28 may be easily removed or replaced without extensive cost or effort. The utility box 10 may be provided with the pipe 35 installed in the fluid-tight configuration. Alternatively, the pipe 35 may be installed in the fluid-tight configuration on site. In some embodiments, one or more second lower receptacle 52 having a different configuration than the first lower receptacles 30 may also be disposed on the lower wall 22, as shown in FIGS. 7 and 8A. The second lower receptacle 52 may have a larger outer diameter than the first lower receptacles 30 to allow for attachment of a pipe 67 having a larger diameter than the pipe 35. A second sidewall 54 having a cylindrical shape with a larger diameter than the sidewall 40 extends downwardly from the lower wall 22 to define a downwardly opening cavity 56. The second sidewall 54 may have a length extending downwardly farther than the sidewall 40. The second lower receptacle 52 may include one or more removable knockout portions for installing a pipe and/or a water supply or drain. For example, an annular first knockout portion 58 of the second lower receptacle 52 is located radially inward of the second sidewall 54. The first knockout portion 58 may be connected to the lower surface 22 by an outer portion 59 and a plurality of the bridge portions 61 substantially similar to those described above, except that there may be a different number of bridge portions than two. For example, the second lower receptacle 52 may have four bridge portions 61 spaced apart at 90° from one another around the perimeter of the first knockout portion 58. The first knockout portion 58, including all portions of the second lower receptacle 52 located radially inward thereof, by severing the bridge portions 61 and the outer portion 59. The second lower receptacle 52 may include a second knockout portion 60 located radially inward from the first knockout portion 58. The second knockout portion 60 may include a circular plate 62 having a radial wall thickness greater than the first knockout portion. The second knockout portion 60 may be connected to the first knockout portion 58 by a plurality of the bridge portions 63 and/or the outer portion in the manner described above. The circular plate 62 is removable from the second lower receptacle 52 without also removing the first knockout portion 58. In particular, a pipe 67 having a similar inner diameter to the first knockout portion 58 may be inserted upward into the cavity 56 and abutting against a lower surface of the first knockout portion 58, as shown in FIGS. 14A and 14B. The first knockout portion 58 is sized such that it is too large to fall into the pipe 67 when the knockout portion 58 is severed or removed from the box main housing 12. The outer portion 37 between the second knockout portion 60 and the first knockout portion 58 may be broken or severed to remove the second knockout portion 60. A blade or other tool may be used to cut along at least some of the outer portion 37, and a user may push or pull the second knockout portion 60 to further separate the second knockout portion 60 and the first knockout portion 58 along the outer portion 37. The bridge portion(s) 36 is thicker than the outer portion 37, and designed so that it may not be broken when the outer portion 37 is severed so as to prevent the second knockout portion 60 from falling into the pipe below the receptacle. After breaking the outer portion 37, the user may then grip the second knockout portion 60 and break the remaining bridge portion 36 to separate the second knockout portion 60 from the second lower receptacle 52 without removing the first knockout portion 58. Thereafter, a drain assembly may be installed in the second lower receptacle 52 through the cavity portion 14 of the utility box 10. The box main housing 12 may include a feature providing a guide or outline 69 indicating where to cut to remove a knockout portion, as shown in FIG. 15. The guide 69 may be an annular recess disposed on an upper surface of the lower wall 22 in the cavity portion 14, and coaxially located with the knockout portions of the second lower receptacle 52 (or other receptacles). The guide 69 in the present embodiment is circumferentially located along the outer diameter of the first knockout portion 58. A user may insert the tip of a blade in and cut along the guide 69 to remove the knockout portion 58 and the portions radially inward therefrom. Therefore, the knockout portion 58 may be removed after the utility box 10 is installed in a building wall or without requiring access to the lower surface of the lower wall 22. In some embodiments, the guide 69 may include an outline or indication provided on the upper surface of the lower wall 22. There may be a plurality of concentrically-located guides 69 on each receptacle for which the guides are provided. For example, there may be another guide 69 located between the first knockout portion 58 and the second knockout portion 60 (i.e. located along the outer portion 59) for removing the second knockout portion 60 while leaving the first knockout portion 58 installed. One or more of the other receptacles (e.g., first lower receptacle 30) may be provided with one or more of the guides 69 for removing knockout portions. Referring to FIG. 8A, the second lower receptacle 52 may also include a pilot guide 64 similar to the pilot guide 38 described above extending partially or completely through the center of the plate section 62, providing a pilot hole or divot to guide a drill bit to drill upwardly through the bottom side of the knockout portion to create an aperture of a desired size therein. The second lower receptacle 52 may further include a third lower receptacle 66 disposed at the center of the plate section 62. The third lower receptacle 66 may be substantially similar in structure and/or size to the first lower receptacle 30. That is, the third lower receptacle 66 may include an annular wall surrounding a removable circular knockout portion, and a cylindrical sidewall portion extending downwardly from a lower surface of the plate section 62 in a structure substantially similar to the lower receptacles 30. The second lower receptacle 52 may have more knockout portions 65 disposed radially inward of the first knockout portion 58 and the second knockout portion 60, as shown in FIG. 14B. The differently sized knockout portions of the second lower receptacle allow for connection of differently sized pipes or hoses to the utility box 10. A pair of laterally offset first upper receptacles 68 may be disposed on the upper wall 24, as shown in FIG. 6. The first upper receptacles 68 may allow for pipes and valves to be connected to an upper side of the utility box 10. The first upper receptacles 68 may have a similar configuration to the first lower receptacles 30. In particular, each of the first upper receptacles 68 may include a knockout portion 70 substantially similar to the knockout portions 34 described above and two narrow bridge portions 72 extending radially inward from the upper wall 24 to the knockout portion 70. The knockout portion 70 may include an outer portion 71 having a thickness less than the upper wall 24 and extending around the circumference of the knockout portion 70 between the bridge portions 72 and connecting the knockout portion to the upper wall 24. The outer portion 71 may have a tapered or angular shape tapering radially inward toward an upper surface of the knockout portion 70. In other embodiments, the outer portion 71 may be omitted and an air gap may separate the knockout portion 70 from the upper wall 24. The center of the knockout portion 70 may include a pilot guide substantially similar to the pilot guide 38. In some embodiments, the first upper receptacles may each include a cylindrical sidewall portion extending upwardly from the upper wall 24 around the connecting ring (or air gap) in a manner similar to the sidewall portion 40. A second upper receptacle 74 may be disposed on a central portion of the upper wall 24. The second upper receptacle 74 may have a plurality of concentrically arranged knockout portions arranged in a “bullseye” configuration for connecting pipes and/or fixtures having different sizes at the upper wall 24, as shown in FIGS. 6, 8A, and 12. For example, the second upper receptacle 74 may include a first knockout portion 76 having a largest outer diameter, a second knockout portion 78 having an outer diameter positioned radially inward of an inner diameter of the first knockout portion, and a third knockout portion 80 having an outer diameter positioned radially inward of an the second knockout portion. The upper wall 24 is connected to the first knockout portion 76 by an outer portion 81 and a pair of narrow radially extending first bridge portions 82, which are similar to the bridge portions 36 and located at 180° from one another around the outer circumference of the first knockout portion. The outer portion 81 has a thickness less than the first knockout portion 76 and extends circumferentially around the first knockout portion. The outer portion 81 may have a tapered or angular cross-sectional shape that tapers radially inward from lower surface to an upper surface of the knockout portion 76. Each of the plurality of concentrically arranged knockout portions may be connected by circumferentially offset bridge portions. The first knockout portion 76 is connected to the second knockout portion 78 by an outer portion 83 and a pair of second bridge portions 84 similar to the bridge portions 36, but each of which are circumferentially offset relative to one of the first bridge portions 82 around at 120° (and conversely −60° to the other of the first bridge portions). The second knockout portion 78 is connected to the third knockout portion 80 by an outer portion 85 and a pair of third bridge portions 86 similar to the bridge portions 36, but each of which are circumferentially offset relative to one of the second bridge portions 84 at 120°. The outer portions 83 and 85 have a structure similar to the outer portion 81 describe above, as shown in FIG. 12. Circumferentially offsetting the bridge portions 82, 84, 86 from one another allows a user to remove an inner knockout portion without removal of an adjacent outer knockout portion, thereby adjusting the circumference of an aperture of the second upper receptacle 74 for installation a pipe or fixture having approximately the same outer circumference. To remove the third knockout portion 80, a user may sever the outer portion 85, then grip the third knockout portion and sever or forcibly break the bridge portions 86. A pipe or fixture having an outer circumference similar to the inner circumference of the second knockout portion 78 may be inserted through the aperture left by the removed third knockout portion 80. An upper surface of the third knockout portion 80 may include a pilot guide substantially similar to the pilot guide 36 described above for drilling an aperture of a desired size in the second upper receptacle 74. The configuration of the lower and/or upper receptacles of the utility box 10 allow for attachment of different fixtures, valves and drains thereto, and to facilitate simple and secure connection of pipes and/or hoses to the different fixtures, valves and drains. Although three receptacles for attaching fixtures are provided on each of the upper wall 24 and lower wall 22 of the box main housing 12, a different number of receptacles may be provided in other embodiments. For example, a box main housing 13A may be provided having four second lower receptacles 52, as shown in FIG. 13A. Accordingly, two separate drain assemblies and two separate water valve assemblies, described below, may be attached to the box main housing, allowing for greater variation in uses and configurations. For example, a dishwasher and ice maker, each using a single water supply assembly and a single drain assembly, may be attached at the same outlet box instead of having two separate outlet boxes. A different number of receptacles may be provided in other embodiments. For instance, a box main housing 13B is shown in FIGS. 13B and 13C having three lower receptacles 52. Each of the lower receptacles 52 may include one of the third lower receptacles 66 (see FIG. 13C) for installing a pipe and/or a valve, as described below. Different configurations of drains and/or valves may be installed in the box main housing 13B. A drain assembly may be installed in each of the leftmost one and center one of the receptacles 52 shown in FIG. 13C, and a water supply valve may be installed in the rightmost one of the receptacles 52, by way of non-limiting example. Therefore, a user may configure the box main housings 13A and 13B according to the application, or the most convenient access to the supply or drain pipe. In one aspect, water supply valves 28 may be installed in the first lower receptacles 30, as shown in FIGS. 1, 31, 48, 49 and 50. During installation of the utility box 10 in a building wall, the knockout portions 34 are removed leaving an aperture through which the pipe 35 may be inserted. Referring to FIGS. 2 and 50, an upper end of the pipe 35 may be inserted through a metallic gripper ring 48 having circumferentially spaced axially and radially inwardly protruding teeth described in U.S. Pat. No. 6,464,266, which is incorporated herein in its entirety by reference. The upper end of the pipe 35 may then be inserted through the O-ring 46 and through the aperture of the lower first receptacle, positioning the upper end of the pipe 35 above the lower wall 22 within the cavity portion 14 of the housing main box 12. The O-ring 46 is positioned within the cylindrical sidewall 40 near or against the lower surface 42 of the lower wall 22. Thereafter, the valve assembly 28 may be installed over the upper end of the pipe 35 in the cavity portion 14. The valve assemblies may be installed in the upper receptacles of the box main housing 12, as shown in FIG. 48, for example. The valve assembly 28 is a “push-fit” assembly comprising components that lock into place when a male component is pushed or inserted into a female component without threaded attachment. The valve assembly 28 includes a substantially L-shaped hollow outlet 90 with a rearwardly extending receiving tube 90T for sealably connecting with a push-fit tube 88T of a manifold 88, as shown in FIG. 2, 3, or 31, or sealably connecting with a pipe 35, as shown in FIGS. 48, 49, and 50. The manifold 88 may be a component of the valve assembly 28 comprising a substantially T-shaped or L-shaped hollow body having a lower connecting portion 88L, as shown in FIGS. 16A, 16B, 17. The manifold 88 and/or outlet 90 may be push-fit components that are monolithically formed by an injection molding process using a polymer material, such as chlorinated polyvinyl chloride (CPVC) or PVC. An upper end of the manifold 88 may include an upper connecting portion 88U for threadably attaching a water arrestor assembly, as described below. The tube 88T extends outwardly from a side of the manifold 88 providing a push-fit connection point for attaching the outlet 90. The single-piece injection-molded manifold 88 eliminates joints or seams that may leak or fail in other devices, and provides a monolithic attachment point for connecting different outlets in a push-fit manner. A manifold spacer 92 may be installed within the cavity portion 14 between the lower wall 22 and the lower connecting portion 88L to space them apart at an appropriate distance according to the length of the end of the pipe 35. As shown in FIGS. 18 and 19, the manifold spacer 92 has an annular upper portion 92U having an outer circumference sized to snuggly fit into the lower end of the lower connecting portion 88L, and a cylindrical lower portion 92L having a circumference larger than the upper portion 92U and sized equal to or larger than the bottom of the lower connecting portion 88L. An upwardly facing ledge 92L of the manifold spacer 92 abuts a lower surface of the lower connecting portion 88L of the manifold 88 when the upper portion 92U is inserted therein. The cylindrical lower portion 92L has a plurality of axially offset and radially inwardly extending guide ribs or ridges 92R for guiding the end of the pipe 35 through the manifold spacer and into the manifold 88. A length of the tube 88T of the manifold 88 may be inserted into a cavity 90A of the receiving tube 90T of the outlet 90 to connect the manifold 88 and the outlet 90. A bushing assembly 93 may be nested or installed at least partially within the cavity 90A of the receiving tube 90T to facilitate water-tight fluid communication between the manifold 88 and the outlet 90, as shown in FIG. 22. The bushing assembly 93 allows for a push-fit assembly of the outlet 90 (or other similar outlet) to the manifold 88 (or the pipe 35). The bushing assembly 93 may include one or more O-rings, one or more gripper rings, and an end bushing 94. The end bushing 94 has a body portion 94B sized and shaped to fit against inner surfaces within the cavity 90A, an inner cavity extending axially through the end bushing 94, and a rear flange portion 90F that abuts a rearward surface of the receiving tube 90T, as shown in FIGS. 23, 24 and 25. The flange portion 94F may include a plurality of recesses 94R axially offset and radially positioned along a rearward surface of the flange portion 90F. One or more of the recesses 94F may engage with a thin fin portion 88F projecting forwardly from and extending vertically along a forward surface of the manifold 88 (see FIGS. 16B and 17) to allow secure rotational movement between the manifold 88 and the outlet 90 without failure of the fluid-tight seal therebetween. The end bushing 94 may further include a plurality of axially offset ridges or ribs 94T projecting radially inward in the inner cavity 94C to guide the tube 88T within the cavity 90A. The outlet 90 has an elongated downwardly extending port 96 extending downwardly from the receiving tube 90T, as shown in FIGS. 20A, 20B, and 21, for sealably connecting and supplying water to a hose of an appliance. The port 96 has a substantially cylindrical shape extending in an axial direction, and an inner conduit portion in fluid communication with the receiving tube 90T and terminating at the lower end, as shown in FIG. 26. An upper portion 96U of the port 96 may have a flared portion 96F flaring outward circumferentially and upwardly. An exterior surface of the cylindrical shape of the port 96 may have one or more circumferentially extending grooves 96G positioned axially along the length of the port 96 for receiving and retaining one or more O-rings. The grooves 96G may have a square cross-sectional shape for securely retaining the O-ring. A lower end portion 96L of the port 96 may include a tapered portion 97 narrowing or tapering inwardly toward the lower end of the port 96. A lower groove or annular recess 96R having a rounded concave cross-sectional shape is provided axially below the grooves 96G for receiving a C-shaped ring described below. The port 96 includes a center portion 96C between the grooves 96G and the recess 96R, which narrows or tapers downwardly toward the lower end portion 96L. In other embodiments, the exterior surface of the port 96 may include a threaded portion to facilitate direct connection of the hose of the appliance to the valve assembly 28. In one aspect, a port interface 98 may be provided for attaching to the hose of an appliance to the port 96, as shown in FIGS. 22 and 27. The port interface 98 may be positioned over the port 96 and attached thereto, allowing for attachment of the hose of the appliance to the valve assembly 28. The port interface 98 has an inner conduit 98C defined by downwardly extending sidewalls 98S extending axially therethrough from an upper end 98U to a lower end 98L of the port interface, a threaded attachment portion 98T for threadably attaching to the hose, and one or more rings 98R projecting circumferentially from an exterior surface of the sidewalls 98S at an axial position above the threaded portion 98T. The inner conduit 98C has a section with an inner contour sized and shaped to snuggly engage with the exterior surface shape of the port 96. Specifically, the inner conduit 98C includes an inwardly projecting annular portion 98A projecting radially inwardly from the inner surfaces of the sidewall 98S. The annular portion 98A may have an angled or tapered upwardly facing surface configured to engage with a downwardly facing surface of the tapered portion 97 of the port 96 when inserted into the inner conduit 98C. The bottom side of the annular portion 98A may have a curved or flat shaped lower portion 99 for retaining a retaining ring, as described below. A resiliently compressible C-shaped clip or retaining ring 101 (see FIG. 29) may be installed in the recess 96R to supportably attach the port interface 98 the port 96, as shown in FIG. 22. Different port interfaces 98 having different outer sidewall diameters may be provided to allow for hoses of different sizes to the valve assembly 28. Moreover, the port interface 98 helps to prevent over-torqueing and/or cracking of the outlet 90 of the valve assembly 28. To attach the port 96 to the port interface 98, the lower end of the port 96 is first inserted into the upper end of the inner conduit 98C of the port interface. The port interface 98 is moved axially upward over the exterior surface of the sidewalls 98S of the port 96 until the annular portion 98A of the port interface 98 is positioned snuggly against a downwardly facing surface of the center portion 96C. O-rings positioned in the grooves 96G axially above center portion 96C may compress against the inner surface of the sidewalls 98S to seal the inner conduit 98C against the outer diameter of the port 96 in a fluid-tight manner. The flared portion 96F of the port fits snuggly against an outwardly opening portion 98W at an upper end 98U, thereby preventing further downward movement of the port 96 within the port interface 98. The c-shaped ring 101 may then be inserted upwardly into the inner conduit 98C of the port interface 98 and installed within the recess 96R. The c-shaped retaining ring 101 installed within the recess 96R abuts the lower portion 99 of the annular portion 98A, preventing separation of the port interface 98 from the port 96. After the port interface 98 is attached to the port 96 in the manner described above, water supplied from a water source attached to the pipe 35 may flow through the valve assembly 28, out of the lower end of the port 96, and through a hose attached to the lower end 98L of the port interface 98. The valve assembly 28 may include other features, such as an arrestor assembly 102 at the upper connecting portion 88U of the manifold 88, and a push-pull liquid flow valve stem 104 at a front of the outlet 90. The flow valve stem 104 may be user-actuated to a first position (e.g., rearward “on” position) that allows fluid flow through the second manifold body 88, and a second position blocking fluid flow through the second manifold body 88 (e.g., forward “off” position). The arrestor assembly 102 is a dampening mechanism that absorbs kinetic energy of fluid flowing into the valve assembly 28 when the flow valve stem 104 is transitioned from the first position to the second position. Specifically, when the flow valve stem 104 is transitioned from the first position to the second position, a sudden pressure change of fluid flowing through the valve assembly may cause vibration in the valve assembly 28 or the pipes in the wall leading to the valve assembly due to overshoot in the system (i.e., “water hammer”). The arrestor assembly 102 has a sliding piston mechanism for absorbing the kinetic energy of the fluid during the transition between positions, thereby reducing or preventing vibration in the system. A cylindrical arrestor lower portion 102L of the arrestor assembly 102 threadably engages with the upper connecting portion 88U to allow fluid communication between the piston of the arrestor assembly 102 and the tube 88T of the manifold 88. According to one aspect, the valve assembly 28 may further include a metallic manifold support ferrule 106 configured to fit over an outer cylindrical portion of the upper connecting portion 88U of the manifold 88 to reduce hoop stresses on the manifold 88 and prevent over-torqueing of the arrestor lower portion 102L against the manifold 88, as shown in FIGS. 2, 3, and 4. The support ferrule 106 includes a cylindrical portion 106C extending in an axial direction, and an upper annular portion 106R extending radially inward from an upper end of the cylindrical portion 106C, as shown in FIGS. 30A and 30B. The cylindrical portion 106C has an outer cylindrical portion 106C with an inner diameter slightly larger (˜1.10″) than an outer diameter of the upper connecting portion 88U (˜1.06″). The plastic or polymer material (e.g., PVC) of the manifold 88 may experience significant hoop or cylinder stresses induced by fluctuations of water pressure flowing therethrough to and from the arrestor assembly 102, which may cause the manifold 88 to crack and/or fail over time. The metallic material (e.g., aluminum, copper, steel) of the support ferrule 106 has significantly higher tensile strength than the plastic or polymer material of the manifold 88. The cylindrical portion 106C absorbs at least some of the hoop or cylindrical stresses induced on the manifold 88 by pressure differentials of water flowing therethrough, thereby reducing cracks and/or failures in the manifold 88 and improving its longevity. When the support ferrule 106 is assembled with the manifold 88, the cylindrical portion 106C of the support ferrule 106 is positioned over the cylindrical outer body of the upper connecting portion 88U and the annular portion 106R is positioned against the upper surface of the manifold 88. The lower portion 102L of the arrestor assembly 102 may then be inserted through the annular portion 106R and threadably engaged with the upper connecting portion 88U of the manifold 88. The annular portion 106R has an inner diameter approximately equal to or slightly larger than the diameter of an uppermost opening of the inner tube 88T at the upper connecting portion 88U. The arrestor assembly 102 may abut an upper surface of the annular portion 106R when the lower portion 102L is threadably engaged with the upper connecting portion 88U of the manifold 88. In some embodiments, an O-ring may be positioned between and abutting the upper surface of the annular portion 106R and the arrestor assembly 102 to help create a fluid-tight seal for fluid communication between the manifold 88 and the arrestor assembly 102. Fixtures other than the valve assembly 28 may be installed in the utility box 10. In one embodiment, a drain assembly 108 is provided that may be installed in the utility box 10, as shown in FIG. 31. The drain assembly 108 includes a drain base 110 that may be installed in the second lower receptacle 52 of the box main housing 12 and a retaining member 112 for retaining a hose and/or funneling liquid into the drain base 110. The drain base 110 includes a hollow cylindrical base portion 114 defining a drain channel, a curved rear wall portion 116 extending upwardly from the base portion 114, and a pair of laterally offset attachment apertures 118 for removably attaching the retaining member 112 to the drain base 110, as shown in FIGS. 32, 33, and 34. A drain tube or hose, such as a condensation hose from an air conditioning unit, may be inserted through the first upper receptacle 68 or the second upper receptacle 74 and into the cavity portion 14, where the drain tube may be attached to the retaining member 112 or inserted into the drain base 110. Additionally, a drain tube from an appliance, such as a dishwasher or washing machine, may be inserted through the opening 18 of the box main housing 12 and into the drain base 110. The cylindrical base portion 114 is sized and shaped for insertion into the first knockout portion 58 of the second lower receptacle 52 after the second knockout portion 60 is removed, as described above. Specifically, a recess 120 extends upwardly from a bottom of the base portion 114 along a front side and a rear side thereof. The front and rear recesses 120 create laterally offset curved sidewalls 122 that may flex laterally or radially inward when the cylindrical base portion 114 is inserted into the second lower receptacle 52 to frictionally retain the drain base 110 therein. The cylindrical base portion 114 may have a tapered shape tapering radially inward from an upper end to a lower end thereof. The cylindrical base portion 114 has a diameter sufficient to allow for insertion of one or more drain tubes. A rim portion 124 may protrude radially outward from the outer circumference of the cylindrical base portion 114 and have an outer dimension or radius larger than the inner diameter of the first knockout portion 58. The rim portion 124 may abut with an upper surface of the lower wall 22 when the cylindrical base portion 114 is inserted into the second lower receptacle 52, preventing further insertion of the drain base 110 therein. One or more hoses or tubes may be inserted into the cylindrical base portion 114 for draining fluid into a pipe attached to a lower side of the second lower receptacle 52. Referring to FIG. 35, the retaining member 112 is configured to retain a hose or tube thereto and drain fluids downwardly into the drain base 110 to which the retaining member is attached. The retaining member 112 includes a bracket portion 126 having bracket sidewalls 126S extending forwardly from a bracket rear wall 126R, a drain conduit 128 having a major surface extending downwardly at an angle from the bracket portion 126, and a hose retention post 130 projecting upwardly from the drain conduit 128 for retaining a drain hose or tube to the retaining member 112. A pair of laterally offset attachment members 132 each project from a rearward facing side of the bracket rear wall 126R. The attachment members 132 may be inserted into corresponding ones of the attachment apertures 118 to removably attach the retaining member 112 to the rear wall portion 116 of the drain base 110. The vertical position of the retention post 130 may be adjusted by moving the retaining member vertically along the rear wall portion 116 according to the length of the hose or tube extending downwardly into the cavity portion 14 from the upper wall 24 of the box main housing 12. Specifically, the attachment apertures 118 may have an elongated shape extending downwardly along the rear wall portion 116 of the drain base 110. The position of the attachment members 132 within the elongated attachment apertures 118 may be adjusted to select the vertical position of the retaining member 112 along the rear wall portion 116 and thereby select the vertical position of the retention post 130. The attachment members 132 may each have a curved shape curving laterally outward toward left and right lateral sides of the retaining member 112. The outwardly curved attachment members 132 press against the lateral outward sides of the attachment apertures 118 when the attachment members 132 are inserted therein to frictionally retain the vertical position of the retaining member 112 within the rear wall portion 116. The end of a drain hose or tube may be positioned around and snuggly fitted over the retention post 130 to attach the drain tube to the retaining member 112. After the drain tube is attached to the retaining member 112 of the drain assembly 108, liquid draining from the drain hose flows rearward along and drips from the drain conduit 128 onto the rear wall portion 116 and/or into the base portion 114 to drain from a drain pipe attached to the second lower receptacle 52. The retention post 130 has a conical or tapered shape tapering inwardly and upwardly from the drain conduit 128 to allow for snug attachment of drain hoses having different inner diameters. The retention post 130 comprises a plurality of fin members 130F (e.g., four) extending radially outward from a central portion 130C of the retention post 130, which allows liquid to flow freely from the attached drain hose onto the drain conduit 128. The bracket sidewalls 126S may extend downwardly along laterally sides of the drain conduit 128 to help guide liquid flow onto the rear wall portion 116 and/or into the base portion 114 and prevent liquid from spilling into the cavity portion 14. The utility box 10 may include several features for securely attaching the box main housing 12 within a building wall. For example, a support receptacle 134 on a rear side of the box main housing 12 is provided for supportably attaching the box main housing 12 to a pipe or tube 136, as shown in FIGS. 8, 9, 10, 11, 36, and 37. The support receptacle 134 in the current embodiment is a rearwardly-opening channel or groove extending horizontally along the entire rear side of the box main housing 12. The cross-sectional shape of the support receptacle 134 channel or groove may include opposing parallel upper and lower receptacle walls 134U and 134L leading to a semi-circular front wall portion 134W centered about an axis 134A, as shown in FIGS. 8A and 9. The cross-sectional shape of the support receptacle 134 is sized to receive a pipe 136 having an outer diameter equal to or less than a standard diameter, such as 0.675″ (⅜″) or less. A protuberance 134P may protrude downwardly from the upper receptacle wall 134U and/or protrude upwardly from the lower receptacle wall 134L to help retain the pipe 136 inserted in the support receptacle 134. The pipe 136 to which the box main housing 12 attaches may be a pre-existing or previously installed pipe in the building wall. However, it is unlikely that a previously installed pipe in the building will be optimally positioned for attachment of the box main housing 12 thereto. A pair of mounting brackets 138 are therefore provided for optimally positioning and installing a length of pipe 136 between opposing wall studs 139 or other opposing surfaces of the building wall, as shown in FIGS. 36 and 37. After the mounting brackets 138 are attached to opposing studs with the length of pipe 136 extending therebetween, the box main housing 12 may be mounted in the wall studs by pressing the housing inward to insert the length of pipe 136 within the support receptacle 134. The mounting brackets 138 have a substantially flat bracket main body 140 having a first section 142 at a first end 144 of the bracket main body 140, a second section 146 extending from a side of the first section 142 opposite to the first end 144 and terminating at a second end 148, and a pipe retaining member 150 for mounting the pipe 136 to the mounting bracket 138, as shown in FIGS. 38, 39, and 40. The first section 142 is a rectangular portion extending in a width direction of the main body 140 and the second section 146 is a rectangular portion extending in a length direction of the bracket main body 140 from a central portion of the side of the first section 142. The first end 144 of the bracket main body 140 has a substantially flat edge with a width wider than a substantially flat edge of the second end 148 opposite to the first end 144. Holes 149 extend through the thickness of the bracket main body 140 for receiving screws or nails therein to supportably mount the bracket main body 140 to a stud. In the present embodiment, there is a pair of holes 149 positioned on lateral sides of the first section 142; however, the position and/or number of holes 149 may vary in other embodiments, such as an additional hole positioned along the second section 146 or at the second end 148. The retaining member 150 is sized and shaped to be inserted into the open end of the length of pipe 136. The length of pipe 136 extends between the pair of mounting brackets attached to the opposing faces of the two opposing wall studs 136 for supportably mounting the support receptacle 134 of the box main housing 12, as shown in FIG. 40. The retaining member 150 is a support projecting outward orthogonally from a first surface 140F of the flat bracket main body 140. The retaining member 150 in the present embodiment has a plurality of fin members 150F (e.g., four) extending radially outward from a central portion 150C. The cross-sectional area of the retaining member 150 is sized to snuggly fit a pipe 136 having a known inner diameter, such as 0.49 inches. The fin members 150F may each have a tapered or angular shape tapering or angled inwardly from the first surface 140F of the bracket main body 140 to a tip 150T of the retaining member 150. The tapered or angular shape may allow attachment of different sized pipes 136 to the mounting bracket 138. In some embodiments, the retaining member 150 may instead have a cylindrical or conical shape without fin members 150F. The mounting brackets 138 are configured to allow the user to position the pipe 136 such that the front 21 of the box main housing 12 will be flush with the forward edge of the wall stud 139. Specifically, affixing the mounting brackets 138 to the wall stud 139 in a certain orientation depending on the standard size of the wall stud will ensure that the front of the box main housing 12 will be flush with the forward edge of the wall stud 139, without measuring the position of the mounting brackets 138 or box main housing 12. According to construction industry standards, the dimensions of wall studs 139 dimensions are typically either approximately 1.5 inches thick by 3.5 inches wide (i.e., “2×4 size”) or approximately 1.5 inches thick by 5.5 inches wide (i.e., “2×6 size”). A central axis C of the retaining member 150 is offset along a length of the mounting bracket 138 at a first distance D1 from the first end 144 of the mounting bracket and at a second distance D2 from the second end 148 of the mounting bracket, as shown in FIGS. 39 and 40. In the current embodiment, for example, the first distance D1 is approximately 0.315 inches and the second distance D2 is approximately 2.315 inches (for a 0.63 inch outer diameter pipe). The mounting brackets 138 should be installed on the wall studs 139 in a first orientation if the wall stud 139 is of the 2×4 size and in a second orientation if the wall stud 139 is of the 2×6 size. In the first orientation, the first end 144 is positioned flush with the rearward side 139R of the 2×4 size wall studs 139 and the second and 148 oriented facing forward toward the forward side 139F of the wall studs 139 opposite to the rearward side 139R, as shown in FIGS. 36 and 37. In the second orientation, the second end 148 is positioned flush with the rearward side 139R of the 2×6 size wall studs 139 and the first end 144 is oriented facing forward toward the forward side of the wall studs 139 opposite to the rearward side 139R. In either case, the central axis C of the pipe 136 extending between the opposing wall studs 139 will be offset from the forward side of the wall studs 139 at approximately the same distance L. In this instance, the distance L is the distance between the front 21 of the box main housing 12 and the center axis 134A of the support receptacle 134 (see FIGS. 8A and 9). The distance L in the current embodiment may be approximately 3.2 inches, for example. The box main housing 12 may include flanges 151 projecting outwardly from lateral sides 26L, 26R of the box main housing, as shown in FIGS. 6, 7, and 11. A front surface of the flanges 151 may be flush with the front 21 of the main box 12 for abutting inwardly facing surfaces of the building walls. The flanges 151 may have screw or nail holes extending therethrough for affixing the box main housing to the building walls. In some embodiments, the flanges 151 may be spaced at the distance L from the center axis 134A of the support receptacle 134 and rearwardly offset from the front 21 of the box main housing 12. Accordingly, when the box main housing 12 is installed and mounted using the mounting brackets 138 described above, the front 21 of the box main housing 12 may project through a hole in the building wall with the flanges 151 positioned flush against the inwardly facing surfaces of the building walls. Mounting tabs 152 are disposed on box lateral sides 26L and 26R near or at the rear wall 20 for affixing the box main housing 12 to the wall studs 139, as shown in FIGS. 6, 11, and 36. The mounting tabs 152 are thin, flat portions having a mounting aperture 154 extending therethrough for receiving a fastener, such as a screw or a nail. The mounting apertures 154 in some embodiments may be elongated slots leading to a rearwardly opening mouth portion at a rear edge of the mounting tabs 152 for slideably receiving the shank of a fastener driven into the wall stud 139. If desired, the box main housing 12 may be affixed to the wall studs by driving a fastener through the mounting apertures 154 and into the wall studs 139, or by sliding the shank of a fastener into the rearwardly opening mouth portion of the elongated slot mounting apertures 154. The rearward edge of the mounting tabs 152 may be flush with or may not extend beyond the back surface of the rear wall 20, thereby reducing the amount of space required to affix the box main housing 12 to wall studs 139 within the building wall. A mounting recess 158 may be disposed in the rear wall 20 on an inwardly facing side of the mounting tab 152 for receiving the head and/or the shank of a fastener. The mounting tabs 152 are disposed at corners of the rear wall 20 in the present embodiment, although the mounting tabs may be disposed between corners on lateral sides of the rear wall 20 in other embodiments. The mounting recesses 156 may include a mouth portion opening upwardly along the upper wall 24 or downwardly along the lower wall 22 to facilitate insertion of a fastener therein. Pipe support brackets are provided for supportably attaching one pipe to another pipe. A pipe support bracket 160 includes a first collar 162 attachable to a first pipe 164, and a brace 166 for attaching a second pipe 168 to the first collar 162, as shown in FIG. 41. The first collar 162 has a C-shaped or semi-circular collar body 170 with opposing ends 170A and 170B spaced apart by an opening 172, as shown in FIG. 42. The first collar 162 has first attachment portions 174A and 174B projecting in parallel away from the ends 170A and 170B, then inwardly toward each other. Each first attachment portion has a latch element 176 protruding from an outwardly facing surface thereof. The collar body 170 is comprised of a resilient material, such as metal, PVC or polymer, that is flexible to space the ends 170A and 170B further apart for inserting the first pipe 164 into the collar body though the opening 172. The brace 166 has an elongated U-shape comprising a pair of brackets 178 extending in parallel with each other outwardly from a base portion 180, as shown in FIGS. 43 and 44. Each of the brackets 178 has a semi-circular or C-shaped pipe receptacle 182 having an opening 184 for receiving the second pipe 168 therein. Both of the pipe receptacles 182 are aligned with each other along a first direction (e.g., length) of the base portion 180 to supportably and firmly retain a length of the second pipe 168 in an orientation along the first direction. The base portion has a pair of collar receptacles 186 each sized and shaped for receiving a corresponding one of the first attachment portions 174A and 174B therein. The collar receptacles 186 may be apertures or recesses disposed on sidewall portions 180S of the base portion 180. A catch 188 located outwardly adjacent to each of the collar receptacles 184 is provided for retaining the attachment portions 174A and 1746 inserted in the adjacent collar receptacle. Specifically, the catch 188 is a resiliently flexible member configured to be flexed or bent outwardly by the latch element 176 when the first attachment portion 174A and 174B is inserted into the collar receptacle 186. The catch 188 is configured to then rebound inwardly back to its original position when the latch element 176 is inserted beyond an inward edge of the catch 188, thereby helping to block or prevent removal of the attachment portion 174A and 1746 from the collar receptacle 186 when inserted therein. In another embodiment, a second collar 190 having a different configuration than the first collar 162 is provided for attaching to the brace 166, as shown in FIGS. 45, 46, and 47. The second collar 190 is sized and shaped for attaching, in conjunction with the brace 166, to a pipe 194 having a smaller diameter than the pipe 164. The second collar 190 has a concave or U-shaped collar body 192 extending in an axial direction. The second collar body 192 has a curved or round rear wall 192R, and may have sidewall portions 192S extending in parallel with each other in a direction orthogonal to the axial direction. End portions 192A and 192B at ends of the second collar body 192 each flare outwardly away from each other. Attachment portions 196A and 1966 project in parallel from the end portions 192A and 1926, then inwardly toward each other. The attachment portions 196A and 1966 are spaced apart by an opening 198 for receiving the pipe 194 within the second collar body 192. The second collar 190 is attachable to the brace 166 by engaging the attachment portions 196A and 1966 with the openings 184 of the brace 166 in a manner substantially identical to the attachment portions 174A and 174B described above. The base portion 180 of the brace 166 attached to the second collar 192 opposes the rear wall 192R and may abut a side of the second pipe 194 to help prevent or reduce movement or vibration of the second pipe therein. FIGS. 51-93 illustrate additional embodiment of the utility box and its component parts similar to those shown in FIGS. 1-50 and described above. Embodiments of the present disclosure can be described in view of the following clauses: 1. A utility box for mounting at least in part within a wall for use with a fluid carrying supply pipe, the box comprising: a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls; a bottom wall aperture in the bottom wall sized for extending the pipe through the bottom wall aperture with the pipe terminating in a free end portion positioned within the interior of the housing at a location above the bottom wall; a valve attachable to the free end portion of the pipe, the junction of the valve and the pipe being within the interior of the housing above the bottom wall; and a first seal positioned to provide a fluid-tight seal between the bottom wall and the pipe to prevent fluid within the interior of the housing from passing out of the interior of the housing through the bottom wall aperture. 2. A utility box mounted at least in part within a wall, the box comprising: a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls; a bottom wall aperture in the bottom wall; a fluid carrying supply pipe extending through the bottom wall aperture and terminating in a free end portion within the interior of the housing at a location above the bottom wall; a valve attached to the free end portion of the pipe, the junction of the valve and the pipe being within the interior of the housing above the bottom wall; a first seal providing a fluid-tight seal between the bottom wall and the pipe to prevent fluid within the interior of the housing from passing out of the interior of the housing through the bottom wall aperture; and a second seal providing a fluid-tight seal between the free end portion of the pipe and the valve. 3. The utility box of clauses 1 or 2, further comprising: a manifold positioned to provide a fluid path between the free end portion of the pipe and the valve, the manifold having a lower connecting portion, an upper connecting portion and a side connecting portion positioned between the lower and upper connecting portions, with the lower connecting portion being connected in a fluid-tight arrangement to the free end portion of the pipe and one of the upper and side connecting portions being connected in a fluid-tight arrangement to the valve. 4. The utility box of any of clauses 1-3 for use with a fitting having a push-fit connector, wherein one of the upper and side connecting portions is a tube sized for having the push-fit connector pressed thereon. 5. The utility box of any of clauses 1-4, wherein the lower connecting portion comprises a push-fit connector sized for being pressed onto the free end portion of the pipe. 6. The utility box of any of clauses 1-5 for use with an arrestor assembly, wherein valve is connected to the side connecting portion and the upper connection portion is configured for connection to the arrestor assembly. 7. The utility box of any of clauses 1-6, further comprising: a manifold positioned to provide a fluid path between the free end portion of the pipe and the valve, the manifold having a lower connecting portion and an upper connecting portion, with the lower connecting portion being connected in a fluid-tight arrangement to the free end portion of the pipe and the upper connecting portions being connected in a fluid-tight arrangement to the valve. 8. A utility box for mounting at least in part within a wall for use with an in-wall drain pipe and a drain-fluid source conduit transporting a drain fluid for entry into the drain pipe, the box comprising: a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls; a bottom wall aperture in the bottom wall sized to be placed in fluid communication with the drain pipe; a drain including a drain base positioned within the bottom wall aperture and in fluid-tight communication with the drain pipe, and a retaining member for removable attachment to the drain base for retaining the drain-fluid source conduit in place relative to the drain base for communication of the drain fluid into the drain base. 9. A method of mounting a utility box at least in part within a wall, the method comprising: providing a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, first side, second side and back walls, the bottom wall having a bottom wall aperture; extending a fluid carrying supply pipe through the bottom wall aperture and an positioning a free end portion of the pipe within the interior of the housing at a location above the bottom wall; attaching a valve to the free end portion of the pipe with the junction of the valve and the pipe being within the interior of the housing above the bottom wall; positioning a first seal between the bottom wall and the pipe to provide a fluid-tight seal prevent fluid therebetween to prevent fluid within the interior of the housing from passing out of the interior of the housing through the bottom wall aperture; and positioning a second seal between the free end portion of the pipe and the valve to provide a fluid-tight seal therebetween. The foregoing described embodiments depict different components contained within, or connected with, different other components. It is to be understood that such depicted architectures are merely exemplary, and that in fact many other architectures can be implemented which achieve the same functionality. In a conceptual sense, any arrangement of components to achieve the same functionality is effectively “associated” such that the desired functionality is achieved. Likewise, any two components so associated can also be viewed as being “operably connected,” or “operably coupled,” to each other to achieve the desired functionality. While particular embodiments of the present invention have been shown and described, it will be obvious to those skilled in the art that, based upon the teachings herein, changes and modifications may be made without departing from this invention and its broader aspects and, therefore, the appended claims are to encompass within their scope all such changes and modifications as are within the true spirit and scope of this invention. Furthermore, it is to be understood that the invention is solely defined by the appended claims. It will be understood by those within the art that, in general, terms used herein, and especially in the appended claims (e.g., bodies of the appended claims) are generally intended as “open” terms (e.g., the term “including” should be interpreted as “including but not limited to,” the term “having” should be interpreted as “having at least,” the term “includes” should be interpreted as “includes but is not limited to,” etc.)."},"background":{"kind":"string","value":"<SOH> BACKGROUND <EOH>Utility outlet boxes may be installed in building walls to provide access and/or disposal points for utilities, such as water. In one application, outlet boxes may be installed within building walls during the construction or renovation, and pipes and/or fixtures may be connected to the outlet boxes. Leaks that develop in the outlet box, such as in the connected pipes and/or fixtures connected thereto, may be difficult to discover because water drains out of the outlet box. Water leaking in the outlet box may drain or otherwise intrude into interior portions of the surrounding wall potentially causing mold or water damage. Additionally, even if the leak is discovered, removal of a portion of the wall or removal of the outlet box from the wall or may be required to repair or discover the offending leak. Accordingly, there is a need for an outlet box that prevents water leaks from intruding into the surrounding building walls, that increases detectability of leaks, and that improves ease of repair of leaky fixtures and/or pipes connected to the outlet box. Previously-implemented outlet boxes may also be difficult to mount to building walls and may not be securely attached when mounted thereto. For example, some currently existing methods for attachment of outlet boxes include securing the outlet boxes using straps. However, straps may require access to the rear of the outlet box during installation, and not provide adequate structural support for the outlet box alone. There is therefore the need for an apparatus that facilitates an easier and more secure means of mounting the outlet boxes within building walls. Previously-implemented outlet boxes are also configured for use in a single application, such as installing a water fixture for supplying water to an appliance. Installation of additional boxes may be necessary to provide additional drains, an air admittance valve, or additional water supply valves, for example. Therefore, currently existing outlet boxes do not provide sufficient versatility for installing different combinations of fixtures. Further, previously-implemented outlet boxes do not easily accommodate attachment of differently sized pipes or different fixtures, and do not allow for pipes and/or fixtures to be connected to the outlet boxes at different positions. For example, a pipe above an outlet box may need to be routed to the underside of the utility box because the top of the utility box does not include an appropriate receptacle for receiving the pipe. Even when the previously-implemented outlet box installed in the building wall has an appropriately located receptacle for receiving a pipe (e.g., at the bottom), the receptacle may not be appropriately sized for connecting the pipe. The previously-implemented may not allow for installation of fixtures having differently sized attachment portions."},"summary":{"kind":"string","value":"<SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>FIG. 1 illustrates a perspective view of a utility box according to a first embodiment. FIG. 2 illustrates a first exploded view of the utility box of FIG. 1 . FIG. 3 illustrates a second exploded view of the utility box of FIG. 1 . FIG. 4 illustrates a third exploded view of the utility box of FIG. 1 . FIG. 5 illustrates a front view of a box main housing of the utility box of FIG. 1 . FIG. 6 illustrates a top plan view of the box main housing of FIG. 5 . FIG. 7 illustrates a bottom plan view of the box main housing of FIG. 5 . FIG. 8A illustrates an enlarged cross-sectional view substantially along line 1 A- 1 A of the box main housing of FIG. 5 . FIG. 8B illustrates an enlarged cross-sectional view substantially along line 1 B- 1 B of the box main housing of FIG. 5 . FIG. 9 illustrates an enlarged cross-sectional view substantially along line 1 A- 1 A of a support receptacle of the box main housing of FIG. 5 . FIG. 10 illustrates a right side view of the box main housing of FIG. 5 . FIG. 11 illustrates a rear view of the box main housing of FIG. 5 . FIG. 12 illustrates an enlarged cross-sectional view substantially along line 1 A- 1 A of a second upper receptacle of the box main housing of FIG. 5 . FIG. 13A illustrates a bottom perspective view of a box main housing according to a second embodiment. FIG. 13B illustrates a front view of a box main housing according to a third embodiment. FIG. 13C illustrates a bottom perspective view of the box main housing of FIG. 13B . FIG. 14A illustrates a bottom perspective view of the box main housing of FIG. 5 positioned against an interior side of a building wall and having a pipe inserted into a second lower receptacle thereof. FIG. 14B illustrates a cross-sectional view of a lower wall of the box main housing of FIG. 14A taken along line 1 - 1 of FIG. 5 . FIG. 15 illustrates a front perspective view of the lower wall of the box main housing of FIG. 5 . FIG. 16A illustrates a front view of a first manifold body of a valve assembly. FIG. 16B illustrates a left side view of the first manifold body of FIG. 16A . FIG. 17 illustrates a cross-sectional view of the first manifold body of FIG. 16A substantially along line 2 - 2 . FIG. 18 illustrates a bottom view of a manifold spacer. FIG. 19 illustrates a cross-sectional view of the manifold spacer of FIG. 18 substantially along line 3 - 3 . FIG. 20A illustrates a front view of a second manifold body of the valve assembly. FIG. 20B illustrates a left side view of the second manifold body of FIG. 20A . FIG. 21 illustrates a cross-sectional view of the second manifold body of FIG. 20A substantially along line 4 - 4 . FIG. 22 illustrates a cross-sectional view of a liquid flow switch and a bushing assembly installed in the second manifold body of FIG. 20A substantially along line 4 - 4 , and having a port interface and a C-clip attached to the second manifold body. FIG. 23 illustrates a bottom plan view of an end bushing of the bushing assembly of FIG. 22 . FIG. 24 illustrates a side view of the end bushing of FIG. 23 . FIG. 25 illustrates a cross-sectional view of the end bushing of FIG. 23 along the line 5 - 5 . FIG. 26 illustrates a side view of a port of the second manifold body of FIG. 20A . FIG. 27 illustrates a side view of the port interface of FIG. 22 . FIG. 28 illustrates a cross-sectional view of the port interface of FIG. 27 . FIG. 29 illustrates a plan view of the C-clip of FIG. 22 . FIG. 30A illustrates a top plan view of a manifold support ferrule. FIG. 30B illustrates a cross-sectional view of the manifold support ferrule of FIG. 30B along the line 6 - 6 . FIG. 31 illustrates the utility box of FIG. 1 equipped with a pair of valve assemblies and a drain assembly. FIG. 32 illustrates a front view of a drain base of the drain assembly of FIG. 31 . FIG. 33 illustrates a right side view of the drain base. FIG. 34 illustrates a cross-sectional view of the drain base of FIG. 32 substantially along line 7 - 7 . FIG. 35 illustrates a top perspective view of a retaining member of the drain assembly of FIG. 31 . FIG. 36 illustrates a top rear perspective view of a mounting bracket and a pipe supportably attaching the utility box of FIG. 1 to wall studs and an adjacent second utility box. FIG. 37 illustrates a top rear perspective view of the mounting bracket and the pipe of FIG. 36 supportably attaching a utility box according to a second embodiment to wall studs. FIG. 38 illustrates a perspective view of the mounting bracket of FIG. 36 . FIG. 39 illustrates a front view of the mounting bracket of FIG. 36 . FIG. 40 illustrates a side view of the mounting bracket of FIG. 36 . FIG. 41 illustrates a perspective view of a pipe support bracket attached to a pipe according to a first embodiment. FIG. 42 illustrates a perspective view of a collar of the pipe support bracket of FIG. 41 . FIG. 43 illustrates a rear perspective view of a brace of the pipe support bracket of FIG. 41 . FIG. 44 illustrates a front perspective view of a brace of the pipe support bracket of FIG. 41 . FIG. 45 illustrates a perspective view of a second collar of a pipe support bracket according to a second embodiment of the pipe support bracket. FIG. 46 illustrates a cross-sectional view of the pipe support bracket of FIG. 45 . FIG. 47 illustrates a perspective view of the pipe support bracket of FIG. 45 . FIG. 48 illustrates a front view of a utility box having a plurality of valve assemblies installed therein, and provided with partially transparent and partial sectional views of some of the valve assemblies. FIG. 49 illustrates a cross-sectional view of the utility box of FIG. 48 taken substantially along line 8 - 8 . FIG. 50 illustrates an enlarged cross-sectional view of a water valve assembly installed in the utility box of FIG. 48 taken substantially along line 8 - 8 . FIGS. 51-93 illustrate additional embodiment of the utility box and its component parts similar to those shown in FIGS. 1-50 . detailed-description description=\"Detailed Description\" end=\"lead\"?"},"cpc_label":{"kind":"string","value":"E03C1021"},"filing_date":{"kind":"string","value":"20170929"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180405"},"examiner_id":{"kind":"string","value":"97595.0"},"ipc_label":{"kind":"string","value":"E03C102"},"npe_litigated_count":{"kind":"number","value":0,"string":"0"},"examiner_full_name":{"kind":"string","value":"MURPHY, KEVIN F"},"invention_title":{"kind":"string","value":"OUTLET BOX"},"small_entity_indicator":{"kind":"string","value":"SMALL"},"continuation":{"kind":"number","value":0,"string":"0"},"decision_as_of_2020":{"kind":"string","value":"ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"E03C"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32892,"cells":{"application_number":{"kind":"number","value":15722239,"string":"15,722,239"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"INFORMATION PROCESSING APPARATUS CAPABLE OF ACHIEVING IMPROVED USABILITY, METHOD OF CONTROLLING INFORMATION PROCESSING APPARATUS, NON-TRANSITORY STORAGE MEDIUM ENCODED WITH PROGRAM READABLE BY COMPUTER OF INFORMATION PROCESSING APPARATUS, AND INFORMATION PROCESSING SYSTEM"},"abstract":{"kind":"string","value":"An information processing system includes an operation apparatus and a main body apparatus which is capable of communicating with the operation apparatus. The operation apparatus includes a first transceiver which transmits operation data to the main body apparatus. The main body apparatus includes a memory in which an operation scheme of the operation apparatus is registered, a second transceiver which receives the operation data, and a controller. The controller registers the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the second transceiver indicates a first operation and registers the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the second transceiver indicates a second operation, and performs processing based on the operation scheme registered in the memory onto the operation data received by the second transceiver."},"claims":{"kind":"string","value":"1. An information processing system comprising: an operation apparatus; and a main body apparatus which is capable of communicating with the operation apparatus, the operation apparatus including a first transceiver which transmits operation data representing an operation by a user to the main body apparatus, the main body apparatus including a memory in which an operation scheme of the operation apparatus is registered, a second transceiver which receives the operation data transmitted from the first transceiver, and a controller, the controller registering the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the second transceiver indicates a first operation and registering the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the second transceiver indicates a second operation, and performing processing based on the operation scheme registered in the memory onto the operation data received by the second transceiver. 2. The information processing system according to claim 1, wherein the operation apparatus further includes a first operation portion and a second operation portion, and the controller registers the operation scheme of the operation apparatus in the memory as the first operation scheme when the operation data received by the second transceiver indicates the first operation of the first operation portion and registers the operation scheme of the operation apparatus in the memory as the second operation scheme when the operation data received by the second transceiver indicates the second operation of the second operation portion. 3. The information processing system according to claim 2, wherein the first operation portion and the second operation portion are disposed on different surfaces of a housing of the operation apparatus, respectively. 4. The information processing system according to claim 2, wherein the operation apparatus further includes a third operation portion, and the controller performs processing on operation data of the third operation portion received by the second transceiver differently between the first operation scheme and the second operation scheme registered in the memory. 5. The information processing system according to claim 4, wherein the controller performs prescribed processing on the operation data of the third operation portion received by the second transceiver when the first operation scheme is registered in the memory, and converts the operation data of the third operation portion received by the second transceiver into converted operation data when the second operation scheme is registered in the memory and performs the prescribed processing based on the converted operation data. 6. The information processing system according to claim 5, wherein the operation data of the third operation portion includes direction data representing a direction of input, and the controller performs the prescribed processing on the direction data of the third operation portion received by the second transceiver when the first operation scheme is registered in the memory, and converts the direction data of the third operation portion received by the second transceiver into converted direction data different in direction of input from the direction data when the second operation scheme is registered in the memory and performs the prescribed processing based on the converted direction data. 7. The information processing system according to claim 2, wherein the first and second operation portions are disposed on identical sides of prescribed operation surfaces of a housing of the operation apparatus, respectively when the user performs an operation in any of the first and second operation schemes. 8. The information processing system according to claim 1, wherein a plurality of operation apparatuses are provided, and when a plurality of pieces of the operation data received by the second transceiver indicate the first operation, the controller sets a plurality of operation apparatuses as one set and registers an operation scheme of the set of the operation apparatuses in the memory as the first operation scheme. 9. The information processing system according to claim 8, wherein two operation apparatuses of the plurality of operation apparatuses are set as one set, and the two operation apparatuses constituting the set are designated in advance. 10. The information processing system according to claim 8, wherein the controller registers the operation scheme of the set of the operation apparatuses in the memory as the first operation scheme when the plurality of pieces of operation data received by the second transceiver simultaneously indicate the first operation. 11. An information processing apparatus which is capable of communicating with an operation apparatus comprising: a memory in which an operation scheme of the operation apparatus is registered; a transceiver which receives operation data transmitted from the operation apparatus; and a controller, the controller registering the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the transceiver indicates a first operation and registering the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the transceiver indicates a second operation, and performing processing based on the operation scheme registered in the memory onto the operation data received by the transceiver. 12. A method of controlling an information processing apparatus which is capable of communicating with an operation apparatus, the method comprising: receiving operation data transmitted from the operation apparatus; registering an operation scheme of the operation apparatus in a storage unit as a first operation scheme when the received operation data indicates a first operation; registering the operation scheme of the operation apparatus in the storage unit as a second operation scheme when the received operation data indicates a second operation; and performing processing based on the operation scheme registered in the storage unit onto the received operation data. 13. An information processing system comprising: a first operation apparatus; a second operation apparatus; and a main body apparatus which is capable of communicating with the first operation apparatus and the second operation apparatus, the first operation apparatus and the second operation apparatus each including a first transceiver which transmits operation data representing an operation by a user to the main body apparatus, the main body apparatus including a memory in which operation schemes of the first operation apparatus and the second operation apparatus are registered, a second transceiver which receives the operation data transmitted from the first transceiver, and a controller, the controller setting, when a plurality of pieces of operation data received from the first operation apparatus and the second operation apparatus by the second transceiver indicate a first operation, the first operation apparatus and the second operation apparatus as one set and registering an operation scheme of the set in the memory as a first operation scheme, and registering, when the operation data received from any one of the first operation apparatus and the second operation apparatus by the second transceiver indicates a second operation, the operation scheme of any of the first operation apparatus and the second operation apparatus in the memory as a second operation scheme. 14. The information processing system according to claim 13, wherein each of the first operation apparatus and the second operation apparatus further includes a first operation portion, a second operation portion, and a third operation portion, and the controller registers the operation scheme in the memory as the first operation scheme when the plurality of pieces of operation data received from the first operation apparatus and the second operation apparatus by the second transceiver indicate the first operation of the first operation portion and registers the operation scheme in the memory as the second operation scheme when the operation data received from any one of the first operation apparatus and the second operation apparatus by the second transceiver indicates the second operation of the second operation portion and the third operation portion."},"description":{"kind":"string","value":"Information Processing Apparatus Capable of Achieving Improved Usability, Method of Controlling Information Processing Apparatus, Non-Transitory Storage Medium Encoded With Program Readable by Computer of Information Processing Apparatus, and Information Processing System This nonprovisional application is based on Japanese Patent Application No. 2016-217073 filed with the Japan Patent Office on Nov. 7, 2016, the entire contents of which are hereby incorporated by reference. FIELD The present disclosure relates to an information processing apparatus, a method of controlling an information processing apparatus, a non-transitory storage medium encoded with a program readable by a computer of an information processing apparatus, and an information processing system, and particularly to operation processing by an information processing apparatus. BACKGROUND AND SUMMARY In a game system representing one example of a conventional information processing system, when a game controller representing an operation apparatus is registered in correspondence with a player number, the game controller may be registered by successively performing the same prescribed operation onto each game controller. Selection from among a plurality of operation schemes can be made for an operation apparatus in some cases. In such a case, though an operation scheme should also be registered, successive registration complicates a procedure for registration and there is a room for improvement in usability. The present disclosure is provided to solve the above-described problems and an object thereof is to provide an information processing system which can achieve improved usability, an information processing apparatus, a method of controlling an information processing apparatus, and an information processing program. An information processing system according to one aspect includes an operation apparatus and a main body apparatus which is capable of communicating with the operation apparatus. The operation apparatus includes a first transceiver which transmits operation data representing an operation by a user to the main body apparatus. The main body apparatus includes a memory in which an operation scheme of the operation apparatus is registered, a second transceiver which receives the operation data transmitted from the first transceiver, and a controller. The controller registers the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the second transceiver indicates a first operation and registers the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the second transceiver indicates a second operation, and performs processing based on the operation scheme registered in the memory onto the operation data received by the second transceiver. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. In the exemplary embodiment, the operation apparatus further includes a first operation portion and a second operation portion. The controller may register the operation scheme of the operation apparatus in the memory as the first operation scheme when the operation data received by the second transceiver indicates the first operation of the first operation portion and register the operation scheme of the operation apparatus in the memory as the second operation scheme when the operation data received by the second transceiver indicates the second operation of the second operation portion. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme based on the operation data transmitted from the first operation portion and register the operation scheme of the operation apparatus in the memory as the second operation scheme based on the operation data transmitted from the second operation portion. Therefore, since the operation scheme of the operation apparatus is registered based on the operation data from different operation portions, registration processing can readily be performed and usability can be improved. In the exemplary embodiment, the first operation portion and the second operation portion may be disposed on different surfaces of a housing of the operation apparatus, respectively. Since the first operation portion and the second operation portion are provided on different surfaces of the housing, respectively, registration processing can readily be performed without confusion and usability can be improved. In the exemplary embodiment, the operation apparatus further includes a third operation portion. The controller may perform processing on operation data of the third operation portion received by the second transceiver differently between the first operation scheme and the second operation scheme registered in the memory. The controller can perform appropriate processing in accordance with the operation scheme by performing processing on the operation data of the third operation portion differently between the first operation scheme and the second operation scheme. In the exemplary embodiment, the controller may perform prescribed processing on the operation data of the third operation portion received by the second transceiver when the first operation scheme is registered in the memory, and convert the operation data of the third operation portion received by the second transceiver into converted operation data when the second operation scheme is registered in the memory and perform the prescribed processing based on the converted operation data. When the second operation scheme is registered, the controller converts the operation data into converted operation data and performs prescribed processing based on the converted operation data. Therefore, even when the second operation scheme is registered, it is not necessary to change prescribed processing in accordance with the operation scheme by conversion to converted operation data corresponding to the operation data under the first operation scheme and processing can readily be realized. In the exemplary embodiment, the operation data of the third operation portion includes direction data representing a direction of input. The controller may perform the prescribed processing on the direction data of the third operation portion received by the second transceiver when the first operation scheme is registered in the memory and convert the direction data of the third operation portion received by the second transceiver into converted direction data different in direction of input from the direction data when the second operation scheme is registered in the memory and perform the prescribed processing based on the converted direction data. In the exemplary embodiment, the first and second operation portions may be disposed on identical sides of prescribed operation surfaces of a housing of the operation apparatus, respectively when the user performs an operation under any of the first and second operation schemes. The first and second operation portions are provided on the side of the prescribed operation surface of the housing of the operation apparatus when the user performs an operation under each of the first operation scheme and the second operation scheme so that an intuitive operation in selection of the operation scheme can be performed and usability can be improved. In the exemplary embodiment, a plurality of operation apparatuses are provided, and when a plurality of pieces of the operation data received by the second transceiver indicate the first operation, the controller may set a plurality of operation apparatuses as one set and register an operation scheme of the set of the operation apparatuses in the memory as the first operation scheme. Since the controller can make registration of one set of operation apparatuses in the memory based on a plurality of pieces of operation data transmitted from a plurality of operation apparatuses, registration processing can readily be performed and usability can be improved. In the exemplary embodiment, two operation apparatuses of the plurality of operation apparatuses are set as one set. The two operation apparatuses constituting the set may be designated in advance. By designating in advance two operation apparatuses to constitute a set, management of the operation apparatuses is facilitated and processing can be accelerated. In the exemplary embodiment, the controller registers the operation scheme of the set of the operation apparatuses in the memory as the first operation scheme when the plurality of pieces of operation data received by the second transceiver simultaneously indicate the first operation. Since the controller can make registration of one set of operation apparatuses in the memory when a plurality of pieces of operation data transmitted from a plurality of operation apparatuses simultaneously indicate the first operation, one set of operation apparatuses can easily be distinguished and registration processing can readily be performed. An information processing apparatus which is capable of communicating with an operation apparatus according to one aspect includes a memory in which an operation scheme of the operation apparatus is registered, a transceiver which receives operation data transmitted from the operation apparatus, and a controller. The controller registers the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the transceiver indicates a first operation and registers the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the transceiver indicates a second operation, and performs processing based on the operation scheme registered in the memory onto the operation data received by the transceiver. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. A method of controlling an information processing apparatus which is capable of communicating with an operation apparatus according to one aspect includes receiving operation data transmitted from the operation apparatus, registering an operation scheme of the operation apparatus in a storage unit as a first operation scheme when the received operation data indicates a first operation, registering the operation scheme of the operation apparatus in the storage unit as a second operation scheme when the received operation data indicates a second operation, and performing processing based on the operation scheme registered in the storage unit onto the received operation data. In the registering an operation scheme, the operation scheme of the operation apparatus can be registered in the storage unit as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. A non-transitory storage medium encoded with a program readable by a computer of an information processing apparatus which is capable of communicating with an operation apparatus according to one aspect is provided. The program causes the computer to perform receiving operation data transmitted from the operation apparatus, registering an operation scheme of the operation apparatus in a memory as a first operation scheme when the received operation data indicates a first operation, registering the operation scheme of the operation apparatus in the memory as a second operation scheme when the received operation data indicates a second operation, and performing processing based on the operation scheme registered in the memory onto the received operation data. The computer can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. An information processing system according to one aspect includes a first operation apparatus, a second operation apparatus, and a main body apparatus which is capable of communicating with the first operation apparatus and the second operation apparatus. The first operation apparatus and the second operation apparatus each include a first transceiver which transmits operation data representing an operation by a user to the main body apparatus. The main body apparatus includes a memory in which operation schemes of the first operation apparatus and the second operation apparatus are registered, a second transceiver which receives the operation data transmitted from the first transceiver, and a controller. The controller sets, when a plurality of pieces of operation data received from the first operation apparatus and the second operation apparatus by the second transceiver indicate a first operation, the first operation apparatus and the second operation apparatus as one set and registers an operation scheme of the set in the memory as a first operation scheme, and registers, when the operation data received from any one of the first operation apparatus and the second operation apparatus by the second transceiver indicates a second operation, the operation scheme of any of the first operation apparatus and the second operation apparatus in the memory as a second operation scheme. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. In the exemplary embodiment, each of the first operation apparatus and the second operation apparatus further includes a first operation portion, a second operation portion, and a third operation portion. The controller registers the operation scheme in the memory as the first operation scheme when the plurality of pieces of operation data received from the first operation apparatus and the second operation apparatus by the second transceiver indicate the first operation of the first operation portion and registers the operation scheme in the memory as the second operation scheme when the operation data received from any one of the first operation apparatus and the second operation apparatus by the second transceiver indicates the second operation of the second operation portion and the third operation portion. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. The foregoing and other objects, features, aspects and advantages of the exemplary embodiments will become more apparent from the following detailed description of the exemplary embodiments when taken in conjunction with the accompanying drawings. BRIEF DESCRIPTION OF THE DRAWINGS FIG. 1 is a schematic diagram showing appearance of a game device 1 according to the present embodiment. FIG. 2 is a schematic diagram showing appearance of another manner of game device 1 according to the present embodiment. FIG. 3 is a diagram of a main body apparatus 2 according to the present embodiment when viewed from six sides. FIG. 4 is a diagram of a left controller 3 according to the present embodiment when viewed from six sides. FIG. 5 is a diagram of a right controller 4 according to the present embodiment when viewed from six sides. FIG. 6 is a schematic diagram showing appearance when game device 1 according to the present embodiment is used together with a cradle. FIG. 7 is a block diagram showing an internal configuration of main body apparatus 2 according to the present embodiment. FIG. 8 is a block diagram showing an internal configuration of left controller 3 and right controller 4 according to the present embodiment. FIG. 9 is a diagram showing one example of a manner of use of game device 1 with left controller 3 and right controller 4 being attached to main body apparatus 2. FIG. 10 is a diagram showing one example of a manner of use of game device 1 with left controller 3 and right controller 4 being detached from main body apparatus 2. FIG. 11 is a diagram showing one example of a manner of use of game device 1 with two users each holding one controller in a detached state. FIG. 12 is a diagram showing one example of a manner of use of game device 1 with main body apparatus 2 being attached to a cradle 5. FIGS. 13A and 13B are diagrams showing examples of a manner of use of three or more controllers. FIG. 14 is a diagram showing appearance of an accessory controller 401 based on an embodiment. FIGS. 15A and 15B are diagrams showing examples illustrating a controller registration screen displayed by game device 1 based on the embodiment. FIG. 16 is a diagram illustrating one example of registration information based on the embodiment. FIG. 17 is a diagram illustrating a functional block configuration of main body apparatus 2 based on the embodiment. FIG. 18 is a flowchart illustrating one example of a flow of processing for registration of a controller performed in main body apparatus 2 based on the embodiment. FIGS. 19A to 19C are diagrams illustrating operation data transmitted from the controller based on the embodiment to main body apparatus 2. FIG. 20 is a diagram showing one example of game processing performed by game device 1 based on the embodiment. FIG. 21 is a flowchart illustrating a processing procedure involved with game processing based on the embodiment. DETAILED DESCRIPTION OF NON-LIMITING EXAMPLE EMBODIMENTS This embodiment will be described in detail with reference to the drawings. The same or corresponding elements in the drawings have the same reference characters allotted and description thereof will not be repeated. [A. Information Processing System] An apparatus configuration relating to an information processing system according to the present embodiment will be described. The information processing system according to the present embodiment is configured at least with an information processing apparatus described below. For example, an information processing apparatus may be a portable (also referred to as mobile) device such as a portable game device, a portable telephone, or a smartphone, a stationary apparatus such as a personal computer or a home game console, or a large apparatus such as an arcade game machine. In the present example, a game device representing one example of an information processing apparatus will be described by way of example. Though a game controller provided for a game device will be described in the present example by way of example of an operation apparatus, limitation in particular to a game controller is not intended and any operation apparatus may be applicable so long as it functions as an input device capable of transmitting operation data to an information processing apparatus. (a1: Overall Configuration of Game Device) FIG. 1 is a schematic diagram showing appearance of a game device 1 according to the present embodiment. As shown in FIG. 1, game device 1 includes a main body apparatus 2, a left controller 3, and a right controller 4. Main body apparatus 2 includes a display 12 representing one example of a display portion and performs various types of processing including game processing in game device 1. FIG. 2 is a schematic diagram showing appearance of another manner of game device 1 according to the present embodiment. As shown in FIG. 2, left controller 3 and right controller 4 may be constructed as being detachable from main body apparatus 2. Left controller 3 and right controller 4 may integrally be constructed or left controller 3 and right controller 4 may be constructed as separate apparatuses. Thus, left controller 3 and right controller 4 corresponding to an operation portion may be constructed separately from main body apparatus 2. Left controller 3 can be attached to a left side (a side of a positive direction of an x axis shown in FIG. 1) of main body apparatus 2. Right controller 4 can be attached to a right side (a side of a negative direction of the x axis shown in FIG. 1) of main body apparatus 2. In the description below, left controller 3 and right controller 4 may collectively be referred to as a “controller”. A more specific configuration example of main body apparatus 2, left controller 3, and right controller 4 will be described below. (a2: Structure of Main Body Apparatus) FIG. 3 is a diagram of main body apparatus 2 according to the present embodiment when viewed from six sides. Referring to FIG. 3, main body apparatus 2 has a housing 11 substantially in a form of a plate. A main surface of housing 11 (that is, a front surface or a surface where display 12 is provided) is substantially in a rectangular shape. In the description below, housing 11 is in a horizontally long shape and a longitudinal direction of the main surface (that is, the direction of the x axis shown in FIG. 1) is referred to as a lateral direction (or a left-right direction) and a direction of a short side of the main surface (that is, a direction of a y axis shown in FIG. 1) is referred to as a vertical direction (or an up-down direction). A direction perpendicular to the main surface of housing 11 (that is, a direction of a z axis shown in FIG. 1) is referred to as a direction of depth (or a front-rear direction). Main body apparatus 2 can be used with its main surface being laterally oriented or with its surface being vertically oriented when a user holds the main body apparatus. Therefore, denotation as the lateral direction and the vertical direction is given for the sake of convenience of description. A shape and a size of housing 11 can arbitrarily be designed. For example, in another embodiment, a protrusion portion or a grip portion for facilitating holding by a user may be added to housing 11. (1) Member Provided on Main Surface of Housing 11 As shown in FIGS. 1 to 3, display 12 is provided on the main surface of housing 11 of main body apparatus 2. Display 12 shows an image obtained or generated by main body apparatus 2 (which may be a still image or moving images). When game processing is performed, display 12 shows a virtual space and an object in the virtual space. Though display 12 is typically implemented by a liquid crystal display (LCD), a display apparatus of any type can be adopted. A touch panel 13 is provided on a screen of display 12. Typically, a device of a type accepting a multi-touch input (for example, a capacitance type) is adopted as touch panel 13. For example, a device of any type such as a device of a type accepting a single-touch input (for example, a resistive film type) can be adopted as touch panel 13. Speaker holes 11a and 11b are provided in the main surface of housing 11 of main body apparatus 2 and sound generated from a speaker (a speaker 88 shown in FIG. 7) arranged in housing 11 is output through speaker holes 11a and 11b. Two speakers are provided in main body apparatus 2 and speaker holes 11a and 11b are provided in correspondence with respective positions of a left speaker and a right speaker. Speaker hole 11a is provided on a left side of display 12 in correspondence with the left speaker and speaker hole 11b is provided on a right side of display 12 in correspondence with the right speaker. A position, a shape, and the number of speaker holes 11a and 11b can arbitrarily be designed. For example, in another embodiment, speaker holes 11a and 11b may be provided in a side surface or a rear surface of housing 11. (2) Member Provided on Left Side Surface of Housing 11 A left rail member 15 for removably attaching left controller 3 to main body apparatus 2 is provided in a left side surface of housing 11. Left rail member 15 extends along the up-down direction in the left side surface of housing 11. Left rail member 15 is in a shape allowing engagement thereof with a slider (a slider 40 shown in FIG. 4) for left controller 3. A slide mechanism is formed by left rail member 15 and slider 40. With such a slide mechanism, left controller 3 can slidably and removably be attached to main body apparatus 2. A left terminal 17 is provided in the left side surface of housing 11. Left terminal 17 is a terminal for wired communication between main body apparatus 2 and left controller 3. Left terminal 17 is provided at a position where it comes in contact with a terminal (a terminal 42 shown in FIG. 4) of left controller 3 when left controller 3 is attached to main body apparatus 2. Left terminal 17 should be arranged at any position where the left terminal of main body apparatus 2 and the terminal of left controller 3 are in contact with each other while left controller 3 is attached to main body apparatus 2. By way of example, as shown in FIG. 3, left terminal 17 is provided around a lower end portion of left rail member 15. (3) Member Provided in Right Side Surface of Housing 11 As shown in FIG. 3, a feature similar to the feature provided in the left side surface is provided in a right side surface of housing 11. A right rail member 19 for removably attaching right controller 4 to main body apparatus 2 is provided in the right side surface of housing 11. Right rail member 19 extends along the up-down direction in the right side surface of housing 11. Right rail member 19 is in a shape allowing engagement thereof with a slider (a slider 62 shown in FIG. 5) for right controller 4. A slide mechanism is formed by right rail member 19 and slider 62. With such a slide mechanism, right controller 4 can slidably and removably be attached to main body apparatus 2. Right rail member 19 is in a shape similar to left rail member 15. Right rail member 19 is in a grooved shape similar in cross-sectional shape to left rail member 15. Right rail member 19 does not have to be exactly the same in shape as left rail member 15. For example, another embodiment may be constructed such that slider 62 for right controller 4 cannot be engaged with left rail member 15 and/or slider 40 for left controller 3 cannot be engaged with right rail member 19 by making a size and/or a shape of the groove different between left rail member 15 and right rail member 19. A right terminal 21 is provided in the right side surface of housing 11. Right terminal 21 is a terminal for wired communication between main body apparatus 2 and right controller 4. Right terminal 21 is provided at a position where it comes in contact with a terminal (a terminal 64 shown in FIG. 5) of right controller 4 when right controller 4 is attached to main body apparatus 2. Right terminal 21 should be arranged at any position where the right terminal of main body apparatus 2 and the terminal of right controller 4 are in contact with each other while right controller 4 is attached to main body apparatus 2. By way of example, as shown in FIG. 3, right terminal 21 is provided around a lower end portion of right rail member 19. As described above, housing 11 of main body apparatus 2 according to the present embodiment is provided with left rail member 15 and right rail member 19 for attaching the controllers. A position, a shape, and a size of left rail member 15 and right rail member 19 can arbitrarily be designed. For example, in another embodiment, left rail member 15 and right rail member 19 may be provided at left and right end portions in a main surface and/or a rear surface of housing 11, respectively. Any feature can be adopted for a mechanism for removably attaching main body apparatus 2 and the controllers to each other, and a slider mechanism different from the slider mechanism shown in FIGS. 1 to 3 may be adopted and a mechanism different from the slider mechanism may be adopted. For example, a construction may be such that a projection provided on a side of the main body apparatus may be fitted and attached to a recess provided on a side of the controller, or a construction may be such that a magnet is provided on the side of the main body apparatus or the side of the controller and a portion made of a magnetic element is provided in the other for attachment of the main body apparatus and the controller to each other by attraction. (4) Member Provided on Upper Side Surface of Housing 11 As shown in FIG. 3, a first slot 23 for attaching a storage medium of a first type is provided in an upper side surface of housing 11. A lid portion which can be opened and closed is provided in an opening in first slot 23 as a typical feature, and a storage medium of the first type can be inserted in first slot 23 while the lid portion is open. The storage medium of the first type is, for example, a storage medium exclusively designed for game device 1 and a game device of the same type (for example, a dedicated memory card). The storage medium of the first type is used, for example, for storing data used in main body apparatus 2 (for example, data saved for an application) and/or a program executed in main body apparatus 2 (for example, a program for an application). A power button 28 for switching on and off main body apparatus 2 is provided on the upper side surface of housing 11. In the present embodiment, power button 28 is used also for switching between an ON mode and a sleep mode. The ON mode refers, for example, to a mode in which representation on a screen of display 12 is provided and the sleep mode refers, for example, to a mode in which representation on the screen of display 12 is not provided. In the sleep mode, representation on the screen of display 12 is not provided, and additionally or instead, processing in an application being executed (for example, game processing in a game application) may be suspended. When power button 28 is pressed and held (for example, power button 28 is continuously pressed for a prescribed time period or longer), processing for switching on and off main body apparatus 2 is performed. When power button 28 is pressed for a short period of time (for example, power button 28 is pressed for a time period shorter than the prescribed time period above), processing for switching between the ON mode and the sleep mode is performed. As described above, power button 28 of main body apparatus 2 according to the present embodiment is used for switching on and off and/or switching between the ON mode and the sleep mode. In another embodiment, power button 28 may be used only for any one type of switching. In this case, another button for the other type of switching may be provided in main body apparatus 2. An audio input and output terminal 25 (specifically an earphone jack) is provided in the upper side surface of housing 11. A microphone or an earphone can be attached to audio input and output terminal 25. (5) Member Provided on Lower Side Surface of Housing 11 As shown in FIG. 3, a lower terminal 27 for wired communication between main body apparatus 2 and a cradle 5 which will be described later is provided in a lower side surface of housing 11. Lower terminal 27 is provided at a position where it comes in contact with a terminal of cradle 5 when main body apparatus 2 is attached to cradle 5. Typically, a universal serial bus (USB) connector (more specifically, a female connector) can be adopted as lower terminal 27. A second slot 24 for attaching a storage medium of a second type different from the first type is provided in the lower side surface of housing 11. Second slot 24 may be provided in the surface where first slot 23 is provided. A lid portion which can be opened and closed is provided in an opening in second slot 24 as a typical feature, and a storage medium of the second type can be inserted in second slot 24 while the lid portion is open. The storage medium of the second type may be, for example, a general-purpose storage medium (for example, an SD card). The storage medium of the second type is used, for example, for storing data used in main body apparatus 2 (for example, data saved for an application) and/or a program executed in main body apparatus 2 (for example, a program for an application), similarly to the storage medium of the first type. A position, a shape, and the number of components (specifically, a button, a slot, and a terminal) provided in housing 11 described above can arbitrarily be designed. For example, in another embodiment, some of power button 28, first slot 23, and second slot 24 may be provided in another side surface or the rear surface of housing 11. Some of the components do not have to be provided. (a3: Structure of Left Controller) FIG. 4 is a diagram of left controller 3 according to the present embodiment when viewed from six sides. Referring to FIG. 4, left controller 3 has a housing 31 substantially in a form of a plate. A main surface of housing 31 (that is, a front surface or a surface on a side of a negative direction of the z axis shown in FIG. 1) is substantially in a rectangular shape. Housing 31 is in a vertically long shape, that is, long in the up-down direction (that is, the direction of the y axis shown in FIG. 1). Left controller 3 can be used with its main surface being vertically oriented or with its surface being horizontally oriented when a user holds the left controller while the left controller is detached from main body apparatus 2. A shape and a size of housing 31 can arbitrarily be designed. In another embodiment, housing 31 may be constructed into a shape other than a shape substantially in a form of a plate. Housing 31 does not have to be rectangular either, and for example, a semicircular shape may be adopted. Housing 31 does not have to vertically be long. A length of housing 31 in the up-down direction is preferably substantially the same as a length in the up-down direction of housing 11 of main body apparatus 2. A thickness of housing 31 (that is, a length in a front-rear direction or a length in the direction of the z axis shown in FIG. 1) is preferably substantially the same as a thickness of housing 11 of main body apparatus 2. Therefore, when left controller 3 is attached to main body apparatus 2 (see FIG. 1), a user can hold main body apparatus 2 and left controller 3 as if they were an integrated apparatus. A left corner portion of the main surface of housing 31 is rounded more than a right corner portion. A portion of connection between an upper side surface and a left side surface of housing 31 and a portion of connection between a lower side surface and the left side surface of housing 31 are rounded more than a portion of connection between the upper side surface and a right side surface and a portion of connection between the lower side surface and the right side surface (that is, a curve of beveling is great). Therefore, when left controller 3 is attached to main body apparatus 2 (see FIG. 1), the left side of game device 1 is rounded and hence such a shape facilitates holding by a user. An analog stick 32 is provided in left controller 3. As shown in FIG. 4, analog stick 32 is provided on the main surface of housing 31. Analog stick 32 represents one example of a direction instruction portion with which a direction can be input. Analog stick 32 includes a stick member which can be tilted in all directions (that is, a 360° direction including up, down, left, right, and diagonal directions) in parallel to the main surface of housing 31. Analog stick 32 is an analog input device with which a user can input a direction in accordance with a direction of tilt by titling the stick member. Analog stick 32 may further be constructed to be able to give an input of magnitude in accordance with an angle of tilt in addition to input of a direction in accordance with a direction of tilt when the stick member is tilted. Alternatively, a slide stick may implement the direction instruction portion. The slide stick is an input portion having a stick member slidable in all directions in parallel to the main surface of housing 31, and the user can give an input in accordance with a direction of slide by sliding the stick member. The slide stick may further be constructed also to give an input of magnitude in accordance with an amount of slide. Alternatively, the direction instruction portion may be implemented as an input portion indicating a direction through an operation to press a button. For example, the direction instruction portion may be implemented as an input portion indicating a direction with a cross-shaped key or four buttons corresponding to up, down, left, and right directions, respectively. In the present embodiment, an input can be given by pressing the stick member (in the direction perpendicular to housing 31). Analog stick 32 in the present embodiment is an input portion with which an input of a direction and magnitude in accordance with a direction of tilt and an amount of tilt of the stick member can be given and an input resulting from pressing of the stick member can be given. Left controller 3 includes four operation buttons 33 to 36 (specifically, a right direction button 33, a down direction button 34, an up direction button 35, and a left direction button 36). As shown in FIG. 4, these four buttons 33 to 36 are provided under analog stick 32 on the main surface of housing 31. Though four operation buttons are provided on the main surface of left controller 3 in the present embodiment, any number of operation buttons may be provided. These operation buttons 33 to 36 are used for giving an instruction in accordance with various programs (for example, an OS program or an application program) executed in main body apparatus 2. Since operation buttons 33 to 36 may be used for giving an input of a direction in the present embodiment, operation buttons 33 to 36 are also referred to as right direction button 33, down direction button 34, up direction button 35, and left direction button 36 for the sake of convenience of description. Operation buttons 33 to 36 may be used for giving an instruction other than an input of a direction. An operation portion (specifically, analog stick 32 and operation buttons 33 to 36) provided on the main surface of left controller 3 is operated, for example, with the left thumb of a user who holds game device 1 when left controller 3 is attached to main body apparatus 2 (see FIG. 9). When left controller 3 is used as being detached from main body apparatus 2, the operation portion is operated, for example, with the left thumb of the user who holds left controller 3 (see FIG. 10). A first L button 38 and a ZL button 39 are provided in left controller 3. These operation buttons 38 and 39 are used for giving an instruction in accordance with various programs executed in main body apparatus 2, similarly to operation buttons 33 to 36 described above. As shown in FIG. 4, first L button 38 is provided in an upper left portion on the side surface of housing 31. ZL button 39 is provided in an upper left portion as extending from the side surface to the rear surface of housing 31 (strictly speaking, the upper left portion when housing 31 is viewed from the front). ZL button 39 is provided in the rear of first L button 38 (a side of a positive direction of the z axis shown in FIG. 1). Since the upper left portion of housing 31 is rounded in the present embodiment, first L button 38 and ZL button 39 are in a rounded shape in conformity with rounding of the upper left portion of housing 31. When left controller 3 is attached to main body apparatus 2, first L button 38 and ZL button 39 are arranged in the upper left portion of game device 1 (see FIG. 1). Therefore, a user who holds game device 1 can operate first L button 38 and ZL button 39 with his/her left forefinger or long finger. Left controller 3 has slider 40 described above. As shown in FIG. 4, slider 40 extends along the up-down direction in the right side surface of housing 31. Slider 40 is in a shape allowing engagement with left rail member 15 (more specifically, a groove in left rail member 15) of main body apparatus 2. Specifically, slider 40 has a projecting cross-section (specifically, a cross-section perpendicular to the up-down direction). More specifically, slider 40 has a cross-section in a T shape in conformity with a shape of a cross-section of left rail member 15. Therefore, slider 40 engaged with left rail member 15 is fixed and does not come off in a direction perpendicular to a direction of slide (that is, a direction of extension of left rail member 15). Left controller 3 includes a second L button 43 and a second R button 44. These buttons 43 and 44 are used for giving an instruction in accordance with various programs executed in main body apparatus 2 similarly to other operation buttons 33 to 36. As shown in FIG. 4, second L button 43 and second R button 44 are provided in the surface where slider 40 is attached. Second L button 43 is provided above the center in terms of the up-down direction (the direction of they axis shown in FIG. 1) on the surface where slider 40 is attached. Second R button 44 is provided under the center in terms of the up-down direction on the surface where slider 40 is attached. Second L button 43 and second R button 44 are arranged at positions where they cannot be pressed while left controller 3 is attached to main body apparatus 2. Second L button 43 and second R button 44 are used while left controller 3 is detached from main body apparatus 2. Second L button 43 and second R button 44 are operated, for example, with a forefinger or a long finger of left and right hands of a user who holds left controller 3 detached from main body apparatus 2. Left controller 3 includes a notification LED 45. Notification LED 45 is a notification unit for notifying a user of prescribed information. Information given by notification LED 45 is any information. In the present embodiment, when main body apparatus 2 communicates with a plurality of controllers, notification LED 45 indicates information for identifying each controller to a user. Specifically, left controller 3 includes as notification LED 45, LEDs as many as left controllers (four here) with which main body apparatus 2 can simultaneously communicate. An LED among four LEDs in accordance with a number provided to a controller is turned on. Thus, the user can be notified of the number through notification LED 45. In another embodiment, notification LED 45 may notify the user of a state of communication between left controller 3 and main body apparatus 2. For example, notification LED 45 may be turned on when communication with main body apparatus 2 has been established. Though the number of LEDs (in other words, light emission portions) functioning as notification LED 45 is set to four in the present embodiment, the number of LEDs is set to any number. In the present embodiment, notification LED 45 is provided on the surface where slider 40 is attached as shown in the figure. Therefore, notification LED 45 is arranged at a position hidden while left controller 3 is attached to main body apparatus 2. Notification LED 45 is used when left controller 3 is detached from main body apparatus 2. In the present embodiment, a button (specifically, second L button 43 and second R button 44) provided on the surface where slider 40 is attached is provided not to protrude from that surface. An upper surface of the button (in other words, a surface which is pressed) is arranged flush with the surface where slider 40 is attached or at a position lower than such a surface. Thus, while slider 40 is attached to left rail member 15 of main body apparatus 2, slider 40 can smoothly be slid with respect to left rail member 15. (a4: Structure of Right Controller) FIG. 5 is a diagram of right controller 4 according to the present embodiment when viewed from six sides. Referring to FIG. 5, right controller 4 has a housing 51 substantially in a form of a plate. A main surface of housing 51 (that is, a front surface or a surface on the side of the negative direction of the z axis shown in FIG. 1) is substantially in a rectangular shape. Housing 51 is in a vertically long shape, that is, long in the up-down direction. Right controller 4 can be used with its main surface being vertically oriented or with its surface being horizontally oriented when a user holds the right controller while the right controller is detached from main body apparatus 2. Similarly to housing 31 of left controller 3, a length of housing 51 of right controller 4 in the up-down direction is preferably substantially the same as the length in the up-down direction of housing 11 of main body apparatus 2 and a thickness thereof is preferably substantially the same as the thickness of housing 11 of main body apparatus 2. Therefore, when right controller 4 is attached to main body apparatus 2 (see FIG. 1), a user can hold main body apparatus 2 and right controller 4 as if they were an integrated apparatus. A right corner portion of the main surface of housing 51 is rounded more than a left corner portion. A portion of connection between an upper side surface and a right side surface of housing 51 and a portion of connection between a lower side surface and the right side surface of housing 51 are rounded more than a portion of connection between the upper side surface and a left side surface and a portion of connection between the lower side surface and the left side surface (that is, a curve of beveling is great). Therefore, when right controller 4 is attached to main body apparatus 2 (see FIG. 1), the right side of game device 1 is rounded and hence such a shape facilitates holding by a user. An analog stick 52 is provided in right controller 4 as a direction instruction portion as in left controller 3. Analog stick 52 is constructed substantially similarly to analog stick 32 in left controller 3. Right controller 4 includes four operation buttons 53 to 56 (specifically, an A button 53, a B button 54, an X button 55, and a Y button 56) similarly to left controller 3. These four operation buttons 53 to 56 are substantially the same in mechanism as four operation buttons 33 to 36 in left controller 3. As shown in FIG. 5, analog stick 52 and operation buttons 53 to 56 are provided on the main surface of housing 51. Though four operation buttons are provided on the main surface of right controller 4 in the present embodiment, any number of operation buttons may be provided. Positional relation between two types of operation portions (analog stick 52 and the operation buttons) in right controller 4 is opposite to positional relation of these two types of operation portions in left controller 3. In right controller 4, analog stick 52 is arranged under operation buttons 53 to 56, whereas in left controller 3, analog stick 32 is arranged above operation buttons 33 to 36. With such arrangement, when two controllers are used as being detached from main body apparatus 2, both of the controllers can be used with similar operational feeling. When right controller 4 is attached to main body apparatus 2, the operation portion (specifically analog stick 52 and operation buttons 53 to 56) provided on the main surface of right controller 4 is operated, for example, with the right thumb of a user who holds game device 1 (see FIG. 9). When right controller 4 is used as being detached from main body apparatus 2, the operation portion is operated, for example, with the right thumb of a user who holds right controller 4. A first R button 60 and a ZR button 61 are provided in right controller 4. As shown in FIG. 5, first R button 60 is provided in an upper right portion on the side surface of housing 51. ZR button 61 is provided in an upper right portion as extending from the side surface to the rear surface of housing 51 (strictly speaking, the upper right portion when housing 51 is viewed from the front). ZR button 61 is provided in the rear of first R button 60 (the side of the positive direction of the z axis shown in FIG. 1). Since the upper right portion of housing 51 is rounded in the present embodiment, first R button 60 and ZR button 61 are in a rounded shape in conformity with rounding of the upper right portion of housing 51. When right controller 4 is attached to main body apparatus 2, first R button 60 and ZR button 61 are arranged in the upper right portion of game device 1 (see FIG. 1). Therefore, a user who holds game device 1 can operate first R button 60 and ZR button 61 with his/her right forefinger or long finger. In the present embodiment, first L button 38 and first R button 60 are not symmetric to each other in shape, and ZL button 39 and ZR button 61 are not symmetric to each other in shape. In another embodiment, first L button 38 and first R button 60 may be symmetric to each other in shape, and ZL button 39 and ZR button 61 may be symmetric to each other in shape. Right controller 4 has terminal 64 for wired communication between right controller 4 and main body apparatus 2. Terminal 64 is provided at a position where it comes in contact with right terminal 21 (FIG. 3) of main body apparatus 2 when right controller 4 is attached to main body apparatus 2. Terminal 64 should be arranged at any position where main body apparatus 2 and right controller 4 are in contact with each other while right controller 4 is attached to main body apparatus 2. By way of example, as shown in FIG. 5, terminal 64 is provided around a lower end portion of a surface where slider 62 is attached. A position, a shape, and the number of components (specifically, a slider, a stick, a button, and an LED) provided in housing 31 of left controller 3 and/or housing 51 of right controller 4 can arbitrarily be designed. For example, in another embodiment, the controller may include a direction instruction portion of a type different from the analog stick. Slider 40 or 62 may be arranged at a position in accordance with a position of left rail member 15 and right rail member 19 provided in main body apparatus 2, and for example, may be arranged in the main surface or the rear surface of housing 31 or 51. Some of the components do not have to be provided. Right controller 4 includes a second L button 65 and a second R button 66 as in left controller 3. These buttons 65 and 66 are used for giving an instruction in accordance with various programs executed in main body apparatus 2 similarly to other operation buttons 53 to 56. As shown in FIG. 5, second L button 65 and second R button 66 are provided on the surface where slider 62 is attached. Second L button 65 is provided under the center in terms of the up-down direction (the direction of the y axis shown in FIG. 1) on the surface where slider 62 is attached. Second R button 66 is provided above the center in terms of the up-down direction on the surface where slider 62 is attached. Second L button 65 and second R button 66 are arranged at positions where they cannot be pressed while right controller 4 is attached to main body apparatus 2. Second L button 65 and second R button 66 are used while right controller 4 is detached from main body apparatus 2. Second L button 65 and second R button 66 are operated, for example, with a forefinger or a long finger of left and right hands of a user who holds right controller 4 detached from main body apparatus 2. Right controller 4 includes a notification LED 67. Notification LED 67 is a notification unit for notifying a user of prescribed information similarly to notification LED 45 of left controller 3. Right controller 4 includes four LEDs as notification LEDs 67, as in left controller 3. An LED among four LEDs in accordance with a number provided to a controller is turned on. Thus, the user can be notified of the number through notification LED 67. In the present embodiment, similarly to notification LED 45, notification LED 67 is provided on the surface where slider 62 is attached as shown in the figure. Therefore, notification LED 67 is arranged at a position hidden while right controller 4 is attached to main body apparatus 2. Notification LED 67 is used when right controller 4 is detached from main body apparatus 2. In the present embodiment, also in right controller 4 as in left controller 3, a button (specifically, second L button 65 and second R button 66) provided on the surface where slider 62 is attached is provided not to protrude from that surface. An upper surface of the button (in other words, a surface which is pressed) is arranged flush with the surface where slider 62 is attached or at a position lower than such a surface. Thus, while slider 62 is attached to right rail member 19 of main body apparatus 2, slider 62 can smoothly be slid with respect to right rail member 19. (a5: Use of Cradle) FIG. 6 is a schematic diagram showing appearance when game device 1 according to the present embodiment is used together with a cradle. The game system shown in FIG. 6 includes game device 1 and cradle 5. Cradle 5 is constructed to be able to carry game device 1 and constructed to be able to communicate with a television 6 representing one example of an external display apparatus separate from display 12 of game device 1. When game device 1 is carried on cradle 5, an image obtained or generated by game device 1 can be shown on television 6. Communication between cradle 5 and television 6 may be wired communication or wireless communication. Cradle 5 may have a function to charge placed game device 1 and a function as a communication hub apparatus (for example, a USB hub). [B. Internal Configuration of Each Apparatus] An internal configuration of each apparatus associated with the information processing system according to the present embodiment will initially be described. (b1: Internal Configuration of Main Body Apparatus) FIG. 7 is a block diagram showing an internal configuration of main body apparatus 2 according to the present embodiment. Main body apparatus 2 includes components shown in FIG. 7. The components shown in FIG. 7 are accommodated in housing 11, for example, as being mounted on an electronic circuit substrate as electronic components. Main body apparatus 2 includes a central processing unit (CPU) 81 corresponding to an information processing unit (or a processor) performing various types of processing including game processing. CPU 81 reads and executes a program stored in an accessible storage unit (specifically, an internal storage medium such as a flash memory 84 or an external storage medium attached to first slot 23 or second slot 24). Main body apparatus 2 includes flash memory 84 and a dynamic random access memory (DRAM) 85 by way of example of an embedded internal storage medium. Flash memory 84 is a non-volatile memory mainly storing various types of data (which may be a program) saved in main body apparatus 2. DRAM 85 is a volatile memory temporarily storing various types of data used in information processing. Main body apparatus 2 includes a first slot interface (I/F) 91 and a second slot interface 92. The first slot interface is connected to first slot 23 and reads and writes data from and into a storage medium of the first type (for example, an SD card) attached to first slot 23, in response to an instruction from CPU 81. Second slot interface 92 is connected to second slot 24 and reads and writes data from and into a storage medium of the second type (for example, a dedicated memory card) attached to second slot 24, in response to an instruction from CPU 81. Main body apparatus 2 includes a network communication unit 82 for communication (specifically, wireless communication) with an external apparatus through a network. For example, a communication module authorized for Wi-Fi is employed for network communication unit 82 and network communication unit 82 communicates with an external apparatus through wireless LAN. In another embodiment, main body apparatus 2 may have a function for connection and communication with a mobile communication network (that is, a portable telephone communication network) in addition to (or instead of) a function for connection and communication with wireless LAN. Main body apparatus 2 includes a controller communication unit 83 for wireless communication with left controller 3 and/or right controller 4. Though any scheme is applicable for communication between main body apparatus 2 and each controller, for example, a communication scheme under the Bluetooth® specifications can be adopted. CPU 81 is connected to left terminal 17, right terminal 21, and lower terminal 27. CPU 81 transmits and receives data to and from left controller 3 through left terminal 17 when wired communication with left controller 3 is established. CPU 81 transmits and receives data to and from right controller 4 through right terminal 21 when wired communication with right controller 4 is established. Data transmitted from CPU 81 to left controller 3 or right controller 4 is, for example, data for controlling a vibration generation portion of left controller 3 or right controller 4. Data received by CPU 81 from left controller 3 or right controller 4 is, for example, operation data output in response to an operation by a user of the operation portion in left controller 3 or right controller 4. CPU 81 transmits data to cradle 5 through lower terminal 27 when it communicates with cradle 5. In the present embodiment, main body apparatus 2 can establish both of wired communication and wireless communication with left controller 3 and right controller 4. Main body apparatus 2 includes a touch panel controller 86 for control of touch panel 13. Touch panel controller 86 generates data indicating a position of a touch input in response to a signal from touch panel 13, and outputs the data to CPU 81. Display 12 shows an image generated by execution of various types of processing by CPU 81 and/or an image obtained from the outside. Main body apparatus 2 includes a codec circuit 87 and speaker 88 (specifically, the left speaker and the right speaker). Codec circuit 87 controls input and output of audio data to and from speaker 88 and audio input and output terminal 25. More specifically, when codec circuit 87 receives audio data from CPU 81, it outputs an audio signal resulting from D/A conversion of the audio data to speaker 88 or audio input and output terminal 25. Thus, sound is output from speaker 88 or an audio output portion (for example, an earphone) connected to audio input and output terminal 25. When codec circuit 87 receives an audio signal from audio input and output terminal 25, it subjects the audio signal to A/D conversion and outputs audio data in a prescribed format to CPU 81. Main body apparatus 2 has an acceleration sensor 89 and an angular speed sensor 90. Acceleration sensor 89 detects magnitude of a linear acceleration along directions of prescribed three axes (for example, the xyz axes shown in FIG. 1). Acceleration sensor 89 may detect an acceleration in a direction of one axis or accelerations in directions of two axes. Angular speed sensor 90 detects angular speeds around prescribed three axes (for example, the xyz axes shown in FIG. 1). Angular speed sensor 90 may detect an angular speed around one axis or angular speeds around two axes. A result of detection by acceleration sensor 89 and angular speed sensor 90 is output to CPU 81. CPU 81 can calculate information on a motion and/or an attitude of main body apparatus 2 based on the result of detection by acceleration sensor 89 and angular speed sensor 90. Main body apparatus 2 includes an electric power control unit 97 and a battery 98. Electric power control unit 97 controls supply of electric power from battery 98 to each component based on a command from CPU 81. Electric power control unit 97 controls supply of electric power in accordance with an input onto power button 28. When an operation to turn off power supply is performed on power button 28, electric power control unit 97 stops supply of electric power totally or in part, and when an operation to turn on power supply is performed on power button 28, it starts full supply of electric power. When an instruction to switch to the sleep mode is given to power button 28, electric power control unit 97 stops supply of electric power to some components including display 12, and when an instruction to switch to the ON mode is given to power button 28, it starts supply of electric power. When an external charging apparatus (for example, cradle 5) is connected to lower terminal 27 and electric power is supplied to main body apparatus 2 through lower terminal 27, battery 98 is charged with supplied electric power. Battery 98 of main body apparatus 2 is preferably higher in charging capacity than a battery of left controller 3 and right controller 4. (b2: Internal Configuration of Controller) FIG. 8 is a block diagram showing an internal configuration of left controller 3 and right controller 4 according to the present embodiment. FIG. 8 also depicts components of main body apparatus 2 associated with left controller 3 and right controller 4. Left controller 3 includes a communication control unit 101 for communication with main body apparatus 2. Communication control unit 101 can communicate with main body apparatus 2 through both of wired communication through terminal 42 and wireless communication not through terminal 42. Communication control unit 101 selects wired communication or wireless communication depending on whether or not left controller 3 is attached to main body apparatus 2, and establishes communication under a selected communication method. While left controller 3 is attached to main body apparatus 2, communication control unit 101 establishes communication with main body apparatus 2 through terminal 42. While left controller 3 is detached from main body apparatus 2, communication control unit 101 establishes wireless communication with main body apparatus 2 (specifically, controller communication unit 83). The communication control unit should only be able to establish communication with the main body apparatus, and for example, it may be configured to establish only either wired communication or wireless communication. While left controller 3 is detached from main body apparatus 2, wireless communication is established by way of example, however, wired communication may be established, for example, through a cable. Left controller 3 includes, for example, a memory 102 such as a flash memory. Communication control unit 101 is implemented, for example, by a microprocessor and performs various types of processing by executing firmware stored in memory 102. Left controller 3 includes an operation button group 103 (specifically operation buttons 33 to 36, 38, and 39) and analog stick 32. Information on an operation onto operation button group 103 and analog stick 32 is repeatedly output to communication control unit 101 with a prescribed period. Left controller 3 has an acceleration sensor 104 and an angular speed sensor 105. Acceleration sensor 104 detects magnitude of a linear acceleration along directions of prescribed three axes (for example, the xyz axes shown in FIG. 1). Acceleration sensor 104 may detect an acceleration in a direction of one axis or accelerations in directions of two axes. Angular speed sensor 105 detects angular speeds around prescribed three axes (for example, the xyz axes shown in FIG. 1). Angular speed sensor 105 may detect an angular speed around one axis or angular speeds around two axes. A result of detection by acceleration sensor 104 and angular speed sensor 105 is repeatedly output to communication control unit 101 with a prescribed period. Communication control unit 101 obtains information on an input from each of operation button group 103, analog stick 32, acceleration sensor 104, and angular speed sensor 105 (for example, information on an operation by a user or a result of detection by the sensor). Communication control unit 101 transmits data including obtained information (or information obtained by subjecting obtained information to prescribed processing) to main body apparatus 2. Data is transmitted to main body apparatus 2 repeatedly with a prescribed period. A period of transmission of information on an input to main body apparatus 2 may or may not be identical among input devices. Main body apparatus 2 can know an input given to left controller 3 based on transmitted data. More specifically, main body apparatus 2 can discriminate an operation onto operation button group 103 and analog stick 32. Main body apparatus 2 can calculate information on a motion and/or an attitude of left controller 3. Left controller 3 includes an electric power supply unit 109 including a battery and an electric power control circuit. Electric power supply unit 109 controls supply of electric power to each component of left controller 3. When left controller 3 is attached to main body apparatus 2, the battery is charged by power feed from main body apparatus 2 through terminal 42. Electric power supply unit 109 gives battery warning information to main body apparatus 2 when the battery runs out of electric power. Right controller 4 is configured basically similarly to left controller 3 described above. Right controller 4 includes a communication control unit 111, an operation button group 113 (specifically operation buttons 53 to 56, 60, and 61), analog stick 52, an acceleration sensor 114, an angular speed sensor 115, and an electric power supply unit 119. When the battery runs out of electric power, electric power supply unit 119 gives battery warning information to main body apparatus 2. Since other components of right controller 4 have features and functions the same as those of corresponding components described in connection with left controller 3, detailed description will not be repeated. Thus, game device 1 according to the present embodiment includes left controller 3 held in the left hand of the user (one hand) (a portion held in the left hand of the user) and right controller 4 held in the right hand (the other hand) of the user (a portion held in the right hand of the user). The “operation portion” herein may mean a function or a feature accepting an operation by a user and encompass any component such as a button, an analog stick, and various sensors arranged in main body apparatus 2, left controller 3, and right controller 4, so long as it can sense an operation by a user. The operation portion may be configured to be able to sense an operation by the user based on combination of a button, an analog stick, and various sensors as being distributed in main body apparatus 2, left controller 3, and right controller 4. [C. Manner of Use of Game System] As described above, game device 1 according to the present embodiment is constructed such that left controller 3 and right controller 4 are removable. Game device 1 can output an image and sound to television 6 by being attached to cradle 5. Therefore, game device 1 can be used in various manners of use as will be described below. A main manner of use of game device 1 will be exemplified below. (c1: Manner of Use With Controller Being Attached to Main Body Apparatus) FIG. 9 is a diagram showing one example of a manner of use of game device 1 with left controller 3 and right controller 4 being attached to main body apparatus 2 (hereinafter also referred to as an “attached state”). As shown in FIG. 9, in the attached state, game device 1 can be used as a portable device. In the attached state, basically, communication between main body apparatus 2, and left controller 3 and right controller 4 is established through wired communication. In another embodiment, communication between main body apparatus 2, and left controller 3 and right controller 4 may be established through wireless communication also in the attached state. In the attached state, four operation buttons 33 to 36 of left controller 3 may be used for inputting a direction (that is, an instruction for a direction). A user can input a direction with analog stick 32 or operation buttons 33 to 36. Since the user can input a direction with his/her preferred operation means, operability can be improved. For which instruction operation buttons 33 to 36 are used may arbitrarily be determined depending on a program executed in main body apparatus 2. In the present embodiment, arrangement of the analog stick and four operation buttons (that is, A, B, X, and Y buttons) is reverse between left controller 3 and right controller 4. In the attached state, analog stick 32 is arranged above four operation buttons 33 to 36 in left controller 3, whereas four operation buttons 53 to 56 are arranged above analog stick 52 in right controller 4. Therefore, when a user holds game device 1 with his/her both hands being located at the same height (that is, at positions the same in the up-down direction) as shown in FIG. 9, the analog stick is located at a position readily operable with one hand and the four operation buttons are located at positions readily operable with the other hand. Game device 1 according to the present embodiment thus provides a feature facilitating an operation of the analog stick and four operation buttons. (c2: Manner of Use With One Set of Controllers Being Detached From Main Body Apparatus) FIG. 10 is a diagram showing one example of a manner of use of game device 1 with left controller 3 and right controller 4 being detached from main body apparatus 2 (hereinafter also referred to as a “detached state”). As shown in FIG. 10, in the detached state, the user can operate left controller 3 and right controller 4 in his/her left and right hands, respectively. In this case, analog stick 32 and four operation buttons 33 to 36 of left controller 3 are operated as being arranged vertically in the left hand in which the controller is held. Similarly, analog stick 52 and four operation buttons 53 to 56 of right controller 4 are operated as being arranged vertically in the right hand in which the controller is held. The controller is used such that the main surface thereof is vertically oriented when the user holds the controller (also referred to as an operation in vertical holding). In the detached state, basically, communication between main body apparatus 2, and left controller 3 and right controller 4 is established through wireless communication. Main body apparatus 2 receives data from the controller with which it has established wireless communication (typically pairing has been done) and performs game processing based on the received data. In the present embodiment, in wireless communication, main body apparatus 2 distinguishes between left controller 3 and right controller 4 which are communication counterparts. Main body apparatus 2 identifies whether the data received from the controller is from left controller 3 or from right controller 4. Though FIG. 10 shows a manner of use by one user of one set of controllers (the left controller and the right controller), such a manner of use that two users use the respective controllers is also applicable. In this case, two users can simultaneously participate in a game with one set of controllers (the left controller and the right controller). Though FIG. 10 shows a state that both of left controller 3 and right controller 4 are detached from main body apparatus 2, limitation thereto is not intended and any one of left controller 3 and right controller 4 can be detached from main body apparatus 2 and game device 1 can be used with the other being attached to main body apparatus 2. (c3: Manner of Use of Respective Controllers by Two Users) FIG. 11 is a diagram showing one example of a manner of use of game device 1 with two users each holding one controller in the detached state. As shown in FIG. 11, two users can perform operations in the detached state. Specifically, one user (called a “first user”) uses left controller 3 to perform an operation and the other user (called a “second user”) can use right controller 4 to perform an operation. Game device 1 performs, for example, information processing for controlling an operation of a first object (for example, a player character) in a virtual space based on an operation onto left controller 3 and for controlling an operation of a second object in the virtual space based on an operation onto right controller 4. In the manner shown in FIG. 11 as well, as in the manner shown in FIG. 10, the user can perform an operation onto the operation portion included in the controller and/or an operation to move the controller itself. In this case, analog stick 32 and four operation buttons 33 to 36 in left controller 3 used by the first user are operated as being arranged laterally between the left and right hands in which the controller is held. Similarly, analog stick 52 and four operation buttons 53 to 56 in right controller 4 used by the second user are operated as being arranged laterally between the left and right hands in which the controller is held. The controller is used such that the main surface thereof is laterally oriented when the user holds the controller (also referred to as an operation in lateral holding). Though description will be given later, under an operation scheme in lateral holding of left controller 3 and right controller 4, functions of the operation portions in left controller 3 and right controller 4 are changed from those in an operation scheme in vertical holding. In the present embodiment, positional relation between analog stick 52 and operation buttons 53 to 56 in right controller 4 is opposite to positional relation between these two types of operation portions in left controller 3. Therefore, when two users hold left controller 3 and right controller 4 in the same orientation, for example, as shown in FIG. 11, positional relation between the two types of operation portions is the same between the two controllers. In the present embodiment, the user can use the two types of operation portions in left controller 3 and right controller 4 detached from main body apparatus 2 with similar operation feeling. Operability of the controller can thus be improved. In the detached state, four operation buttons 33 to 36 of left controller 3 may be used to perform functions the same as those of four operation buttons 53 to 56 in right controller 4 (in other words, may be used for giving the same instruction). Specifically, right direction button 33 may be used to perform a function the same as that of Y button 56, down direction button 34 may be used to perform a function the same as that of X button 55, up direction button 35 may be used to perform a function the same as that of B button 54, and left direction button 36 may be used to perform a function the same as that of A button 53. Thus, in the present embodiment, functions of operation buttons 33 to 36 may be changed between the attached state and the detached state. For which instruction each operation button is used may freely be determined depending on a program executed in main body apparatus 2. In FIG. 11, in game device 1, a display area of display 12 of main body apparatus 2 is divided into two sections, and game device 1 shows an image for the first user (for example, an image including the first object) in one divided display area and shows an image for the second user (for example, an image including the second object) in the other divided display area. Depending on an application executed in game device 1, however, game device 1 may show an image for two users (for example, an image including both of the first object and the second object) without the display area of display 12 being divided. In the manner shown in FIG. 11 as well, as in the manner shown in FIG. 10, communication between main body apparatus 2, and left controller 3 and right controller 4 is established through wireless communication. Main body apparatus 2 distinguishes between controllers to be communication counterparts. (c4: Manner of Use of Television) FIG. 12 is a diagram showing one example of a manner of use of game device 1 with main body apparatus 2 being attached to cradle 5. As shown in FIG. 12, by attaching main body apparatus 2 to cradle 5, an image obtained or generated by game device 1 can be shown on television 6. A user operates left controller 3 and/or right controller 4 while the user watches an image shown on television 6 (and an image shown on the display of main body apparatus 2 as necessary). (c5: Manner of Use of Three or More Controllers) As described above, in the present embodiment, main body apparatus 2 can communicate with a plurality of left controllers. Main body apparatus 2 can communicate with a plurality of right controllers. Therefore, in the present embodiment, three or more controllers can simultaneously be used. FIGS. 13A and 13B are diagrams showing examples of a manner of use of three or more controllers. FIGS. 13A and 13B show examples in which four controllers in total of two left controllers 3a and 3b and two right controllers 4a and 4b are used. Each controller is detached from main body apparatus 2. Thus, when the four controllers are used, at least a manner of use of one controller by each of four users (FIG. 13A) and a manner of use of two controllers by each of two users (specifically, one set of controllers on each of a left side and a right side) (FIG. 13B) are possible. (Manner of Use of One Controller by One User) In FIG. 13A, four controllers 3a, 3b, 4a, and 4b are used by respective users. In the present embodiment, when four controllers are prepared, four users of a user A to a user D can use the controllers to perform operations. Game device 1 performs, for example, information processing controlling an operation of an object corresponding to each controller based on an operation onto the controller. In FIG. 13A, main body apparatus 2 establishes wireless communication with each of four controllers 3a, 3b, 4a, and 4b. In the present embodiment, main body apparatus 2 distinguishes among four controllers 3a, 3b, 4a, and 4b. Main body apparatus 2 identifies from which of the four controllers received operation data has come. In FIG. 13A, main body apparatus 2 distinguishes between left controller 3a and left controller 3b and distinguishes between right controller 4a and right controller 4b. (Manner of Use of One Set of Controllers by One User) In FIG. 13B, one user uses one set of controllers. User A uses one set of left controller 3a and right controller 4a, and user B uses one set of left controller 3b and right controller 4b. Thus, in the present embodiment, when four controllers are prepared, each of two users can operate one set of controllers. Game device 1 performs information processing with two pieces of operation data received from one set of controllers being defined as one set. For example, game device 1 performs information processing controlling an operation of an object corresponding to one set of controllers based on an operation onto that one set of controllers. Specifically, an operation of the first object is controlled based on an operation onto left controller 3a and right controller 4a, and an operation of the second object is controlled based on an operation onto left controller 3b and right controller 4b. In the present embodiment, in the manner of use shown in FIG. 13B, main body apparatus 2 sets a set of a left controller and a right controller to be used by one user. Main body apparatus 2 performs information processing by using two pieces of operation data from the two controllers included in the set as one set (for example, using the data as operation data for controlling one operation target). Any method may be adopted as a method of setting a set of controllers, and in the present embodiment, a set is set by attaching left and right controllers to main body apparatus 2. Main body apparatus 2 sets simultaneously attached left controller and right controller as one set of controllers. For example, when a set of controllers shown in FIG. 13B is set, the user initially attaches left controller 3a and right controller 4a to main body apparatus 2, detaches left controller 3a and right controller 4a from main body apparatus 2, and thereafter attaches left controller 3b and right controller 4b to main body apparatus 2. Thus, a set of left controller 3a and right controller 4a and a set of left controller 3b and right controller 4b can be set (or registered) in main body apparatus 2. When three or more controllers are used, other than manners of use shown in FIGS. 13A and 13B, the information processing system can be used in various manners. For example, the information processing system can be used in such a manner that one user uses a set of controllers consisting of left and right controllers and another user uses one controller. Alternatively, for example, one user can use a controller attached to main body apparatus 2 and another user can use a controller detached from main body apparatus 2. (c6: Other Manners) In addition to the manners of use as described above, a head mounted display (HMD) type display can also be used. (c7: Advantages in Terms of Operation) In the present embodiment, information on a motion and/or an attitude of each controller can be calculated based on a result of detection by the acceleration sensor and/or the angular speed sensor in the left controller and the right controller. Game device 1 can accept an operation by a user to move the controller itself as an input. The user can perform not only an operation onto the operation portion (the operation buttons and the analog stick) in each controller but also an operation to move the controller itself. In the present embodiment, game device 1 can provide a user with an operation to move a controller (without moving a display) while it is a portable device. Game device 1 can also provide a game device allowing a user to perform an operation at a location distant from display 12 while it is a portable device. Game device 1 can calculate information on a motion and/or an attitude of game device 1 based on a result of detection by the acceleration sensor and/or the angular speed sensor in the left controller and the right controller not only in the detached state but also in the attached state. Game device 1 can also calculate information on a motion and/or an attitude of game device 1 based on a result of detection by acceleration sensor 89 and/or angular speed sensor 90 in main body apparatus 2 in the attached state. [D. Accessory Controller] An accessory controller 401 will now be described. Separately from left controller 3 and right controller 4, accessory controller 401 which can communicate with main body apparatus 2 of game device 1 can also be provided. FIG. 14 is a diagram showing appearance of accessory controller 401 based on an embodiment. As shown in FIG. 14, accessory controller 401 is mainly constituted of a housing 402 including grip portions 400L and 400R on the left and right (which may hereinafter collectively also be called a grip portion 400) and an operation portion including two analog sticks protruding through openings provided in a surface of housing 402 and a plurality of operation buttons (which will be described later). Housing 402 is substantially in a smooth trapezoidal shape with a longitudinal direction thereof being defined as a lateral direction when viewed from the front. The housing may be in such a shape that an upper side is slightly recessed and a lower side is more recessed than the upper side, in other words, grip portions 400L and 400R extend toward a bottom surface (forward when viewed from a player while the controller is held). A front surface side may be constructed substantially planar except for a position where the analog stick is provided. A position where the analog stick is located is slightly raised and grip portions 400L and 400R may be in a shape gently curved rearward from the front. Housing 402 in the present example may be formed, for example, through plastic molding. A first analog stick 411 (hereinafter a left stick) is provided around an upper surface side at a left end on a front surface of housing 402 and a second analog stick 412 (hereinafter a right stick) is provided around a lower surface side at a right end on the front surface of housing 402. More specifically, left stick 411 is arranged at a position operable with the thumb of the left hand with which grip portion 400L is held (more suitably, a position where the thumb of the left hand with which grip portion 400L is held is naturally located), and right stick 412 is arranged at a position operable with the thumb of the right hand with which grip portion 400R is held. Left stick 411 and right stick 412 are sticks which can be tilted in any direction around 360 degrees and used for indicating any direction. Left stick 411 and right stick 412 can be pressed rearward and also play a role as a push button. Left stick 411 and right stick 412 function in accordance with a program executed by main body apparatus 2 to which the controller is connected. Since a distance between left stick 411 and right stick 412 is thus great, a distance between the thumbs is not small even in an operation to tilt both of them inward and hence operability is good. A cross-shaped key (which may also be called a direction key) 421 is provided at a position on the left of a substantially central position on the front surface of housing 402 and on an inner side of left stick 411, where the cross-shaped key is operable with the thumb of the left hand with which grip portion 400L is held. More specifically, cross-shaped key 421 is provided at a position on the lower right of left stick 411. Cross-shaped key 421 is such a four-directional cross-shaped push switch that operation portions corresponding to four respective directions (front, rear, left, and right) are arranged at an interval of 90° on respective projecting parts of the cross. As a player presses any operation portion of cross-shaped key 421, any of the front, rear, left, and right directions is selected. Cross-shaped key 421 functions in accordance with a program executed by main body apparatus 2 to which the controller is connected. Cross-shaped key 421 is not limited to the shape as illustrated and any shape is applicable so long as a shape allows input of four directions. For example, such a shape that a cross-shaped raised portion is provided in a circular base is acceptable and four separate keys may be acceptable. Operation buttons 422A to 422D (which may hereinafter also be called a first operation button group) are arranged at upper, lower, left, and right positions of a cross pattern on the right of substantially the center on the front surface of housing 402 in an area above right stick 412, where the buttons are operable with the thumb of the right hand with which grip portion 400R is held. More specifically, operation buttons 422A to 422D are arranged at upper, lower, left, and right positions of the cross-pattern in an area located on the upper right of right stick 412. For example, operation buttons 422A to 422D are used for indicating enter or cancel. By arranging cross-shaped key 421 at a position on the lower right of left stick 411, the thumb pad can be moved to the position of cross-shaped key 421 by moving the thumb with the root of the left thumb being set as the fulcrum. In other words, the thumb pad can be moved to the position of cross-shaped key 421 simply by moving the thumb to the right with the root of the thumb being set as the fulcrum without particularly changing an attitude to hold grip portion 400L and the thumb can also be returned to the position of left stick 411 by moving the thumb to the left. Skip between left stick 411 and cross-shaped key 421 is facilitated and operability can be improved. In other words, there is no lowering in operability caused by the stick constituting the obstacle as being located between the tip end of the thumb (the position of the cross-shaped key) and the root of the thumb in operation of cross-shaped key 421. Similarly, by arranging right stick 412 at the position on the lower left of the first operation button group (operation buttons 422A to 422D), the thumb can be moved between right stick 412 and the first operation button group simply by moving the thumb with the root of the right thumb being set as the fulcrum. Skip between right stick 412 and the first operation button group is thus facilitated and operability can be improved. An L button 425L is provided on a front side in a left end portion of the upper surface of housing 402 and a ZL button is provided under the same (on a rear side). An R button 425R is arranged on the front side in a right end portion of the upper surface of housing 402 and a ZR button is arranged under the same (on the rear side). L button 425L is arranged at a position where the L button can be reached by the forefinger of the left hand with which grip portion 400L is held and the ZL button is arranged at a position where the ZL button can be reached by the left long finger or ring finger. R button 425R is arranged at a position where the R button can be reached by the forefinger of the right hand with which grip portion 400R is held and the ZR button is arranged at a position where the ZR button can be reached by the right long finger or ring finger. Functions in accordance with a program executed by the information processing apparatus are allocated as appropriate to L button 425L, R button 425R, the ZL button, and the ZR button. Operation buttons similar to the operation buttons provided in left controller 3 and right controller 4 described above are also provided in accessory controller 401. A plurality of indicators are provided on a bottom surface side of the front surface of housing 402. Specifically, a notification LED 431 is provided. Notification LED 431 serves as a notification unit for notifying a user of prescribed information, similarly to the notification LED of the left controller. Notification LED 431 includes four LEDs. Among the four LEDs, an LED in accordance with a player number allocated to a controller is turned on. Thus, the user can be notified of the player number by notification LED 431. Since accessory controller 401 is basically similar in internal configuration to left controller 3 or right controller 4 described with reference to FIG. 8, detailed description thereof will not be repeated. Identification information represented by a value (for example, an ID) specifically provided to accessory controller 401 is stored in a memory of accessory controller 401. Main body apparatus 2 can identify a controller as the accessory controller, not as left controller 3 or right controller 4, based on the identification information. Unlike left controller 3 and right controller 4, selection from among a plurality of operation schemes is not allowed for accessory controller 401 in the present example. In another embodiment, selection from among a plurality of operation schemes may be allowed. [E: Controller Registration Processing] FIGS. 15A and 15B are diagrams showing examples illustrating a controller registration screen displayed by game device 1 based on the embodiment. As shown in FIGS. 15A and 15B, controllers held by users PA to PD representing four players are registered in a controller registration screen shown on television 6. The controller registration screen represents one example of a screen shown when controller registration is indicated in a home menu. The home menu is provided to allow launch of a game application together with various types of setting (controller registration). For example, an icon for launching a game application is provided, and a game application is launched by selecting the icon. An icon for registering a controller is also provided. An application for controller registration processing is launched by selecting the icon and the controller registration screen is shown. An instruction for registration of a controller can be given also from each game application, and in that case, a manner of an available controller is shown depending on a game application. For example in an example of a game application in which only left and right controllers are used but the accessory controller is not used, the accessory controller is not shown. Since an instruction for registration of a controller can also be given from each game application, it is not necessary to perform a bothersome procedure for performing setting processing by returning to the home menu, and hence usability can be improved. Television 6 in the present example in FIG. 15A shows a message that “press ‘L’ and ‘R’ of controller to be used.” In the present example, each user is invited to press the L button and the R button in registration of a controller held by each user. Through a series of processes in response to pressing, a player number is registered for a controller of each user. One operation scheme is set in a controller adapted to a plurality of operation schemes. In the present example, any of an operation scheme in vertical holding of two controllers and an operation scheme in lateral holding of one controller representing a plurality of operation schemes is set. For example, in specifying an operation scheme, an operation scheme may be specified based on whether two controllers or one controller are/is held, or an operation scheme can also be specified based on whether the controller is held vertically or laterally. A controller can be registered in accordance with such a message. A state that a controller has not been registered is shown. A player number is allocated as a controller is registered. Then, a manner of a registered controller corresponding to the allocated player number is schematically shown in areas from P1 to P4 corresponding to player numbers. A manner of a controller which can be registered is shown in an upper area of the controller registration screen. Registration of two controllers of left controller 3 and right controller 4, registration of accessory controller 401, and registration of one controller, that is, left controller 3 or right controller 4, are shown. When two controllers are registered, in order to show a position of a button to be selected, together with an image of two controllers, the position is shown as being emphasized with a circular image being added. When accessory controller 401 is registered, in order to show a position of a button to be selected, together with an image of accessory controller 401, the position is shown as being emphasized with a circular image being added. Possibility of use of two controllers by two persons is also shown. In registration of one controller, in order to show a position of a button to be selected, together with an image of one controller, the position is shown as being emphasized with a circular image being added. A user can register a controller in a more simplified manner by checking on the controller registration screen, a position of the button emphasized by the circular image, together with the image of the controller. By way of example, user PA holds left controller 3a and right controller 4a. User PB holds accessory controller 401. User PC holds left controller 3b. User PD holds right controller 4b. When user PA registers two controllers, the user presses first L button 38 provided in left controller 3a and first R button 60 provided in right controller 4a. When user PB registers accessory controller 401, the user presses L button 425L and R button 425R in accessory controller 401. When user PC registers one controller with left controller 3b, the user presses second L button 43 and second R button 44 provided in left controller 3b. When user PD registers one controller with right controller 4b, the user presses second L button 65 and second R button 66 provided in right controller 4b. Game device 1 receives operation data transmitted from each controller, allocates a player number to each controller based on the received operation data, and registers an operation scheme in registration information as necessary. FIG. 15B shows an example in which a controller is registered in accordance with operation data. Specifically, an image of two controllers held by user PA is shown as the controller to which a player number P1 is allocated. An image of the accessory controller held by user PB is shown as the controller to which a player number P2 is allocated. An image of one controller held by user PC is shown as the controller to which a player number P3 is allocated. A state that a player number P4 has not yet been registered (an area shown with a dotted line) is shown. In the present example, a check image is shown in an area for player number P4 which has not yet been registered. In the check image, an image of a controller representing an operation scheme in lateral holding and an image of a controller representing an operation scheme in vertical holding are alternately shown. By showing the image of two controllers for which the operation scheme in vertical holding has been registered and an image of one controller for which the operation scheme in lateral holding has been registered, difference in manner of a method of operation of the controller is clearly shown and hence usability is improved. By further showing a name and a function of a button of the controller for which the operation scheme in vertical holding has been registered together with the image, information on the method of operation may be presented. By further showing a name and a function of a button of the controller for which the operation scheme in lateral holding has been registered together with the image, information on the method of operation may be presented. FIG. 16 is a diagram illustrating one example of registration information based on the embodiment. As shown in FIG. 16, registration information includes number information, identification information, information associated with wireless communication information, a player number, and information on an operation scheme. The number information is represented by a number provided to a registered controller. The identification information is information representing a value (for example, an ID) specifically provided to a controller. A controller can uniquely be identified based on the identification information. In the present embodiment, the identification information includes information indicating whether a controller is the left controller or the right controller. Main body apparatus 2 can determine based on the identification information provided to the controller whether the controller is the left controller or the right controller. In another embodiment, the identification information does not have to include information indicating whether the controller is the left controller or the right controller. The registration information may include (separately from the identification information) information indicating whether a controller is the left controller or the right controller. The wireless communication information indicates whether connection setting (that is, pairing) in connection with wireless communication with main body apparatus 2 has been made. When pairing between main body apparatus 2 and a controller has been completed, information indicating “set” is stored as wireless communication information associated with the controller. When pairing between main body apparatus 2 and a controller has not been completed, information indicating “not set” is stored as wireless communication information associated with the controller. Main body apparatus 2 may store information on connection setting for wireless communication (separately from the registration information), and does not have to carry out pairing again with the controller with which pairing has once been done. A player number represents identification information specifying a player operated in an application. The notification LED described above in the controller is controlled to indicate a value based on this number. The player number may be allocated in the order of registration of players or randomly by way of example. Information on the operation scheme represents information indicating a selected operation scheme when selection from among a plurality of operation schemes can be made for a controller. For left controller 3 and right controller 4 in the present example, an operation in vertical holding and an operation in lateral holding representing a plurality of operation schemes can be selected as described with reference to FIGS. 10 and 11. Some of registration information may be deleted or changed in accordance with an instruction from a user. For example, main body apparatus 2 may delete information on a designated controller and change information on a number provided to the controller, a player number, and an operation scheme in accordance with an instruction from a user. A functional block configuration of main body apparatus 2 based on the embodiment will now be described. FIG. 17 is a diagram illustrating a functional block configuration of main body apparatus 2 based on the embodiment. Referring to FIG. 17, a game execution processing module 302, a registration processing module 304, and a communication control module 310 are implemented by execution of a program by CPU 81 of main body apparatus 2. A program implementing the functional block is read, for example, from flash memory 84 of main body apparatus 2 or a memory card attached to the first slot, saved in DRAM 85, and executed. Communication control module 310 performs processing for communication with the controller as necessary. Game execution processing module 302 is a module controlling game processing and successively updates contents of representation on display 12 in accordance with contents of an operation by a user. Registration processing module 304 performs processing for pairing with a controller in wireless communication in wireless setting processing, obtains identification information of the controller, and updates registration information. Registration processing module 304 performs controller registration processing to have a player number registered and updated in the registration information in the flash memory. Registration processing module 304 registers an operation scheme of the controller as necessary. FIG. 18 is a flowchart illustrating one example of a flow of processing for registration of a controller performed in main body apparatus 2 based on the embodiment. Processing in each step in the flowchart shown in FIG. 18 is merely by way of example. So long as similar results can be obtained, an order of processing in the steps may be changed or another processing may be performed in addition to (or instead of) processing in each step. Though processing in each step in the flowchart is described as being performed by CPU 81 of main body apparatus 2 in the present embodiment, processing in some steps in the flowchart may be performed by a processor or a dedicated circuit other than CPU 81. A part of processing performed in main body apparatus 2 may be performed by another information processing apparatus which can communicate with main body apparatus 2 (for example, a server which can communicate with main body apparatus 2 through a network). Each processing shown in FIG. 18 may be performed by cooperation of a plurality of information processing apparatuses including main body apparatus 2. Referring to FIG. 18, CPU 81 makes setting (also called pairing) for establishing wireless communication between main body apparatus 2 and a controller (step S2). In the present embodiment, main body apparatus 2 performs wireless setting processing for making setting for wireless communication with a controller. CPU 81 determines whether or not pairing has been completed through wireless communication with the controller. When pairing has been completed, the process proceeds to a next step. When CPU 81 determines that pairing has not been completed through wireless communication with the controller, it has necessary registration information registered in the storage unit. Specifically, registration information stored in the storage unit is updated to add number information, identification information, and wireless communication information of the controller to registration information in association with one another. For example, information representing a number which has not been set for other registered controllers is set as number information. Identification information provided to the controller is set. As pairing is completed, information representing “set” is set. A player number and an operation scheme are set in subsequent processing. CPU 81 determines whether or not an instruction to register the controller has been given (step S4). In the present embodiment, an instruction to register the controller is given in response to transmission of a prescribed command from the controller to main body apparatus 2. By way of example, main body apparatus 2 performs processing for registering the controller by selecting an item for controller registration processing in a not-shown menu screen through the controller. Initially, when CPU 81 determines that an instruction to register the controller has been given (YES in step S4), it has a controller registration screen shown (step S20). CPU 81 maintains a state in step S4 until an instruction to register the controller is given. When an instruction to register the controller is given, registration processing module 304 has the controller registration screen as described with reference to FIG. 15 (A) shown. CPU 81 determines whether or not it has received operation data (step S22). Specifically, registration processing module 304 determines whether or not it has received operation data from the controller through communication control module 310. When CPU 81 does not receive operation data in step S22 (NO in step S22), it stands by until it receives operation data, and when it determines that it has received operation data (YES in step S22), it determines whether or not the operation data is operation data of the accessory controller (step S24). Specifically, registration processing module 304 determines whether or not the controller is the accessory controller based on the identification information in the received operation data. When CPU 81 determines in step S24 that the operation data is not operation data of the accessory controller (NO in step S24), it determines whether or not the operation data has second L button operation data and second R button operation data (step S26). Specifically, registration processing module 304 determines whether or not the received operation data includes second L button operation data and second R button operation data. When CPU 81 determines in step S26 that the operation data has second L button operation data and second R button operation data (YES in step S26), it has a player number for one controller registered (step S28). Specifically, registration processing module 304 has a player number registered in the registration information. The player number is registered in accordance with the order of registration of players. A player number P1 is registered for the first player, a player number P2 is registered for the second player, and so on. CPU 81 has the operation scheme in lateral holding registered in the registration information (step S30). Specifically, registration processing module 304 has information representing the operation scheme in lateral holding registered in a field of the operation scheme in the registration information. FIGS. 19A to 19C are diagrams illustrating operation data transmitted from the controller based on the embodiment to main body apparatus 2. FIG. 19A shows operation data 500 transmitted from controller 3b by way of example. Operation data 500 includes identification information data 501, second L button operation data 502, and second R button operation data 503. By way of example, second L button operation data 502 and second R button operation data 503 are operation data resulting when user PC presses both of second L button 43 and second R button 44 provided in left controller 3b. Though operation data of controller 3b is described, operation data of controller 4b is basically also similar. In the case of operation data of controller 4b, second L button operation data 502 and second R button operation data 503 are operation data resulting when user PD presses both of second L button 65 and second R button 66 provided in right controller 4b. Main body apparatus 2 can identify a type of a controller based on identification information data 501 included in operation data 500. In this case, when it is determined that the controller is not the accessory controller in accordance with identification information data 501, CPU 81 determines whether or not operation data 500 includes second L button operation data and second R button operation data. In this case, one controller is registered in operation data 500 based on second L button operation data 502 and second R button operation data 503. A player number is allocated to one controller. Main body apparatus 2 has the operation in lateral holding registered as the operation scheme in the registration information. Referring again to FIG. 18, CPU 81 updates the controller registration screen (step S32). Specifically, registration processing module 304 has an image of the controller set in accordance with the order of registration of players shown. For example, when a third player number is registered, a left controller operated as being laterally held is shown in a region third from the left in the controller registration screen. An indicator image showing that the third player number is set is shown as an indicator image. A corresponding notification LED in the left controller may be turned on in correspondence with the player number. CPU 81 determines whether or not controller registration processing has ended (step S34). Specifically, when the “A” button is selected in the controller registration screen described with reference to FIG. 15, registration processing module 304 determines that the controller registration processing has ended. When CPU 81 determines in step S34 that controller registration processing has ended (YES in step S34), the process ends (end). When CPU 81 determines that controller registration processing has not ended (NO in step S34), the process returns to step S22 and the process is repeated. When CPU 81 determines in step S26 that the operation data is not second L button operation data and second R button operation data (NO in step S26), it has a check image shown (step S35). Registration processing module 304 has the controller registration screen as described with reference to FIG. 15B shown. Specifically, by way of example, a check image shown in a region for player number P4 is shown. An image of the controller showing the operation scheme in lateral holding and an image of the controller showing the operation scheme in vertical holding are alternately shown. In this case, the image of the controller is shown in a region of a player number which has not yet been registered. CPU 81 determines whether or not it has received operation data (step S36). Specifically, registration processing module 304 determines whether or not it has further received operation data from the controller through communication control module 310. CPU 81 maintains a state in step S36 until it receives operation data. When CPU 81 determines in step S36 that it has received operation data (YES in step S36), the process proceeds to a next step S37. CPU 81 determines in step S37 whether or not first L button operation data and first R button operation data have simultaneously been received as the operation data. Specifically, registration processing module 304 determines whether or not one piece of a plurality of simultaneously received pieces of operation data includes the first L button operation data and the other piece of them includes the first R button operation data. When CPU 81 determines in step S37 that the first L button operation data and the first R button operation data have simultaneously been received as the operation data (YES in step S37), it has a player number for two controllers constituting a set registered (step S40). Specifically, registration processing module 304 has a player number registered in the registration information. The player number for two controllers is registered in accordance with the order of registration of players. A player number P1 is registered for the first player, a player number P2 is registered for the second player, and so on. Left controller 3 and right controller 4 constitute a set in the present example. Therefore, two left controllers or two right controllers do not constitute a set. Simultaneous reception of operation data is not limited to exactly the same timing of reception, and it is a concept encompassing also an example in which a period from reception of first operation data until reception of subsequent operation data is extremely short. CPU 81 has the operation scheme in vertical holding registered in the registration information (step S42). Specifically, registration processing module 304 has information representing the operation scheme in vertical holding registered in a field of the operation scheme in the registration information. FIG. 19B shows operation data 510 and 520 transmitted from controllers 3a and 4a, respectively, by way of example. Operation data 510 includes identification information data 512 and first L button operation data 514. Operation data 520 includes identification information data 522 and first R button operation data 524. By way of example, first L button operation data 514 is operation data resulting when user PA presses first L button 38 provided in left controller 3a. First R button operation data 524 is operation data resulting when user PA presses first R button 60 provided in right controller 4a. Main body apparatus 2 can identify a left controller based on identification information data 512 included in operation data 510. Main body apparatus 2 can identify a right controller based on identification information data 522 included in operation data 520. Main body apparatus 2 determines whether or not it has received the first L button operation data and the first R button operation data from the left controller and the right controller, respectively, and when it determines that the main body apparatus has received both of them, it has two controllers registered. A player number is allocated to the two controllers. Main body apparatus 2 has the operation in vertical holding registered as the operation scheme. Referring again to FIG. 18, CPU 81 updates the controller registration screen (step S32). Specifically, registration processing module 304 has an image of the controller set in accordance with the order of registration of players shown. For example, when the first player number is registered, a left controller and a right controller operated as being vertically held are shown in a region first from the left in the controller registration screen. An indicator image showing that the first player number is set is shown as an indicator image. Notification LEDs in the left controller and the right controller corresponding to the player number may be turned on. Since subsequent processing is similar, detailed description thereof will not be repeated. When CPU 81 determines in step S37 that the operation data does not have the first L button operation data or the first R button operation data (NO in step S37), CPU 81 determines whether or not the operation data has second L button operation data and second R button operation data (step S45). When CPU 81 determines that the operation data has second L button operation data and second R button operation data (YES in step S45), the process proceeds to “A”. A player number for one controller is registered (step S28). Specifically, registration processing module 304 has a player number registered in the registration information. The player number is registered in accordance with the order of registration of players. A player number P1 is registered for the first player, a player number P2 is registered for the second player, and so on. CPU 81 has the operation scheme in lateral holding registered in the registration information (step S30). Specifically, registration processing module 304 has information representing the operation scheme in lateral holding registered in a field of the operation scheme in the registration information. CPU 81 updates the controller registration screen (step S32). Specifically, registration processing module 304 has an image of the controller set in accordance with the order of registration of players shown. For example, when the third player number is registered, a left controller operated as being laterally held is shown in a region third from the left in the controller registration screen. An indicator image showing that the third player number is set is shown as an indicator image. A notification LED in the corresponding left controller may be turned on in correspondence with the player number. When CPU 81 determines in step S45 that the operation data does not have second L button operation data and second R button operation data (NO in step S45), the process proceeds to step S34 as determining that no operation scheme has been set. When CPU 81 determines in step S24 that the operation data is operation data of the accessory controller (YES in step S24), it determines whether or not the operation data has L button operation data and R button operation data (step S44. Specifically, registration processing module 304 determines whether or not the received operation data includes L button operation data and R button operation data. When CPU 81 determines in step S44 that the operation data has L button operation data and R button operation data (YES in step S44), it has a player number for the accessory controller registered (step S46). Specifically, registration processing module 304 has a player number registered in the registration information. The player number is registered in accordance with the order of registration of players. A player number P1 is registered for the first player, a player number P2 is registered for the second player, and so on. FIG. 19C shows operation data 530 transmitted from accessory controller 401 by way of example. Operation data 530 includes identification information data 532, L button operation data 534, and R button operation data 536. By way of example, L button operation data 534 and R button operation data 536 are operation data resulting when user PB presses both of L button 425L and R button 425R provided in accessory controller 401. Main body apparatus 2 can identify the accessory controller based on identification information data 532 included in operation data 530. Main body apparatus 2 has the accessory controller registered based on L button operation data 534 and R button operation data 536 included in operation data 530. A player number is allocated to the accessory controller. Since the accessory controller is not provided with a plurality of operation schemes, no operation scheme is registered therefor. Though description will be given later, whether or not operation data is converted is determined based on contents of registration of the operation scheme (whether or not the operation scheme is the operation scheme in vertical holding or the operation scheme in lateral holding), and therefore data on conversion may be registered also for the accessory controller. Specifically, no conversion may be registered as a conversion scheme. Referring again to FIG. 18, CPU 81 updates the controller registration screen (step S32). Specifically, registration processing module 304 has an image of the controller set in accordance with the order of registration of players shown. For example, when the second player number is registered, the accessory controller is shown in a region second from the left in the controller registration screen. An indicator image showing that the second player number is set is shown as an indicator image. A notification LED in the accessory controller corresponding to the player number may be turned on. Since subsequent processing is similar, detailed description thereof will not be repeated. When CPU 81 determines in step S44 that the operation data does not have L button operation data and R button operation data (NO in step S44), the process proceeds to step S34 as determining that no operation scheme has been set. Through the processing, controller registration processing can be performed based on operation data transmitted from each controller. In the controller registration processing, one operation scheme can be registered for a controller for which selection from among a plurality of operation schemes can be made based on operation contents of the operation data. Controller registration processing in connection with the operation scheme can thus be performed in a simplified manner and usability can be improved. In the controller registration processing, the operation scheme once registered can also be changed. For example, after the operation scheme in vertical holding using two controllers is registered, change to the operation scheme in lateral holding using one controller can also be made. Specifically, both of the second L button and the second R button are pressed in left controller 3 of two controllers registered as player number P1. Through the processing, operation data is transmitted from the left controller to main body apparatus 2. Main body apparatus 2 receives the operation data and performs processing for registering again the player and processing for registering lateral holding. The operation scheme of left controller 3 registered as player number P1 is changed to the operation scheme in lateral holding while the player number in the registration information is maintained. Information on allocation of the player number and the operation scheme in the registration information for right controller 4 registered as player number P1 is deleted. Though description is given for left controller 3, description is also the same for right controller 4, and processing for registering again the player and processing for registering lateral holding can similarly be performed. After the operation scheme in lateral holding using one controller is registered, change to the operation scheme in vertical holding using two controllers can also be made. Specifically, both of the first L button and the first R button in both of left controller 3 registered as player number P3 and right controller 4 registered as player number P4 are pressed. Through the processing, operation data is transmitted from left controller 3 and right controller 4 to main body apparatus 2. Main body apparatus 2 receives the operation data and performs processing for registering again the player and processing for registering vertical holding in accordance with the scheme described above. Left controller 3 registered as player number P3 and right controller 4 registered as player number P4 are determined as controllers constituting a set. In the registration information, the operation scheme of left controller 3 registered as player number P3 is changed to the operation scheme in vertical holding while the player number is maintained. The player number of right controller 4 registered as player number P4 is changed to player number P3 and the operation scheme thereof is changed to the operation scheme in vertical holding. [F. Game Processing] FIG. 20 is a diagram of one example illustrating game processing performed by game device 1 based on the embodiment. In FIG. 20, an image generated by game device 1 is shown on television 6. In the present example, four players are shown. User PA operates a corresponding object with two controllers 3a and 4a. User PB operates a corresponding object with accessory controller 401. User PC operates a corresponding object with one controller 3b. User PD operates a corresponding object with one controller 4b. In the present example, game device 1 divides a display area of television 6 into four sections, and shows an image for user PA (for example, an image including the first object) in a divided display area 6A and an image for user PB (for example, an image including the second object) in a divided display area 6B. Similarly, game device 1 shows an image for user PC (for example, an image including a third object) in a divided display area 6C and an image for user PD (for example, an image including a fourth object) in a divided display area 6D. Each controller controls a notification LED based on a player number from game device 1. In the present example, users PA to PD representing four players operate corresponding objects with the controllers, respectively. This is also applicable to an example in which there is one player. [G. Processing Procedure] A processing procedure involved with game processing in game device 1 based on the embodiment will now be described. FIG. 21 is a flowchart showing a processing procedure involved with the game processing based on the embodiment. Each step shown in FIG. 21 is typically performed by execution of a program by CPU 81 of main body apparatus 2. Referring to FIG. 21, CPU 81 determines whether or not start of game processing has been indicated (step S50). Game execution processing module 302 determines whether or not start of game processing has been indicated. When CPU 81 determines that start of game processing has been indicated (YES in step S50), it generates a game image in which an object is arranged in a game space (step S51). Game execution processing module 302 generates a game image in which an object is arranged in a game space based on a program saved and executed in DRAM 85. Then, CPU 81 determines whether or not it has obtained operation data (step S52). Specifically, game execution processing module 302 determines whether or not operation data has been obtained through communication control module 310. When CPU 81 determines in step S52 that it has obtained operation data (YES in step S52), it determines whether or not the operation data is operation data of the accessory controller (step S53). Specifically, game execution processing module 302 determines whether or not the controller is the accessory controller based on identification information in the received operation data described with reference to FIG. 20. When CPU 81 determines in step S53 that the operation data is not the operation data of the accessory controller (NO in step S53), it determines whether or not an operation in lateral holding has been registered (step S54). Specifically, game execution processing module 302 determines whether or not the operation scheme in lateral holding has been registered in the information on the operation scheme in the registration information for a controller corresponding to the obtained operation data, by referring to the registration information stored in flash memory 84. When CPU 81 determines in step S54 that the operation in lateral holding has not been registered (NO in step S54), it performs processing based on the operation data (step S56). Specifically, when game execution processing module 302 determines that the operation scheme in lateral holding has not been registered in the information on the operation scheme in the registration information for the controller corresponding to the obtained operation data by referring to the registration information stored in flash memory 84, it performs game processing based on the obtained operation data. Then, CPU 81 updates the game image (step S58). Specifically, game execution processing module 302 generates a game image in accordance with the operation data in accordance with an obtained operation by a user. Then, updated output is given to television 6 in accordance with the generated game image. Then, CPU 81 determines whether or not end of game processing has been indicated (step S60). When CPU 81 determines in step S60 that end of game processing has been indicated (YES in step S60), the process ends (end). When CPU 81 determines in step S60 that end of game processing has not been indicated (NO in step S60), the process returns to step S52 and the process is repeated. When CPU 81 determines in step S53 that the operation data is the operation data of the accessory controller (YES in step S53), it performs processing based on the operation data (step S56). Specifically, when game execution processing module 302 determines that the operation data is the operation data of the accessory controller, it performs game processing based on the obtained operation data. Then, CPU 81 updates the game image (step S58). Specifically, game execution processing module 302 generates a game image in accordance with the operation data in accordance with an obtained operation by a user. Then, updated output is given to television 6 in accordance with the generated game image. Since subsequent processing is similar, detailed description thereof will not be repeated. When CPU 81 determines in step S54 that the operation in lateral holding has been registered (YES in step S54), it performs processing for converting operation data into converted operation data (step S62). Specifically, when game execution processing module 302 determines that the operation scheme in lateral holding has been registered in the information on the operation scheme in the registration information for the controller corresponding to the obtained operation data by referring to the registration information stored in flash memory 84, it performs processing for converting the operation data into converted operation data. Specifically, in the case of left controller 3, conversion to such converted operation data that a direction instruction from analog stick 32 is rotated counterclockwise by 90° is made. Thus, an instruction from left controller 3 operated as being laterally held onto an object can be the same in direction as a direction instruction from analog stick 32 of left controller 3 operated as being vertically held. Functions of four operation buttons 33 to 36 are allocated to the X button, the A button, the Y button, and the B button, respectively. Thus, the operation buttons in left controller 3 operated as being laterally held for an object can be the same in function as four operation buttons 33 to 36 under the operation scheme in vertical holding. In the case of right controller 4, conversion to such converted operation data that a direction instruction from analog stick 52 is rotated clockwise by 90° is made. Thus, an instruction from right controller 4 operated as being laterally held onto an object can be the same in direction as a direction instruction from analog stick 52 of right controller 4 operated as being vertically held. Functions of four operation buttons 53 to 56 are allocated to the B button, the Y button, the A button, and the X button, respectively. Thus, the operation buttons in right controller 4 operated as being laterally held for an object can be the same in function as four operation buttons 53 to 56 under the operation scheme in vertical holding. Then, CPU 81 performs processing based on the converted operation data (step S64). Specifically, game execution processing module 302 generates a game image in accordance with the converted operation data. Then, updated output is given to television 6 in accordance with the generated game image. Since subsequent processing is similar, detailed description thereof will not be repeated. Then, CPU 81 updates the game image (step S58). Specifically, game execution processing module 302 generates a game image in accordance with operation data in accordance with an obtained operation by a user. Then, updated output is given to television 6 in accordance with the generated game image. Since subsequent processing is similar, detailed description thereof will not be repeated. An application executable on a personal computer may be provided as a program in the present embodiment. The program according to the present embodiment may be incorporated as some functions of various application programs executed on the personal computer. Though embodiments of the present invention have been described, it should be understood that the embodiments disclosed herein are illustrative and non-restrictive in every respect. The scope of the present invention is defined by the terms of the claims and is intended to include any modifications within the scope and meaning equivalent to the terms of the claims. While certain example systems, methods, devices, and apparatuses have been described herein, it is to be understood that the appended claims are not to be limited to the systems, methods, devices, and apparatuses disclosed, but on the contrary, are intended to cover various modifications and equivalent arrangements included within the spirit and scope of the appended claims."},"background":{"kind":"string","value":"<SOH> BACKGROUND AND SUMMARY <EOH>In a game system representing one example of a conventional information processing system, when a game controller representing an operation apparatus is registered in correspondence with a player number, the game controller may be registered by successively performing the same prescribed operation onto each game controller. Selection from among a plurality of operation schemes can be made for an operation apparatus in some cases. In such a case, though an operation scheme should also be registered, successive registration complicates a procedure for registration and there is a room for improvement in usability. The present disclosure is provided to solve the above-described problems and an object thereof is to provide an information processing system which can achieve improved usability, an information processing apparatus, a method of controlling an information processing apparatus, and an information processing program. An information processing system according to one aspect includes an operation apparatus and a main body apparatus which is capable of communicating with the operation apparatus. The operation apparatus includes a first transceiver which transmits operation data representing an operation by a user to the main body apparatus. The main body apparatus includes a memory in which an operation scheme of the operation apparatus is registered, a second transceiver which receives the operation data transmitted from the first transceiver, and a controller. The controller registers the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the second transceiver indicates a first operation and registers the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the second transceiver indicates a second operation, and performs processing based on the operation scheme registered in the memory onto the operation data received by the second transceiver. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. In the exemplary embodiment, the operation apparatus further includes a first operation portion and a second operation portion. The controller may register the operation scheme of the operation apparatus in the memory as the first operation scheme when the operation data received by the second transceiver indicates the first operation of the first operation portion and register the operation scheme of the operation apparatus in the memory as the second operation scheme when the operation data received by the second transceiver indicates the second operation of the second operation portion. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme based on the operation data transmitted from the first operation portion and register the operation scheme of the operation apparatus in the memory as the second operation scheme based on the operation data transmitted from the second operation portion. Therefore, since the operation scheme of the operation apparatus is registered based on the operation data from different operation portions, registration processing can readily be performed and usability can be improved. In the exemplary embodiment, the first operation portion and the second operation portion may be disposed on different surfaces of a housing of the operation apparatus, respectively. Since the first operation portion and the second operation portion are provided on different surfaces of the housing, respectively, registration processing can readily be performed without confusion and usability can be improved. In the exemplary embodiment, the operation apparatus further includes a third operation portion. The controller may perform processing on operation data of the third operation portion received by the second transceiver differently between the first operation scheme and the second operation scheme registered in the memory. The controller can perform appropriate processing in accordance with the operation scheme by performing processing on the operation data of the third operation portion differently between the first operation scheme and the second operation scheme. In the exemplary embodiment, the controller may perform prescribed processing on the operation data of the third operation portion received by the second transceiver when the first operation scheme is registered in the memory, and convert the operation data of the third operation portion received by the second transceiver into converted operation data when the second operation scheme is registered in the memory and perform the prescribed processing based on the converted operation data. When the second operation scheme is registered, the controller converts the operation data into converted operation data and performs prescribed processing based on the converted operation data. Therefore, even when the second operation scheme is registered, it is not necessary to change prescribed processing in accordance with the operation scheme by conversion to converted operation data corresponding to the operation data under the first operation scheme and processing can readily be realized. In the exemplary embodiment, the operation data of the third operation portion includes direction data representing a direction of input. The controller may perform the prescribed processing on the direction data of the third operation portion received by the second transceiver when the first operation scheme is registered in the memory and convert the direction data of the third operation portion received by the second transceiver into converted direction data different in direction of input from the direction data when the second operation scheme is registered in the memory and perform the prescribed processing based on the converted direction data. In the exemplary embodiment, the first and second operation portions may be disposed on identical sides of prescribed operation surfaces of a housing of the operation apparatus, respectively when the user performs an operation under any of the first and second operation schemes. The first and second operation portions are provided on the side of the prescribed operation surface of the housing of the operation apparatus when the user performs an operation under each of the first operation scheme and the second operation scheme so that an intuitive operation in selection of the operation scheme can be performed and usability can be improved. In the exemplary embodiment, a plurality of operation apparatuses are provided, and when a plurality of pieces of the operation data received by the second transceiver indicate the first operation, the controller may set a plurality of operation apparatuses as one set and register an operation scheme of the set of the operation apparatuses in the memory as the first operation scheme. Since the controller can make registration of one set of operation apparatuses in the memory based on a plurality of pieces of operation data transmitted from a plurality of operation apparatuses, registration processing can readily be performed and usability can be improved. In the exemplary embodiment, two operation apparatuses of the plurality of operation apparatuses are set as one set. The two operation apparatuses constituting the set may be designated in advance. By designating in advance two operation apparatuses to constitute a set, management of the operation apparatuses is facilitated and processing can be accelerated. In the exemplary embodiment, the controller registers the operation scheme of the set of the operation apparatuses in the memory as the first operation scheme when the plurality of pieces of operation data received by the second transceiver simultaneously indicate the first operation. Since the controller can make registration of one set of operation apparatuses in the memory when a plurality of pieces of operation data transmitted from a plurality of operation apparatuses simultaneously indicate the first operation, one set of operation apparatuses can easily be distinguished and registration processing can readily be performed. An information processing apparatus which is capable of communicating with an operation apparatus according to one aspect includes a memory in which an operation scheme of the operation apparatus is registered, a transceiver which receives operation data transmitted from the operation apparatus, and a controller. The controller registers the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the transceiver indicates a first operation and registers the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the transceiver indicates a second operation, and performs processing based on the operation scheme registered in the memory onto the operation data received by the transceiver. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. A method of controlling an information processing apparatus which is capable of communicating with an operation apparatus according to one aspect includes receiving operation data transmitted from the operation apparatus, registering an operation scheme of the operation apparatus in a storage unit as a first operation scheme when the received operation data indicates a first operation, registering the operation scheme of the operation apparatus in the storage unit as a second operation scheme when the received operation data indicates a second operation, and performing processing based on the operation scheme registered in the storage unit onto the received operation data. In the registering an operation scheme, the operation scheme of the operation apparatus can be registered in the storage unit as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. A non-transitory storage medium encoded with a program readable by a computer of an information processing apparatus which is capable of communicating with an operation apparatus according to one aspect is provided. The program causes the computer to perform receiving operation data transmitted from the operation apparatus, registering an operation scheme of the operation apparatus in a memory as a first operation scheme when the received operation data indicates a first operation, registering the operation scheme of the operation apparatus in the memory as a second operation scheme when the received operation data indicates a second operation, and performing processing based on the operation scheme registered in the memory onto the received operation data. The computer can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. An information processing system according to one aspect includes a first operation apparatus, a second operation apparatus, and a main body apparatus which is capable of communicating with the first operation apparatus and the second operation apparatus. The first operation apparatus and the second operation apparatus each include a first transceiver which transmits operation data representing an operation by a user to the main body apparatus. The main body apparatus includes a memory in which operation schemes of the first operation apparatus and the second operation apparatus are registered, a second transceiver which receives the operation data transmitted from the first transceiver, and a controller. The controller sets, when a plurality of pieces of operation data received from the first operation apparatus and the second operation apparatus by the second transceiver indicate a first operation, the first operation apparatus and the second operation apparatus as one set and registers an operation scheme of the set in the memory as a first operation scheme, and registers, when the operation data received from any one of the first operation apparatus and the second operation apparatus by the second transceiver indicates a second operation, the operation scheme of any of the first operation apparatus and the second operation apparatus in the memory as a second operation scheme. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. In the exemplary embodiment, each of the first operation apparatus and the second operation apparatus further includes a first operation portion, a second operation portion, and a third operation portion. The controller registers the operation scheme in the memory as the first operation scheme when the plurality of pieces of operation data received from the first operation apparatus and the second operation apparatus by the second transceiver indicate the first operation of the first operation portion and registers the operation scheme in the memory as the second operation scheme when the operation data received from any one of the first operation apparatus and the second operation apparatus by the second transceiver indicates the second operation of the second operation portion and the third operation portion. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. The foregoing and other objects, features, aspects and advantages of the exemplary embodiments will become more apparent from the following detailed description of the exemplary embodiments when taken in conjunction with the accompanying drawings."},"summary":{"kind":"string","value":"<SOH> BACKGROUND AND SUMMARY <EOH>In a game system representing one example of a conventional information processing system, when a game controller representing an operation apparatus is registered in correspondence with a player number, the game controller may be registered by successively performing the same prescribed operation onto each game controller. Selection from among a plurality of operation schemes can be made for an operation apparatus in some cases. In such a case, though an operation scheme should also be registered, successive registration complicates a procedure for registration and there is a room for improvement in usability. The present disclosure is provided to solve the above-described problems and an object thereof is to provide an information processing system which can achieve improved usability, an information processing apparatus, a method of controlling an information processing apparatus, and an information processing program. An information processing system according to one aspect includes an operation apparatus and a main body apparatus which is capable of communicating with the operation apparatus. The operation apparatus includes a first transceiver which transmits operation data representing an operation by a user to the main body apparatus. The main body apparatus includes a memory in which an operation scheme of the operation apparatus is registered, a second transceiver which receives the operation data transmitted from the first transceiver, and a controller. The controller registers the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the second transceiver indicates a first operation and registers the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the second transceiver indicates a second operation, and performs processing based on the operation scheme registered in the memory onto the operation data received by the second transceiver. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. In the exemplary embodiment, the operation apparatus further includes a first operation portion and a second operation portion. The controller may register the operation scheme of the operation apparatus in the memory as the first operation scheme when the operation data received by the second transceiver indicates the first operation of the first operation portion and register the operation scheme of the operation apparatus in the memory as the second operation scheme when the operation data received by the second transceiver indicates the second operation of the second operation portion. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme based on the operation data transmitted from the first operation portion and register the operation scheme of the operation apparatus in the memory as the second operation scheme based on the operation data transmitted from the second operation portion. Therefore, since the operation scheme of the operation apparatus is registered based on the operation data from different operation portions, registration processing can readily be performed and usability can be improved. In the exemplary embodiment, the first operation portion and the second operation portion may be disposed on different surfaces of a housing of the operation apparatus, respectively. Since the first operation portion and the second operation portion are provided on different surfaces of the housing, respectively, registration processing can readily be performed without confusion and usability can be improved. In the exemplary embodiment, the operation apparatus further includes a third operation portion. The controller may perform processing on operation data of the third operation portion received by the second transceiver differently between the first operation scheme and the second operation scheme registered in the memory. The controller can perform appropriate processing in accordance with the operation scheme by performing processing on the operation data of the third operation portion differently between the first operation scheme and the second operation scheme. In the exemplary embodiment, the controller may perform prescribed processing on the operation data of the third operation portion received by the second transceiver when the first operation scheme is registered in the memory, and convert the operation data of the third operation portion received by the second transceiver into converted operation data when the second operation scheme is registered in the memory and perform the prescribed processing based on the converted operation data. When the second operation scheme is registered, the controller converts the operation data into converted operation data and performs prescribed processing based on the converted operation data. Therefore, even when the second operation scheme is registered, it is not necessary to change prescribed processing in accordance with the operation scheme by conversion to converted operation data corresponding to the operation data under the first operation scheme and processing can readily be realized. In the exemplary embodiment, the operation data of the third operation portion includes direction data representing a direction of input. The controller may perform the prescribed processing on the direction data of the third operation portion received by the second transceiver when the first operation scheme is registered in the memory and convert the direction data of the third operation portion received by the second transceiver into converted direction data different in direction of input from the direction data when the second operation scheme is registered in the memory and perform the prescribed processing based on the converted direction data. In the exemplary embodiment, the first and second operation portions may be disposed on identical sides of prescribed operation surfaces of a housing of the operation apparatus, respectively when the user performs an operation under any of the first and second operation schemes. The first and second operation portions are provided on the side of the prescribed operation surface of the housing of the operation apparatus when the user performs an operation under each of the first operation scheme and the second operation scheme so that an intuitive operation in selection of the operation scheme can be performed and usability can be improved. In the exemplary embodiment, a plurality of operation apparatuses are provided, and when a plurality of pieces of the operation data received by the second transceiver indicate the first operation, the controller may set a plurality of operation apparatuses as one set and register an operation scheme of the set of the operation apparatuses in the memory as the first operation scheme. Since the controller can make registration of one set of operation apparatuses in the memory based on a plurality of pieces of operation data transmitted from a plurality of operation apparatuses, registration processing can readily be performed and usability can be improved. In the exemplary embodiment, two operation apparatuses of the plurality of operation apparatuses are set as one set. The two operation apparatuses constituting the set may be designated in advance. By designating in advance two operation apparatuses to constitute a set, management of the operation apparatuses is facilitated and processing can be accelerated. In the exemplary embodiment, the controller registers the operation scheme of the set of the operation apparatuses in the memory as the first operation scheme when the plurality of pieces of operation data received by the second transceiver simultaneously indicate the first operation. Since the controller can make registration of one set of operation apparatuses in the memory when a plurality of pieces of operation data transmitted from a plurality of operation apparatuses simultaneously indicate the first operation, one set of operation apparatuses can easily be distinguished and registration processing can readily be performed. An information processing apparatus which is capable of communicating with an operation apparatus according to one aspect includes a memory in which an operation scheme of the operation apparatus is registered, a transceiver which receives operation data transmitted from the operation apparatus, and a controller. The controller registers the operation scheme of the operation apparatus in the memory as a first operation scheme when the operation data received by the transceiver indicates a first operation and registers the operation scheme of the operation apparatus in the memory as a second operation scheme when the operation data received by the transceiver indicates a second operation, and performs processing based on the operation scheme registered in the memory onto the operation data received by the transceiver. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. A method of controlling an information processing apparatus which is capable of communicating with an operation apparatus according to one aspect includes receiving operation data transmitted from the operation apparatus, registering an operation scheme of the operation apparatus in a storage unit as a first operation scheme when the received operation data indicates a first operation, registering the operation scheme of the operation apparatus in the storage unit as a second operation scheme when the received operation data indicates a second operation, and performing processing based on the operation scheme registered in the storage unit onto the received operation data. In the registering an operation scheme, the operation scheme of the operation apparatus can be registered in the storage unit as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. A non-transitory storage medium encoded with a program readable by a computer of an information processing apparatus which is capable of communicating with an operation apparatus according to one aspect is provided. The program causes the computer to perform receiving operation data transmitted from the operation apparatus, registering an operation scheme of the operation apparatus in a memory as a first operation scheme when the received operation data indicates a first operation, registering the operation scheme of the operation apparatus in the memory as a second operation scheme when the received operation data indicates a second operation, and performing processing based on the operation scheme registered in the memory onto the received operation data. The computer can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. An information processing system according to one aspect includes a first operation apparatus, a second operation apparatus, and a main body apparatus which is capable of communicating with the first operation apparatus and the second operation apparatus. The first operation apparatus and the second operation apparatus each include a first transceiver which transmits operation data representing an operation by a user to the main body apparatus. The main body apparatus includes a memory in which operation schemes of the first operation apparatus and the second operation apparatus are registered, a second transceiver which receives the operation data transmitted from the first transceiver, and a controller. The controller sets, when a plurality of pieces of operation data received from the first operation apparatus and the second operation apparatus by the second transceiver indicate a first operation, the first operation apparatus and the second operation apparatus as one set and registers an operation scheme of the set in the memory as a first operation scheme, and registers, when the operation data received from any one of the first operation apparatus and the second operation apparatus by the second transceiver indicates a second operation, the operation scheme of any of the first operation apparatus and the second operation apparatus in the memory as a second operation scheme. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. In the exemplary embodiment, each of the first operation apparatus and the second operation apparatus further includes a first operation portion, a second operation portion, and a third operation portion. The controller registers the operation scheme in the memory as the first operation scheme when the plurality of pieces of operation data received from the first operation apparatus and the second operation apparatus by the second transceiver indicate the first operation of the first operation portion and registers the operation scheme in the memory as the second operation scheme when the operation data received from any one of the first operation apparatus and the second operation apparatus by the second transceiver indicates the second operation of the second operation portion and the third operation portion. The controller can register the operation scheme of the operation apparatus in the memory as the first operation scheme or the second operation scheme based on the operation data transmitted from the operation apparatus. Therefore, processing for registering the operation scheme of the operation apparatus can readily be performed and usability can be improved. The foregoing and other objects, features, aspects and advantages of the exemplary embodiments will become more apparent from the following detailed description of the exemplary embodiments when taken in conjunction with the accompanying drawings."},"cpc_label":{"kind":"string","value":"A63F1322"},"filing_date":{"kind":"string","value":"20171002"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180510"},"examiner_id":{"kind":"string","value":"65883.0"},"ipc_label":{"kind":"string","value":"A63F1322"},"npe_litigated_count":{"kind":"number","value":0,"string":"0"},"examiner_full_name":{"kind":"string","value":"WILLIAMS, ROSS A"},"invention_title":{"kind":"string","value":"INFORMATION PROCESSING APPARATUS CAPABLE OF ACHIEVING IMPROVED USABILITY, METHOD OF CONTROLLING INFORMATION PROCESSING APPARATUS, NON-TRANSITORY STORAGE MEDIUM ENCODED WITH PROGRAM READABLE BY COMPUTER OF INFORMATION PROCESSING APPARATUS, AND INFORMATION PROCESSING SYSTEM"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":0,"string":"0"},"decision_as_of_2020":{"kind":"string","value":"ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"A63F"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32893,"cells":{"application_number":{"kind":"number","value":15724732,"string":"15,724,732"},"decision":{"kind":"string","value":"ACCEPTED"},"title":{"kind":"string","value":"MASK SYSTEM WITH SNAP-FIT SHROUD"},"abstract":{"kind":"string","value":"A shroud (1020) for a mask system includes a retaining portion structured to retain a frame (1040), a pair of upper headgear connectors (1024) each including an elongated arm (1026) and a slot (1027) at the free end of the arm adapted to receive a headgear strap, and a pair of lower headgear connectors (1025) each adapted to attach to a headgear strap. The retaining portion, the upper headgear connectors, and the lower headgear connectors are integrally formed as a one piece structure."},"claims":{"kind":"string","value":"1. A mask system, comprising: a frame defining a breathing chamber; a cushion provided to the frame and adapted to form a seal with the patient's face; and a shroud provided to the frame, wherein the shroud and the frame are co-molded with one another, the frame being constructed of a first, relatively soft, elastomeric material and the shroud being constructed of a second material that is more rigid than the frame, and at least a portion of the frame includes a concertina section having a plurality of folds, each of the folds having a side wall with the side walls of the folds becoming progressively longer away from the patient's face. 2. A mask system according to claim 1, wherein the frame is constructed of silicone. 3. A mask system according to claim 1, wherein the shroud is constructed of polycarbonate. 4. A mask system according to claim 1, wherein the concertina section is provided to a nasal bridge region of the frame. 5. A mask system according to claim 1, wherein the cushion is a full-face cushion. 6. A mask system according to claim 1, wherein the flexibility of the concertina section is variable. 7. A mask system according to claim 6, wherein the flexibility of the concertina section is variable by varying at least one of a number of folds, a wall thickness of each fold, and a depth of each fold. 8. A cushion module, comprising: a frame defining a breathing chamber; and a cushion adapted to form a seal with the patient's face, wherein the frame and the cushion are co-molded with one another, the cushion being constructed of a first, relatively soft, elastomeric material and the frame being constructed of a second material that is more rigid than the cushion, and at least a portion of the frame includes a concertina section. 9. A cushion module according to claim 8, wherein the concertina section includes a bellows structure with one or more folds. 10. A cushion module according to claim 9, wherein the flexibility of the concertina section is variable. 11. A cushion module according to claim 10, wherein the flexibility of the concertina section is variable by varying at least one of a number of folds, a wall thickness of each fold, and a depth of each fold. 12. A cushion module according to claim 8, wherein the concertina section is provided to a nasal bridge region of the frame. 13. A cushion module according to claim 8, wherein the cushion is a full-face cushion. 14. A mask system, comprising: a shroud; and a cushion module according to claim 8 provided to the shroud. 15. A mask system according to claim 14, wherein the shroud includes headgear connectors adapted to removably attach to respective headgear straps of headgear. 16. A mask system according to claim 15, wherein the shroud includes upper and lower headgear connectors on each side of the shroud. 17. A mask system according to claim 16, wherein each upper headgear connector includes an elongated arm and a slot at the free end of the arm adapted to receive a respective headgear strap in use. 18. A mask system according to claim 16, wherein each lower headgear connector includes a clip receptacle adapted to be removably interlocked with a headgear clip associated with a respective headgear strap. 19. A mask system according to claim 14, wherein the shroud includes an open construction that provides an annular retaining portion structured to retain the frame. 20. A mask system according to claim 14, further comprising an elbow adapted to be connected to an air delivery tube that delivers breathable gas to the patient."},"description":{"kind":"string","value":"CROSS-REFERENCE TO APPLICATION This application is a continuation of U.S. patent application Ser. No. 15/682,117, filed Aug. 21, 2017, pending, which is a continuation of U.S. patent application Ser. No. 15/440,972, filed Feb. 23, 2017, now U.S. Pat. No. 9,770,568, which is a continuation of U.S. patent application Ser. No. 13/964,280, filed Aug. 12, 2013, now U.S. Pat. No. 9,757,533, which is a continuation of U.S. application Ser. No. 13/745,077, now U.S. Pat. No. 8,528,561, filed on Jan. 18, 2013, which is a continuation of U.S. application Ser. No. 12/736,024, now U.S. Pat. No. 8,550,084, filed on Sep. 2, 2010, which is the U.S. National Stage of PCT/AU2009/000241, filed Feb. 27, 2009, which claims benefit to U.S. Provisional Application Nos. 61/064,406, filed Mar. 4, 2008, 61/071,893, filed May 23, 2008, and 61/136,617, filed Sep. 19, 2008, each of which is incorporated herein by reference in its entirety. FIELD OF THE INVENTION The present invention relates to a mask system used for treatment, e.g., of Sleep Disordered Breathing (SDB) with Continuous Positive Airway Pressure (CPAP) or Non-Invasive Positive Pressure Ventilation (NIPPV). BACKGROUND OF THE INVENTION Patient interfaces, such as a full-face or nasal mask systems, for use with blowers and flow generators in the treatment of sleep disordered breathing (SDB), typically include a soft face-contacting portion, such as a cushion, and a rigid or semi-rigid shell or frame. In use, the interface is held in a sealing position by headgear so as to enable a supply of air at positive pressure (e.g., 2-30 cm H2O) to be delivered to the patient's airways. One factor in the efficacy of therapy and compliance of patients with therapy is the comfort and fit of the patient interface. The present invention provides alternative arrangements of mask systems to enhance the efficacy of therapy and compliance of patients with therapy. SUMMARY OF THE INVENTION One aspect of the invention relates to a mask system provided without a forehead support adapted to engage the patient's forehead. Another aspect of the invention relates to a mask system including a frame and a shroud removably connected to the frame and adapted to attach headgear. Another aspect of the invention relates to a mask system including a frame defining a breathing chamber, a cushion provided to the frame and adapted to form a seal with the patient's face, and a shroud provided to the frame. The shroud and the frame are co-molded with one another. The frame is constructed of a first, relatively soft, elastomeric material and the shroud is constructed of a second material that is more rigid than the frame. At least a portion of the frame includes a concertina section having a plurality of folds. Each of the folds has a side wall with the side walls of the folds becoming progressively longer away from the patient's face. Another aspect of the invention relates to a cushion module including a frame defining a breathing chamber and a cushion adapted to form a seal with the patient's face. The frame and the cushion are co-molded with one another. The cushion is constructed of a first, relatively soft, elastomeric material and the frame is constructed of a second material that is more rigid than the cushion. At least a portion of the frame includes a concertina section. Another aspect of the invention relates to a method for constructing a cushion module. The method includes molding a first part of the cushion module with a first, relatively soft, elastomeric material, co-molding a second part of the cushion module to the first part with a second material that is more rigid than the first material, and molding at least a portion of the second part to include a concertina section. Another aspect of the invention relates to a shroud for a mask system including a retaining portion structured to retain a frame, a pair of upper headgear connectors each including an elongated arm and a slot at the free end of the arm adapted to receive a headgear strap, and a pair of lower headgear connectors each adapted to attach to a headgear strap, wherein the retaining portion, the upper headgear connectors, and the lower headgear connectors are integrally formed as a one piece structure. Another aspect of the invention relates to a mask system including a frame defining a breathing chamber, a cushion provided to the frame and adapted to form a seal with the patient's face, a shroud provided to the frame and adapted to attach headgear, and an elbow provided to the frame and adapted to be connected to an air delivery tube that delivers breathable gas to the patient. The shroud includes a retaining mechanism structured to establish a positive connection between the shroud and the frame. Another aspect of the invention relates to a mask system including a frame defining a breathing chamber and a cushion provided to the frame. The cushion includes a main body and a cushion, wherein the cushion is adapted to engage at least a portion of the patient's face. The cushion includes a base wall connected to an undercushion layer and a membrane, wherein the membrane extends around the perimeter of the cushion and contacts the patient's face. The undercushion layer is positioned underneath the membrane and supports the membrane. The under cushion layer provides differential support to the membrane at predetermined regions of the face. Another aspect of the invention relates to a mask assembly for use in medical applications having a top and bottom ends defined by its position relative to a patient's face, wherein the mask assembly is connected to a plurality of flexible straps, which are adapted to engage the patient's head. The flexible straps engage at least two elongated rigid arms integrally molded to a portion of the mask assembly, and wherein the elongated arms are molded to the mask assembly proximal to the top end of the mask assembly. Another aspect of the invention relates to a mask assembly for use in medical applications including a main body connected to a cushion adapted to cover nose and/or mouth and wherein the mask assembly is attached by a force substantially perpendicular towards the face and wherein the force is approximately constant along the length of the mask and is balanced by a portion of the cushion engaging the patient's cheeks. Another aspect of the invention relates to a cushion for use with a medical mask including an outer membrane layer adapted to sealably engage a face and an undercushion layer adapted to support the membrane layer. The membrane or undercushion layer includes a surface positioned between the two layers adapted to allow the layers to slide against the respective surface. Another aspect of the invention relates to a mask system including a frame defining a breathing chamber, a cushion provided to the frame and adapted to form a seal with the patient's face, and a releasable shroud adapted to engage a portion of the outer surface of the frame, wherein the shroud is connected to straps to position the mask system. Another aspect of the invention relates to a mask assembly for use in medical applications including an upper end and a lower end wherein the upper end is adapted to cover the nose and the lower end is adapted to cover the mouth of a patient. The mask assembly includes no forehead support and includes two stiffened members attached to the upper end on opposed sides of the mask assembly, and wherein the stiffened members include a general curved shape and adapted to avoid covering the patient's field of vision. Another aspect of the invention relates to a cushion for attaching to a medical mask, wherein the cushion is flexible and includes a membrane attached to the circumference of the cushion adapted to seal against the face of a patient, and at least one undercushion adapted to support the membrane and positioned underneath the membrane to prevent collapse of the membrane, in use. The membrane is softer than the undercushion. The undercushion in the regions of nasal bridge or chin is between 0 mm and 30 mm in height as measured between the base and the tip of the undercushion. Another aspect of the invention relates to a mask assembly for use in medical applications including an upper end and a lower end wherein the upper end is adapted to cover the nose and the lower end is adapted to cover the mouth of a patient. The mask assembly includes no forehead support and includes two stiffened members attached to the upper end on opposed sides of the mask assembly, and wherein the stiffened members include a general curved shape and adapted to avoid covering the patient's field of vision. In an alternative embodiment, the mask system may include a headgear connector or rigidizer structured to attach to the frame with a snap-fit, mechanical interlock, friction fit, and/or grommet arrangement (e.g., constructed of rubber). In an alternative embodiment, the mask system may include headgear having an arrangement of straps constructed of silicone and/or Breath-O-Prene™ material. Other aspects, features, and advantages of this invention will become apparent from the following detailed description when taken in conjunction with the accompanying drawings, which are a part of this disclosure and which illustrate, by way of example, principles of this invention. BRIEF DESCRIPTION OF THE DRAWINGS The accompanying drawings facilitate an understanding of the various embodiments of this invention. In such drawings: FIG. 1 is a front perspective view of a mask system according to an embodiment of the present invention: FIG. 1B is a perspective view showing the mask system of FIG. 1 with headgear positioned on a patient's head; FIG. 1C is a cross-sectional view through the mask system of FIG. 1; FIG. 1D is another cross-sectional view through the mask system of FIG. 1; FIG. 1E is a side view of the mask system of FIG. 1; FIG. 2 is a front perspective view showing the frame and cushion of the mask system of FIG. 1; FIG. 3 is an exploded perspective view of the mask system of FIG. 1 showing the frame, cushion, shroud, and elbow; FIG. 4 is another exploded perspective view of the mask system of FIG. 1 showing the frame, cushion, and shroud; FIG. 5 is an exploded perspective view of the mask system of FIG. 1 showing the shroud and assembled frame/cushion: FIG. 6 is a front perspective view showing the shroud of the mask system of FIG. 1; FIG. 7 is a front perspective view showing the cushion of the mask system of FIG. 1; FIG. 8 is a cross-sectional view showing a portion of the cushion of FIG. 7: FIG. 8B is a cross-sectional view through nasal bridge and chin regions of the cushion of FIG. 7; FIG. 9 is a plan view of headgear laid out flat according to an embodiment of the present invention; FIG. 10 is a front perspective view of a mask system according to another embodiment of the present invention; FIG. 11 is a front perspective view showing the frame of the mask system of FIG. 10; FIG. 12 is a front view showing the frame of the mask system of FIG. 10: FIG. 13 is a side view showing the frame of the mask system of FIG. 10; FIG. 14 is a front perspective view showing the shroud of the mask system of FIG. 10: FIG. 15 is a front view showing the shroud of the mask system of FIG. 10; FIG. 16 is a side view showing the shroud of the mask system of FIG. 10: FIG. 17 is a rear perspective view showing the shroud of the mask system of FIG. 10; FIGS. 18-1 to 18-2 are cross-sectional views showing in sequential relation attachment of the shroud to the frame of the mask system of FIG. 10; FIGS. 19-1 to 19-4 are cross-sectional views showing in sequential relation attachment of the shroud to the frame of the mask system of FIG. 10: FIG. 20 is a perspective view showing an alternative arrangement for attaching the shroud to the frame; FIG. 21 is a rear perspective view showing the shroud of the mask system of FIG. 10: FIG. 22 is a cross-sectional view showing attachment of the shroud to the frame of the mask system of FIG. 10; FIG. 23 is a cross-sectional view showing attachment of the shroud, frame, and elbow of the mask system of FIG. 10; FIG. 24 is a cross-sectional view showing an alternative arrangement for attaching the shroud to the frame; FIG. 25 is a front perspective view of a mask system according to another embodiment of the present invention; FIG. 26 is a rear perspective view of the mask system of FIG. 25: FIG. 27 is a front perspective view of a mask system according to another embodiment of the present invention; FIG. 28 is an exploded view of the mask system shown in FIG. 27; FIG. 29 is an enlarged front perspective view of the mask system shown in FIG. 17; FIG. 30 is a side view of the mask system shown in FIG. 27: FIGS. 31-1 is a rear view of a cushion according to an embodiment of the present invention; FIG. 31-2 is a front view of the cushion shown in FIG. 31-1 with a partial cut-away: FIG. 31-3 is a cross-section view through line 31-3-31-3 in FIG. 31-1: FIG. 31-4 is a cross-section view through line 31-4-31-4 in FIG. 31-1: FIG. 31-5 is a cross-section view through line 31-5-31-5 in FIG. 31-1; FIGS. 32-1 to 32-3 illustrate top, front, and side views respectively of a concertina section according to an embodiment of the present invention; FIG. 33 is a side view of a mask system according to a variation of the present invention; FIG. 34 illustrates a cushion including a concertina section according to an embodiment of the present invention: FIGS. 35-1 to 35-3 are front, side, and rear views of a mask system according to another embodiment of the present invention; FIG. 36 is a perspective view of a shroud for a mask system according to an embodiment of the present invention: FIGS. 37-1 to 37-3 are perspective, front, and side views of a mask system according to another embodiment of the present invention; FIGS. 38-1 to 38-5 are perspective, front, top, side, and bottom views of a shroud of the mask system shown in FIGS. 37-1 to 37-3: FIGS. 39-1 to 39-6 are perspective, front, side, bottom, and top views of a mask system according to another embodiment of the present invention: FIGS. 40-1 and 40-2 are perspective and side views of a mask system according to another embodiment of the present invention: FIG. 40-3 is a perspective view of the frame of the mask system shown in FIGS. 40-1 and 40-2; FIGS. 40-4 and 40-5 illustrate a retaining member of the frame shown in FIG. 40-3; FIGS. 40-6 and 40-7 illustrate a clip-on upper headgear connector of the mask system shown in FIGS. 40-1 and 40-2; FIGS. 41-1 and 41-2 are rear and front perspective views of a mask system according to another embodiment of the present invention; FIGS. 41-3 and 41-4 are exploded views of the mask system shown in FIGS. 41-1 and 41-2; FIGS. 41-5 to 41-12 are various views of a clip-on upper headgear connector of the mask system shown in FIGS. 41-1 and 41-2; FIG. 42-1 is a rear perspective view of a mask system according to another embodiment of the present invention; FIG. 42-2 is an exploded view of the mask system shown in FIG. 42-1; FIGS. 42-3 to 42-7 are various views of a clip-on upper headgear connector of the mask system shown in FIG. 42-1; FIGS. 43-1 to 43-4 are perspective, side, front, and rear views of a mask system according to another embodiment of the present invention; FIG. 44 illustrates a mask system according to another embodiment of the present invention; and FIG. 45 illustrates a mask system according to another embodiment of the present invention. DETAILED DESCRIPTION OF ILLUSTRATED EMBODIMENTS The following description is provided in relation to several embodiments or examples which may share common characteristics and features. It is to be understood that one or more features of any one embodiment or example may be combinable with one or more features of the other embodiments or examples. In addition, any single feature or combination of features in any of the embodiments or examples may constitute additional embodiments or examples. In this specification, the word “comprising” is to be understood in its “open” sense, that is, in the sense of “including”, and thus not limited to its “closed” sense, that is the sense of “consisting only of”. A corresponding meaning is to be attributed to the corresponding words “comprise”, “comprised” and “comprises” where they appear. The term “air” will be taken to include breathable gases, for example air with supplemental oxygen. The term “shroud” will be taken to include components that partially or fully cover a second component within the illustrated embodiments. In an embodiment, the shroud may include the component that partially covers or is mounted on the frame components of the illustrated embodiments. The term “positive connection” will be taken to include connections between components of the illustrated embodiments wherein connectors mounted on respective components are adapted to engage each other respectively. 1. Mask System Embodiments of the invention are directed towards a mask system provided without a forehead support adapted to engage the patient's forehead. Such arrangement provides the mask system with a less obtrusive arrangement which does not significantly affect the patient's field of view. Although the system is designed such that a forehead support is not required, such a forehead support can be added if desired. As described in greater detail below, the mask system includes a frame, a cushion provided to the frame and adapted to form a seal with the patient's face, a shroud provided to the frame and adapted to attach headgear, and an elbow provided to the frame and adapted to be connected to an air delivery tube that delivers breathable gas to the patient. Headgear may be removably attached to the shroud to maintain the mask system in a desired adjusted position on the patient's face. The mask system is intended for use in positive pressure therapy for users with Obstructive Sleep Apnea (OSA) or another respiratory disorder. While each embodiment below is described as including a full-face or oro-nasal interface type, each embodiment may be adapted for use with other suitable interface types. That is, the interface type is merely exemplary, and each embodiment may be adapted to include other interface types, e.g., nasal interface, nasal mask, nasal prongs, etc. 2. Stabilizing Mechanisms The stabilizing mechanisms (e.g., frame, shroud, headgear with associated headgear vectors) of a mask system according to embodiments of the invention are structured to accommodate the elimination of a forehead support from a full-face type interface. For example, a forehead support typically eliminates rotation of the mask system in the sagittal and coronal planes, so the mask system and headgear according to embodiments of the invention are structured to take on these functions since there is no forehead support. The headgear is connected to the top and bottom of the frame either directly or via the shroud, which shroud provides headgear connection points for headgear positioned and arranged to stably maintain the mask system in position on the patient's face. 2.1 Frame As shown in FIGS. 1, 1B-1E, and 2-5, the frame 1040 of the mask system 1010 is structured to maintain the cushion 1060, shroud 1020, and elbow 1070 in an operative position with respect to the patient's face. The frame 1040 is constructed (e.g., injection molded) from a more rigid material (e.g., polyurethane) than the cushion 1060 (made of, e.g., silicone), however other materials may function likely as well (e.g., polycarbonate). In an embodiment, the frame has a general wall thickness of about 1-2 mm. e.g., 1.5 mm. The frame 1040 defines a breathing chamber or cavity adapted to receive the patient's nose and mouth and provide air communication to the patient. One or the lower portion of the frame 1040 includes an opening 1046 adapted to receive or otherwise communicate with the elbow 1070 (e.g., swivel elbow) and another or upper portion of the frame 1040 includes a vent arrangement 1076 for gas washout. In addition, the upper portion of the frame 1040 includes an interfacing structure 1048 adapted to interface or otherwise removably connect to the shroud 1020. FIGS. 27-30 shows a mask system 10 including a frame 40 with a cushion 44 that provides a sealing portion or sealing ring adapted to form a seal with the patient's nose and/or mouth. Also, the frame 40 includes an opening 46 that is adapted to communicate with the elbow 70. 2.2 Shroud As shown in FIGS. 1 and 3-6, the shroud 1020 is connected to the frame 1040 and is structured to attach headgear to the mask system. In an embodiment, the shroud 1020 is constructed (e.g., injection molded) of a resilient material including but not limited to plastic or nylon (e.g., Nylon 12). However, the shroud may be constructed of other suitable materials, e.g., polycarbonate, polypropylene, thermoplastic elastomer (TPE), Pocan®, etc. In an embodiment, the shroud has a general wall thickness of about 1-2 mm, e.g., 1.3 mm. The top end of the shroud 1020 is adapted to be positioned proximal to the nasal bridge region or nose of the patient and the bottom end is adapted to be positioned proximal to the mouth or chin of the patient. The top end includes an opening or vent receiving hole 1021 to accommodate the vent arrangement 1076 that protrudes from the frame 1040, and the bottom end includes an opening or elbow hole 1032 to accommodate the elbow 1070 and elbow opening into the frame 1040 (e.g., shroud provides no contact with elbow when assembled). Upper headgear connectors 1024 extend from each side of the top end, and lower headgear connectors 1025 extend from each side of the lower end. The headgear connectors 1024, 1025 may be integrally molded or otherwise attached to the shroud. 2.2.1 Upper Headgear Connectors Each upper headgear connector 1024 includes an elongated arm 1026 and a slot or receiving hole 1027 at the free end of the arm 1026 adapted to receive a respective headgear strap. In use, the arms 1026 extend around the face of the patient in a generally concave angle below the eyes of the patient so as to avoid the patient's field of view, i.e., direct headgear away from the patient's eyes. For example, as shown in FIG. 1E, each arm 1026 may extend at an angle α between about 10-25° (e.g., 170) with respect to horizontal. That is, each arm 1026 is suitably formed, shaped, or contoured to follow the contours of the patient's face and avoid line of sight in use. In an embodiment, the shape of the arms may be generally arcuate and adapted to extend in a direction across the cheek of the patient, % while avoiding the eyes or limiting the field of vision. In an embodiment, the arms may be integrally molded to the shroud of the mask system. One possible advantage of molding the arms onto the shroud is that it greatly increases manufacturability and also the shroud may be easily replaced in the case of accidental breakage of the arms rather than replacing the complete mask system. Additionally, molding of the arms onto the shroud may greatly increase the strength of the connection and reduce or limit the actual likelihood of breakage of the arms. In an embodiment, the arms 1026 are at least semi-rigid (e.g., relatively rigid) so as to prevent up and down movement or bending of the arms relative to the face of the patient. Thus, the arms 1026 may act as rigidizers to effectively act as a level arrangement and generate a mechanical advantage wherein the pressure or force applied to top end of the mask system is readjusted to a fulcrum point being about the center of balance between the top and bottom ends of the mask system. In an embodiment, the arms are attached to the highest possible point relative to the mask system to additionally stabilize the configuration. In an embodiment, the fulcrum point or moment of pivoting is positioned between the upper and lower connection points of the straps, and wherein the design, angle, length and/or configuration of the arms 1026 may effectively adjust the fulcrum point. In the illustrated embodiment, the fulcrum point is shown to be between the vent arrangement and elbow of the mask system. Additionally, when positioned on the face, the mask system may have a fulcrum point around or about the region between the bottom of the patient's nose and lip area. This feature effectively stabilizes the mask system on the patient's face without the traditional need for a forehead support. The net result of the arms 1026 mounted in a position extending from the top end of the mask system around the face of the patient is that the mask system is more stable and reduces the net torsional forces experiences about the x-axis 1001 (see FIG. 1) for the mask system in use. Please note that the arms 1026 may be rigidly connected to the mask system in other suitable positions to generate a similar result. In an embodiment, the arms 1026 may be used to stabilize the mask system by contacting the patient's face at the cheeks. A cheek pad may be provided to the inner surface of the arm to support the arm on the patient's cheek in use. Also, the arms 1026 may be enveloped in a soft fabric sleeve to act as additional padding against the cheeks of the patient. The soft fabric sleeve may be in the configuration of an elastic tube covering a portion of the arms 1026. 2.2.2 Lower Headgear Connectors Each lower headgear connector 1025 includes an abbreviated arm and a clip receptacle 1031 at the free end of the arm adapted to be removably interlocked with a headgear clip associated with a respective headgear strap. The clips allow for easier positioning or donning/removal of the mask system. In an embodiment, the abbreviated arms and clips are also relatively rigid so as to prevent lateral movement of the arms along the y-axis 1002, relative to the mask system in use. FIGS. 27-30 illustrate an exemplary headgear clip 33 adapted to be removably interlocked with a clip receptacle 31. As best shown in FIG. 28, each clip 33 includes two spring arms 35 adapted to interlock with the respective clip receptacle 31 with a snap-fit and a slot 37 adapted to receive a respective headgear strap in use. 2.2.3 Alternative Headgear Connectors As shown in FIGS. 27-30, the arm 26 may be removably coupled to the shroud, e.g., arm 26 includes clip structure adapted to removably interlock with a clip receptacle provided to the shroud. This arrangement allows different styles of upper and lower headgear connectors to be used with the shroud, e.g., arms for both upper and lower headgear connectors, clips for both upper and lower headgear connectors, different length arms for upper and lower headgear connectors, etc. However, the shroud may provide other suitable arrangements for attaching headgear straps of headgear. Also, the shroud may include one or more additional components, e.g., forehead support. 2.2.4 Headgear Connector Positioning In the embodiment of FIGS. 1-6, the upper and lower headgear connectors 1024, 1025 provide headgear connection points that are as far from each other as possible (i.e., top and bottom of frame) to allow for greater adjustability (e.g., allows adjustment at the top and bottom of the mask system) and stability (e.g., anchor points spread out around the mask system so more secure on the patient's face). Also, the upper headgear connectors are positioned as close to the top of the mask system as possible without obstructing the patient's eyes in use. 2.2.5 Separate Shroud In the embodiment of FIGS. 1-6, the shroud 1020 is formed separately (e.g., molded) and attached to the frame 1040. Such arrangement facilitates molding of the shroud, allows different materials to be used for the frame and shroud (e.g., frame can be semi-rigid or rigid for stability and shroud with headgear rigidizers can be flexible for adjustment, allows the shroud to hide elbow retention features around elbow/frame opening for retaining elbow to frame (e.g., provides visual shroud for aesthetics), allows frame to be free of lower clip receptacles, allows shroud to be used with different size frames, and allows the shroud to be designed or stylized to minimize obtrusiveness of the mask system. The separate shroud may also allow the headgear, frame, cushion, and/or elbow to be replaced or washed independently. 2.2.6 Sleeves In an embodiment, soft fabric sleeves may be mounted on the upper and/or lower headgear connectors. For example, the sleeves may be elastic and adapted to slide over the arms of the headgear connectors to form a tight fit. In an embodiment, the sleeves form elastic tubes. The sleeves may be padded to increase the comfort of the mask system in use. The sleeves may be particularly useful where the arms of the headgear connectors contact the patient's skin, e.g., to protect the patient's skin from irritation. 2.2.7 Arm Extends Over the Patient's Ear FIGS. 35-1 to 35-3 and 36 illustrate a shroud 220 for mask system 210 according to another embodiment of the present invention. The shroud 220 includes an annular retaining portion 222 structured to retain the frame 240 and upper and lower headgear connectors 224, 225 on each side of the retaining portion 222. In the illustrated embodiment, the shroud 220 is integrally formed in one piece (e.g., see FIG. 36). In the illustrated embodiment, each upper headgear connector 224 includes an elongated arm 226 and a slot 227 at the free end of the arm 226 adapted to receive a respective rear strap 298 in use. As illustrated, the arm 226 is suitably contoured to extend along the cheeks and over the patient's ear just anterior of the patient's temple and retain the respective rear strap 298 in spaced relation over the patient's ear, e.g., to avoid the strap rubbing or irritating the patient's ear in use. Also, each arm 226 is structured to extend along and engage an upper strap 292 of the headgear in use. As illustrated, each arm 226 is secured to the upper strap 292 to add rigidity to the strap and stabilize the mask system on the patient's face in use. In addition, the strap 292 provides padding to the arm 226 on the patient's face in use. In an embodiment, the upper strap 292 may be fixed to the arm 226 by gluing or stitching for example. Alternatively, the arms 226 may be encapsulated by or inserted into respective straps 292 so that the arms 226 are substantially not visible. Each lower headgear connector 225 includes an abbreviated arm 228 with a slot 229 at the free end of the arm 229 adapted to receive a respective lower strap 294 in use. As illustrated, the arm 228 is suitably oriented to retain the respective lower strap 294 in spaced relation under the patient's ear, e.g., to avoid the strap rubbing or irritating the patient's ear in use. In an embodiment, each arm may be attached to the upper end of the mask system and curves below the patient's field of vision or eyes and curves upwards at an angle between about 10 to 20 degrees away from the horizontal axis. In an alternative embodiment, as shown in FIG. 36, each lower headgear connector 225 may include a clip receptacle 231 adapted to be removably interlocked with a headgear clip (not shown) associated with a respective lower strap 294. In an embodiment, the headgear clip receptacle and clip may be similar to that on ResMed's Mirage Liberty™ mask. Exemplary clip arrangements are disclosed in U.S. Patent Publication Nos. 2007/0144525 and 2006/0283461, each of which is incorporated herein by reference in its entirety. 2.2.8 Shroud without Upper Headgear Connector FIGS. 37-1 to 37-3 illustrate a mask system 310 according to another embodiment of the present invention. As illustrated, the mask system 310 includes a shroud 320, a frame 340, a cushion 344, and an elbow 370. As best shown in FIGS. 38-1 to 38-5, the shroud 320 includes an opening 322 structured to receive the elbow 370 and a headgear connector 325 on each side thereof. In the illustrated embodiment, each headgear connector 325 includes a clip receptacle 331 adapted to be removably interlocked with a headgear clip (not shown) associated with a respective lower headgear strap. The frame 340 is removably attached to the shroud 320, e.g., fingers and tabs 345 extending from opening 322 adapted to engage collar of frame 340. The frame 340 includes an upper headgear connector 324 on each upper side thereof. Each headgear connector 324 includes a clip retainer 333 adapted to be removably interlocked with a headgear clip (not shown) associated with a respective upper headgear strap. FIGS. 39-1 to 39-6 illustrate an alternative version of the mask system 310, which is indicated with similar reference numerals. As illustrated, the frame 340 is provided without upper headgear connectors, and the each clip receptacle 331 includes an alternative configuration (e.g., holes for snap-fit tabs on the clip). Also, the shroud 320 in FIGS. 39-1 to 39-6 includes support bars 329 structured to wrap around respective auxiliary ports 343, while the shroud 320 in FIGS. 37-1 to 38-5 includes support bars 329 that extend in front of respective auxiliary ports 343. 2.3 Headgear Headgear may be removably attached to the headgear connectors 1024, 1025 of the shroud 1020 to maintain the mask system 1010 in a desired position on the patient's face, e.g., see FIG. 1B. As shown in FIG. 9, the headgear 1090 includes a pair of upper and lower straps 1092, 1094 with the upper straps 1092 removably attached to respective upper headgear connectors 1024 and the lower straps 1094 removably attached to respective lower headgear connectors 1025. The free end of each strap may include a Velcro® tab structured to engage the remainder of the strap to secure the strap in place. Such Velcro® attachment also allows adjustment of the length of the straps. However, the upper and lower headgear straps may be secured to the shroud in any other suitable manners, e.g., adjustable ladder-lock arrangement, etc. The upper straps 1092 split at the crown of the patient's head to top straps 1096 (e.g., connected to one another by a buckle) adapted to pass over the top of the patient's head in use and rear straps 1098 adapted to pass behind the patient's head in use. In an embodiment, the headgear 1090 is structured to be self-supporting. In FIG. 9, the top straps 1096 are adapted to be connected to one another by a buckle. In an alternative embodiment, as shown in FIG. 27-30, headgear 90 may include upper and lower straps 92, 94, top strap 96, and rear strap 98, with the top straps 96 integral with one another. The upper straps 1092 are designed to adjust the position of the mask in a similar way that an adjustable forehead support would alter the position of the mask system, i.e., move the top of the mask system closer or further away from the patient's nasal bridge. Without the forehead support, the headgear is connected at the top and bottom of the mask frame 1040 via the shroud 1020, and in order to avoid the eyes and ears, the arm 1026 of the upper headgear connector extends at an angle. In doing so, the headgear vectors V1 and V2 (see FIGS. 1 and 1B) are aligned such that the mask system may have a tendency to ride up the patient's face (i.e., upper headgear connectors position upper headgear vectors upwardly from horizontal and lower headgear connectors position lower headgear vectors generally horizontal). By splitting the upper headgear strap 1092 at the crown of the patient's head (i.e., top and rear straps 1096, 1098), the upper headgear vectors are realigned to prevent the mask system from sliding up the patient's face. 2.3.1 Headgear Adjustment FIGS. 35-1 to 35-3 illustrate headgear 290 attached to the headgear connectors 224, 225 of the shroud 220 to maintain the mask system in a desired position on the patient's face. In the illustrated embodiment, the headgear 290 includes a pair of upper or top straps 292, a pair of lower or bottom straps 294, and a pair of rear straps 298. In use, the upper straps 292 are secured to respective upper connectors or arms 226, the lower straps 294 are removably attached to respective lower connectors via slots 229/clip arrangement 231, and the rear straps 298 are removably attached to respective upper connectors via slots 227. The upper straps 292 may include upper strap portions adapted to pass over the top of the patient's head and couple to one another, e.g., via a headgear buckle or adjustable ladder-lock arrangement 299. In the illustrated embodiment, the lower straps 294 and rear straps 298 are formed in one piece. This headgear arrangement allows adjustment to occur at three positions, i.e., upper straps 292 at the headgear buckle 299, lower straps 294 at the slot 229/clip 231 connection, and rear straps 298 at the slot 227 connection. As illustrated, the free end of each strap may include a hook and loop tab 295 (e.g., Velcro®) structured to engage the remainder of the strap to removably secure the strap in place. Such hook and loop attachment also facilitates adjustment of the length of the straps. In the illustrated embodiment, the lower straps 294 and rear straps 298 are adapted to join and pass behind the patient's head in use (e.g., see FIG. 35-3). As illustrated, the lower straps 294 join at an angle α (e.g., similar to the bottom strap in ResMed's Mirage Liberty mask) to prevent the strap from irritating the patient's neck and/or prevent movement of the strap due to movement of the patient's neck in use. In an embodiment, the headgear may be similar to that for ResMed's Mirage Liberty mask, however the top straps have been modified and there is an added rigidizer system. The top straps may be similar to ResMed's Swift style headgear, with the rigidizers extending along the sides. 2.3.2 Alternative Headgear Material FIGS. 43-1 to 43-4 illustrate a mask system 610 including a mask 615 and headgear 690 according to another embodiment of the present invention. In the illustrated embodiment, the headgear 690 includes an arrangement of straps wherein some of the straps are constructed of silicone and some of the straps are constructed of Breath-O-Prene™ material. However, the headgear may be constructed such that the straps are completely constructed of silicone or completely constructed of Breath-O-Prene™. As illustrated, the lower strap portion 692 of the headgear is constructed of Breath-O-Prene™ and extends along the cheeks and around the back of the patient's head. The upper strap portion 694 of the headgear is constructed of silicone and includes side straps 694(1) that extend along the upper cheek and over the patient's ear, a top strap 694(2) that extends over the top of the patient's head, rear straps 694(3) that extend behind the patient's head and connects to the lower strap portion 692 (see FIG. 43-4), and connecting portions 694(4) that extend from respective side straps 694(1) in front of the patient's ear and connect to the lower strap portion 692. The headgear straps may be connected to the mask in any suitable manner. For example, in the illustrated embodiment, the lower strap portion 692 is connected to the mask by a headgear clip arrangement and the upper strap portion 694 is connected to the mask using an elongated buckle 695 with buckle portions on each end thereof. In an embodiment, the headgear straps are arranged such that the force vectors applied by the headgear to the mask are substantially perpendicular to the mask and substantially parallel to one another (e.g., as shown by the arrows in FIG. 43-2). This arrangement enhances the mask seal as the headgear forces the mask directly into the patient's face. 3. Seal The seal (i.e., cushion) of the mask system is structured to accommodate the elimination of a forehead support from a full-face type interface. 3.1 Cushion As shown in FIGS. 1-5 and 7-8, the cushion 1060 is structured to interface with the frame 1040 and form a seal with the patient's nose and mouth in use. In the illustrated embodiment, the cushion is a full-face cushion adapted to engage the patient's face generally along nasal bridge, cheek, and lower lip/chin regions of the patient's face. However, other cushion interfaces are possible, e.g., nasal. The cushion 1060 is structured be more compliant or flexible (e.g., particularly in the nasal bridge region) to accommodate more movement due to loss of some stability without a forehead support. The cushion 1060 is constructed of a soft and flexible biocompatible material, e.g., such as silicone. In the illustrated embodiment, the cushion 1060 includes a dual wall configuration wherein the cushion comprises an undercushion or support wall 1062 underneath a membrane 1064 as shown in FIG. 8. The membrane 1064 is generally softer and less stiff than the undercushion 1062 and provides a seal against the patient's face in use. The membrane may be relatively thin to allow for wider fit range and better conformance to the patient's face in view of less mask stability with a forehead support. The undercushion is structured to generally support the membrane and prevents collapse of the membrane when the mask system is attached and tightened using the headgear. The membrane 1064 is generally concave and curves inwards towards the breathing chamber. The undercushion 1062 may also curve inwardly but is generally shorter, thicker, and more rigid than the membrane. In an embodiment, the undercushion 1062 at the regions of the nasal bridge and/or chin of the patient is shorter in height or completely absent and the height from the tip to base of the undercushion 1062 may be between about 0 mm and 30 mm. The membrane is generally longer than the undercushion 1062 at any given cross-section and may be between about 1 mm and 40 mm. For example, FIG. 8B illustrates a cross-section through nasal bridge and chin regions of the cushion to illustrate the membrane 1064 without an undercushion in these regions. In an embodiment, the undercushion 1062 may only be provided in selected regions of the mask system, e.g., where the mask system is to be pushed away from the patient's face. Certain pre-determined regions of the patient's face may be preferably avoided for applying pressure by the tightening of the headgear. In the illustrated embodiment, the nasal bridge and chin regions of the patient do not include an undercushion 1062. In these regions, the undercushion is only provided along lateral sides of the cushion (e.g., see FIG. 7) which press against the cheeks of a patient so as to more evenly distribute the force vectors applied by the mask system in use. In an embodiment, the undercushion may be relatively stiff along the cheek regions because these points of contact are acting as anchor points, i.e., holds mask system in position to provide effective seal. This configuration of avoiding the nasal bridge and chin of the patient may increase the comfort of the mask system for patients by reducing the pressure or force applied to sensitive areas or to protruding regions of the patient's face that experience relatively higher contact pressures. Additionally, this arrangement avoids the cushion pinching the nasal bridge of the patient when the mask system is adjusted. Additionally, the cushion of this embodiment may be noticeably softer in the regions of the nasal bridge and chin because of the absence of the undercushion. In an embodiment, the undercushion may include a variable height, stiffness, and/or thickness to generate a variable softness in the aforementioned predetermined regions of the face that require lighter support. In the illustrated embodiment, the cushion may be structured to seal lower down on the patient's nasal bridge and the eye sockets so that the cushion is less obtrusive. In an embodiment, the cushion may be generally frosted except at patient contacting surfaces where it is polished. In an embodiment, the frosting of the cushion may reduce restriction between the face and membrane and/or the membrane and undercushion. The frosting allows the surface of the membrane and undercushion to slide against each other's respective surface without the same restriction of unfrosted silicone. This feature may also prevent or limit sticking of the membrane to the undercushion components and also may generally improve the overall comfort and sealing properties of the cushion. Additionally, the frosting of the cushion may be easier to manufacture and may lead to a reduction of costs of manufacturing. The cushion may be constructed of frosted silicone or other suitable materials. 3.2 Cushion Lower on Nasal Bridge FIGS. 31-1 to 31-5 illustrate various views of a cushion 44 (e.g., constructed of silicone) according to an embodiment of the present invention. As illustrated, the cushion 44 includes a base wall 44(1) provided to the frame, an undercushion layer (UCL) 44(2) extending away from the base wall 44(1), and a membrane 44(3) provided to substantially cover the UCL 44(2) and provide a sealing structure. In the illustrated embodiment, the cushion 44 is structured to sit lower on the nasal bridge to reduce mask obtrusiveness and improve “line of sight” in use. Also, as best shown in FIGS. 31-3 and 31-5, the UCL 44(2) design in the nasal bridge region is structured to provide improved stability across the nasal bridge in use. As shown in FIGS. 31-1 and 31-3, the UCL is not provided in the lower lip/chin region. However, other arrangements of the UCL are possible, e.g., UCL around entire perimeter. In an embodiment of the cushion shown in FIGS. 31-1 to 31-5, D1 may be about 15-20 mm, e.g., 18.2 mm, D2 may be about 53-59 mm, e.g., 55.8 mm, D3 may be about 88-93 mm, e.g., 90 mm, D4 may be about 78-83 mm, e.g., 81.1, D5 may be about 58-63 mm, e.g., 60 mm, D6 may be about 95-100 mm, e.g., 98.1 mm, D7 may be about 57-62 mm. e.g., 59.7 mm, D8 may be about 77-82 mm, e.g., 79 mm, D9 may be about 88-93 mm, e.g., 90.7 mm, D10 may be about 30-35 mm, e.g., 33.1 mm, D11 may be about 14-19 mm. e.g., 16.4 mm, D12 may be about 8-13 mm, e.g., 9.6 mm. D13 may be about 0.3-0.5 mm, e.g., 0.35 mm, D14 may be about 0.4-0.6 mm, e.g., 0.5 mm, and D15 may be about 0.3-0.5 mm. e.g., 0.4 mm. Although specific dimensions and ranges are indicated, it is to be understood that these dimensions and ranges are merely exemplary and other dimensions and ranges are possible depending on application. For example, the exemplary dimensions may vary by 10-20% or more or less depending on application. 3.3 Cushion Higher on Nasal Bridge FIGS. 35-1 and 35-2 illustrate a full-face cushion 244 adapted to engage the patient's face generally along nasal bridge, cheek, and lower lip/chin regions of the patient's face. In this embodiment, the cushion 244 is structured such that it is positioned higher on the bridge of the nose for sealing and comfort (e.g., with respect to the cushion 44 described above). The cushion 244 may also be better for anthropometrics, i.e., the cushion will fit more people. In an embodiment, the cushion 244 may include a concertina section as described below (e.g., in the nasal bridge region) to enhance the flexibility of the cushion in use. 3.4 Concertina Section As best shown in FIGS. 30 and 33, a concertina section 50 may be provided in a nasal bridge region of the cushion and/or frame. As illustrated, the concertina section 50 includes a bellows structure with one or more folds 52 that provide a higher degree of flexibility or increased movement. That is, the concertina section 50 provides a higher level of adaptability or flexibility to the nasal bridge region of the cushion/frame which is a more sensitive region of the patient's face in use. Moreover, the concertina section 50 provides increased movement without compromising seal. FIGS. 32-1 to 32-3 illustrate various views of a concertina section 50 (isolated from the remainder of the cushion/frame) with one or more folds 52 according to an embodiment of the present invention. As best shown in FIG. 32-3, the folds may have different lengths, depths, and/or contours with respect to one another to optimize the concertina effect, e.g., provide sufficient degree of movement without compromising seal. For example, as shown in FIG. 32-3, each fold 52 includes a first side wall 52(1) and a second side wall 52(2) that interconnects adjacent side walls 52(1). In the illustrated embodiment, the first side walls 52(1) and/or the second side walls 52(2) may become progressively longer away from the patient's face. For example, the first side wall 52(1) and/or the second side wall 52(2) adjacent patient's face, or the combination of side walls 52(1) and 52(2), may have a length that is longer than and in some cases significantly longer than the adjacent side wall 52(1) and/or 52(2) (e.g., one side wall at least 25% greater than and up to 5× as long as the other side wall, e.g., 1×, 2×, 3×, or 4×). The folds may be constructed and arranged to provide a predetermined order of movement or folding, e.g., folds structured to fold in a sequential or progressive manner wherein one fold collapses before an adjacent fold collapses. For example, upon application of force, the folds closest to the patient's face may fold or collapse before the folds furthest from the patient's face. Also, the folds may be constructed and arranged to provide various degrees of fold or collapse, e.g., folds may fold or collapse more than others. In an embodiment of the concertina section shown in FIGS. 32-1 to 32-3, D1 may be about 50-60 mm, e.g., 55.7 mm, D2 may be about 5-15 mm, e.g., 9.7 mm, and D3 may be about 0.3-0.5 mm, e.g., 0.4 mm. Although specific dimensions and ranges are indicated, it is to be understood that these dimensions and ranges are merely exemplary and other dimensions and ranges are possible depending on application. For example, the exemplary dimensions may vary by 10-20% or more or less depending on application. It should be appreciated that a concertina section 50 may be provided in other regions of the cushion and/or frame, e.g., depending on patient comfort. For example, the concertina section 50 may be provided around the entire perimeter of the cushion and/or frame or may be provided in selected regions of the cushion and/or frame. Also, the flexibility of the concertina section 50 may be varied and may be varied in different regions of the cushion and/or frame, e.g., depending on patient comfort. For example, the cushion and/or frame may include a concertina section in the nasal bridge region with a relatively high degree of flexibility and a concertina section in the lower lip/chin region with a relatively low degree of flexibility. The flexibility of the concertina section 50 may be varied by varying the number of folds 52 (e.g., 1-5 folds), the wall lengths, the wall thickness of the folds 52, the depth of the folds 52, etc. As noted above, the cushion and frame may be co-molded of two parts with different materials/rigidities or may be integrally formed of the same material. In both embodiments, the concertina section may be provided in the frame and/or the cushion. In FIGS. 27-30, the cushion 44 and frame 40 are co-molded of two parts with the concertina section 50 provided in the frame 40. The frame 40 and cushion 44 include different rigidities in order to optimize the function of each part. For example, one part (i.e., cushion 44) may be constructed of a relatively soft, supple material to optimize the sealing effect and the other part (i.e., frame 40) may be constructed of a more rigid material to provide adequate support for the cushion while at the same time allowing a sufficient degree of movement to optimize the concertina effect. While the frame is more rigid than the cushion, the frame may be constructed of a flexible material to allow the concertina effect. In FIG. 33, the frame 40 and cushion 44 are integrally formed in one piece with the concertina section 50 provided in the frame 40. The material properties and/or dimensions may be selectively modified to optimize sealing and concertina effects. For both embodiments of FIGS. 27-30 and 33, it should be appreciated that the concertina section may be alternatively provided in the cushion 44 or in both the frame 40 and cushion 44. For example, FIG. 34 illustrates a concertina section 50 integrally formed with the cushion 44 in the nasal bridge region. 4. Elbow As shown in FIG. 3, the elbow 1070 (e.g., constructed of a relatively hard material such as polycarbonate or polypropylene) includes a first end portion 1074(1) and a second end portion 1074(2). The first end portion 1074(1) provides an interfacing structure structured to interface or otherwise attach to the frame 1040. The second end portion 1074(2) is adapted to be connected to an air delivery tube. 4.1 Elbow Connection to Frame The frame 1040 is structured to maintain the elbow 1070 in an operative position with respect to the patient's face. That is, the frame acts as a carrier and bearing surface for the elbow. The frame and elbow may connect with a friction fit, snap-fit, mechanical interlock, or other suitable attachment mechanism. However, other suitable arrangements for attaching the elbow to the frame are possible. In the illustrated embodiment, the elbow 1070 includes a series of tangs 1075 adapted to releasably engage within the opening 1032 of the frame 1040, e.g., with a snap-fit. The tangs 1075 hold the elbow in place (e.g., preferably a relatively airtight connection) and permit rotation or swiveling of the elbow with respect to the frame. That is, the elbow is rotatably attached to the frame so that the elbow may be rotated relative to the frame in use, e.g., 360° rotation. This arrangement allows the elbow to assume different orientations in use, e.g., depending on patient preference. For example, the elbow may assume a first orientation so that the elbow extends generally downwardly from the mask to direct the air delivery tube under the patient's head in use. Alternatively, the elbow may be rotated and assume a second orientation so that the elbow extends upwardly from the mask to direct the air delivery tube over the patient's head in use. In an embodiment, the frame and elbow may be constructed of dissimilar materials to prevent or at least reduce squeak between the components in use. The second end portion of the elbow may be provided to a swivel joint adapted to be connected to the air delivery tube. For example, FIGS. 27-30 illustrate a swivel joint 80 provided to the second end portion 74(2) of elbow 70. In the illustrated embodiment, the swivel joint 80 is provided to a short tube 82 (e.g., extendable and retractable tube) that interconnects the elbow with the air delivery tube. In an embodiment, the swivel joint 80 may be integrally formed in one piece with the short tube 82. 4.2 AAV The elbow 1070 includes a slot 1081 to receive an anti-asphyxia valve (AAV), a port 1079 that is selectively closed by a flap portion of the AAV (depending on the presence of pressurized gas), and structure for attaching the AAV, e.g., with a snap-fit. FIGS. 27-30 illustrate an exemplary AAV 85 including a flap portion 86 to selectively close port 79 in elbow 70. In this embodiment, a clip portion 88 is provided to the flap portion 86 for attaching the AAV 85 to the elbow 70. In the illustrated embodiment, the flap portion 86 and the clip portion 88 are co-molded with one another to form a one-piece, integrated component. However, the flap portion 86 and clip portion 88 may be secured to one another in other suitable manners, e.g., mechanical interlock. In an embodiment, the flap portion 86 may be constructed of a relatively soft elastomeric material (e.g., silicone) and the clip portion 88 may be constructed of a more rigid material (e.g., rigid plastic) for interfacing with the elbow 70. The clip portion 88 of the AAV 85 includes structure for removably interlocking with the elbow 70, e.g., with a snap-fit. For example, the clip portion 88 may include tabs structured to interlock with respective recesses/protrusions provided to the elbow. FIGS. 35-1 and 35-2 illustrate an elbow 270 including a port 279 that is selectively closed by a flap portion 286 of the AAV 285 (depending on the presence of pressurized gas). Also, FIGS. 37-1 to 37-3 illustrate elbow 370 including a port 379 and a slot 381 to retain the AAV. Alternative embodiments of the AAV are disclosed in PCT Application No. PCT/AU2006/000031, which is incorporated herein by reference in its entirety. 4.3 Large Diameter End Portion As shown in FIGS. 27-30, the first end portion 74(1) of the elbow 70 may provide a relatively large diameter which allows the potential for cleaner/smoother lines thereby contributing to the overall mask aesthetic and reduced obtrusiveness. In addition, the relatively large diameter elbow offers the potential for the patient's nose to protrude into the elbow cavity thereby permitting the mask to be brought closer to the patient's face (i.e., reduced obtrusiveness), less moment since center of gravity of mask is closer to the patient's face, and/or improved line of sight. 5. Modular Design The mask system provides a modular design that allows different styles and/or sizes of the frame (also referred to as a frame module), shroud (also referred to as a shroud module), cushion (also referred to as a cushion module), and/or elbow (also referred to as an elbow module) to be interchanged or mixed and matched with one another to provide a more customized mask system for the patient. In addition, such design allows selected modules to be easily replaced, e.g., treatment requirements change, worn out or damaged, etc. In an embodiment, the mask system may be provided with a number of different cushions, e.g., each having cushions of different styles and/or sizes (e.g., depending on patient preference and/or fit). For example, the non-face contacting side of each cushion may include a common or universal configuration for interfacing with the frame, and the face-contacting side of the cushion may include different styles and/or sizes. This provides a modular arrangement that allows the frame to be selectively (e.g., and removably) coupled to one of multiple cushion. For example, the different cushions may include different size cushions (e.g., small, medium, and large) and may include a different cushion structures. In an embodiment, the mask system may be provided with different shrouds, e.g., each shroud having a different style and/or size (e.g., shroud with different arrangement/style of headgear connectors, shroud with forehead support, different headgear vectors, etc). In an embodiment, the mask system may be provided with different frames, e.g., each frame having a different style and/or size (e.g., frame with different vent arrangement, small, medium, and large size frame, etc). In an embodiment, the mask system may be provided with a number of different elbows, e.g., each having a vent arrangement, AAV (in the case of an oro-nasal mask), and/or elbow of different styles and/or sizes. In the illustrated embodiment of FIGS. 27-30, the vent arrangement 76 and AAV 85 are structured to be removably attachable to the elbow 70. This provides a modular arrangement that allows the elbow to be selectively and removably coupled to one of multiple vent arrangements and/or AAVs. This also allows the vent arrangement and AAV to be easily replaced, e.g., if damaged. 5.1 Shroud to Frame Connection The shroud is mounted on the outer surface of the frame, e.g., preferably with a tight, conforming fit on the frame. 5.1.1 Upper Retaining Mechanism In the illustrated embodiment of FIGS. 1-5, the shroud 1020 is connected to the frame 1040 by an upper retaining mechanism or interfacing structure 1048 located on the top end of the frame and shroud. As shown in FIGS. 2 to 5, the upper retaining mechanism 1048 is in the form of two taper locks structured to secure the shroud 1020 on the frame 1040 and prevent unintentional disassembly particularly due to headgear forces. In this embodiment, opposing sides of the frame include a female slot 1055 adapted to receive a respective tang protrusion (which tapers along its length) on the underside of the shroud 1020. The tapered protrusion engages within a respective female slot, e.g., with a friction fit. FIGS. 10 to 19-4 show another embodiment of a mask system 1110 which more clearly illustrates an embodiment of the taper lock. FIGS. 10 to 17 show various views of the frame 1140, shroud 1120, and elbow 1170 of the mask system 1110. As best shown in FIGS. 11 to 13, opposing sides of the top end of the frame 1140 include a platform 1154 which provides a first female slot 1155(1). In addition, the space between the platform 1154 and the outer surface of the frame 1140 defines a second female slot 1155(2). As best shown in FIG. 17, opposing sides of the top end of the shroud 1120 include a tang protrusion 1156 on the underside of the shroud 1120. The tang protrusion 1156 includes a first tang 1156(1) and a second tang 1156(2) that extends generally transverse to the first tang 1156(1). As shown in FIGS. 18-1 and 18-2, each tang may taper along its length, i.e., thinner towards its free end. FIGS. 18-1 and 18-2 and 19-1 to 19-4 sequentially illustrate attachment of the shroud 1120 to the frame 1140. As illustrated, the tangs 115((1), 1156(2) of each tang protrusion 1156 are structured to engage with respective slots 1155(1). 1155(2), e.g., with a friction fit. As best shown in FIGS. 19-1 to 19-4, each slot 1155(2) includes lead-ins or guides 1157 that curve along their length (i.e., extend in vertical and horizontal direction) so as to guide the tang 1156(2) into the slot 1155(2) and aid assembly. FIGS. 18-2 and 19-4 show the tangs 1156(1), 1156(2) when fully inserted with respective slots 1155(1), 1155(2). In an alternative embodiment, as shown in FIG. 20, the upper retaining mechanism may include a clip-type arrangement. As illustrated, opposing sides of the top end of the frame 1240 provide a shoulder 1255(1) and a tapered protrusion 1255(2). Opposing sides of the top end of the shroud 1220 include a first tang 1256(1) and a second tang 1256(2) on the underside of the shroud 1220. In use, each first tang 1256(1) is engaged with the respective shoulder 1255(1) and the second tang 1256(2) is engaged or clipped onto the tapered protrusion 1255(2), e.g., with a snap-fit. 5.1.2 Lower Retaining Mechanism In an embodiment, the shroud may also be connected to the frame by a lower retaining mechanism located on the bottom end of the frame and shroud. For example, a retaining mechanism may be provided to the opening of the shroud which is structured to interlock or otherwise engage with the opening of the frame. For example, as shown in FIGS. 14, 15, 17, and 21, the opening 1132 of the shroud 1120 may include structure adapted to engage the collar 1149 surrounding the frame opening 1146 with a snap-fit. As illustrated, the shroud 1120 includes snap fingers 1145(1) (e.g., three snap fingers) and sandwich tabs 1145(2) (e.g., three sandwich tabs) that extend from the opening 1132. The snap fingers and sandwich tabs are alternatively spaced about the opening. In use, the snap fingers 1145(1) resiliently deflect (e.g., 0.5 mm deflection) and engage respective part-annular protrusions 1149(1) provided to the collar 1149 (e.g., see FIGS. 22 and 23) to provide an initial retention of the shroud 1120 to the frame 1140 (e.g., with allowable stresses), e.g., to facilitate assembly and disassembly. In addition, as the snap fingers 1145(1) engage respective protrusions 1149(1), the sandwich tabs 1145(2) are received in respective recesses 1149(2) provided to the end of the collar 1149 (e.g., see FIGS. 22 and 23). When the elbow 1170 is engaged with the frame 1140 (e.g., see FIG. 23), an annular protrusion 1171 on the elbow 1170 is positioned on an opposing side of the sandwich tabs 1145(2) so that the sandwich tabs 1145(2) are sandwiched between the collar 1149 and the elbow 1170. Thus, the sandwich tabs utilize elbow retention forces to retain the shroud on the frame during use. The elbow 1170 has a distal shoulder 1173 adapted to extend under the edge of the frame 1140 to retain the elbow to the frame. The snap fingers 1145(1) allow the shroud to connect to the frame independent of the elbow. In an alternative embodiment, as shown in FIG. 24, the shroud's lower section may be structured to clip to a single point below the collar. As illustrated, the lower end of the shroud 1320 includes a snap finger 1345 that is engaged or clipped onto a protrusion 1349(1) spaced below the collar 1349 of the frame 1340, e.g., with a snap-fit. In this embodiment, the protrusion 1349 extends from the cover enclosing auxiliary ports. This arrangement may facilitate molding of the collar on the frame, e.g., uniform thickness of the collar prevents molding distortions. In addition, removal of the protrusions 1149(1)/recesses 1449(2) from the collar may reduce the risk of leak. 5.1.3 Finger Grip In an embodiment, the outer surface of the frame 1040 may include finger grips or recessed portions 1097, which are positioned to be exposed under the shroud 1020. The finger grips are adapted to allow the patient an improved ability to grip the frame and/or shroud which is particularly useful when disengaging the shroud from the frame. 5.1.4 Alternative Interfacing Structure In an alternative embodiment, as shown in FIG. 27-30, the shroud 20 includes an open construction that provides an annular or part annular retaining portion 22 structured to retain the frame 40 and the elbow 70. As illustrated, the annular retaining portion 22 includes an interfacing structure 23 along an inner edge that is adapted to interface with or otherwise removably connect to an interfacing structure 48 along the outer perimeter of the frame 40 (e.g., see FIG. 28). In the illustrated embodiment, the interfacing structure 23 is in the form of opposed flanges 23(1) that are adapted to interlock with respective locking structures 48(1) provided on opposing sides of the frame 40. However, other suitable arrangements for attaching the frame 40 to the shroud 20 are possible, e.g., friction fit, snap-fit, mechanical interlock, or other suitable attachment mechanism. For example, the frame 40 may be coupled to the shroud 20 in a manner that allows the frame 40 to be locked in different angular positions with respect to the shroud 20, e.g., pivotally mounted. 5.1.5 Alternative Upper Headgear Connector FIGS. 40-1 to 40-7 illustrate a frame and a clip-on upper headgear connector or rigidizer according to another embodiment of the present invention. The frame 442 includes an opening 449 adapted to engage a frame shroud and/or elbow. Around and under the opening 449 is the u-shaped slot 402 for gas washout and auxiliary ports 443 on each side thereof. In this embodiment, each upper side of the frame 442 includes a retaining member 433 and an upper intermediate portion of the frame 442 includes retaining grooves 435, which are structured and arranged to retain an upper headgear connector or rigidizer 424. As best shown in FIGS. 40-6 and 40-7, the upper headgear connector 424 includes a pair of elongated arms or rigidizers 426 coupled by a pair of wire members 428. Each rigidizer 426 includes a slot 427 at its free end adapted to receive a respective headgear strap in use. In use, the upper headgear connector 424 is adapted to clip onto the frame 442 (e.g., see FIGS. 40-1 and 40-2). Specifically, intermediate portions of the wire members 428 are received in respective grooves 435 of the frame 442, and end portions of the wire members 428 extend through respective retaining members 433 with the rigidizers 426 providing a shoulder to interlock with respective retaining members 433. FIGS. 40-4 and 40-5 show an upper portion of a retaining member 433 to illustrate the groove 433(1) adapted to receive a respective wire. As illustrated, the end of the groove 433(1) includes tapered side walls 433(2) and drops off towards a rear side 433(3) to position the rigidizers 426 into interlocking engagement with the retaining member 433. FIGS. 41-1 to 41-12 illustrate an upper portion of a frame and a clip-on upper headgear connector or rigidizer according to another embodiment of the present invention. As illustrated, the upper portion of the frame 542 includes a retaining member 533 on each side thereof and a retaining groove 535 along an intermediate portion thereof, which are structured and arranged to retain an upper headgear connector or rigidizer 524. As best shown in FIGS. 41-5 and 41-12, the upper headgear connector 524 includes a pair of elongated arms or rigidizers 526 coupled by a connecting portion 528. Each rigidizer 526 includes a slot 527 at its free end adapted to receive a respective headgear strap in use. In addition, the upper headgear connector 524 includes a clip structure 525 on each side of the connecting portion 528. In use, the upper headgear connector 524 is adapted to clip onto the frame 542 (e.g., see FIGS. 41-1 and 41-2). Specifically, the connecting portion 528 is received in the groove 535 of the frame 542, and the clip structures 525 releasably interlock with respective retaining members 533. As best shown in FIGS. 41-3 and 41-4, each retaining member 533 provides a cross-bar, and each clip structure 525 provides a v-shaped configuration that is adapted to resiliently deflect through the cross-bar and provide a shoulder to releasably interlock with the cross-bar. FIGS. 42-1 to 42-7 illustrate an alternative embodiment for engaging the upper headgear connector with the frame. As illustrated, each retaining member 533 provides an open-ended cross-bar, and each clip structure 525 provides an elongated arm. In this embodiment, the cross-bar is structured to resiliently deflect to allow the clip structure 525 to extend through the cross-bar and releasably engage the cross-bar, e.g., with a friction fit. In addition, the upper headgear connector 524 of FIGS. 42-1 to 42-7 includes a c-shaped clip structure 529 adapted to interlock with a tab 549 provided to the frame 542 (see FIGS. 42-1 and 42-2). 5.1.6 Grommet Attachment FIGS. 44 and 45 illustrate an alternative mask arrangement in which the shroud is attached to the frame via a grommet. For example, as shown in FIG. 44, the frame 740 includes a grommet 745 (e.g., constructed of a rubber) and the shroud 720 includes an opening 725 adapted to receive the grommet 745 to secure the shroud 720 to the frame 740. As illustrated, the shroud 720 includes elongated upper and lower arms 724, 726 each with a slot 727 at its free end adapted to receive a respective headgear strap in use. FIG. 45 illustrates an alternative shroud 820 which includes a single arm with a slot 827 at each end adapted to receive a respective headgear strap in use. In addition, the shroud 820 provides an elongated inner slot 825 adapted to receive the grommet 745 of the frame 740. The elongated slot 825 allows the grommet 745 to be fixed in one of multiple positions along the length of the slot 825, in contrast to the shroud 720 which provides a single fixed position. In an embodiment, the shroud 820 may be slidable with respect to the grommet 745 to allow an infinite number of positions with respect to the frame 740. In each embodiment, the grommet 745 (e.g., constructed of a rubber) fixes the shroud in position but the inherent flexibility of the grommet provides a flexible connection to decouple the shroud from the frame and allow a range of movement between the two components, e.g., like a ball joint or gimbal. Such arrangement helps with fitting and sealing of the mask to the patient's face. That is, the flexible connection allows the mask to selectively adjust and/or self-fit with the patient's face. 5.2 Cushion to Frame Connection In FIGS. 1-8, the non-face contacting side of the cushion 1060 is connected to frame 1040 in a tongue and groove relationship. The tongue 1066 (see FIGS. 1C, 1D, and 8) of the cushion 1060 is inserted within a groove 1041 (see FIGS. 1C and 1D) provided along the perimeter of the frame 1040. The tongue and groove relationship may also include a locking lip or sealing lip 1068 (see FIGS. 1C, 1D, and 8) on the cushion that is adapted to interlock with an undercut bead 1042 (see FIGS. 1C and 1D) within the frame groove to fixably retain the cushion to the frame. In the illustrated embodiment, the cushion 1060 also includes one or more positioning features located around its circumference to assist with proper alignment of the cushion with the frame 1040. As shown in FIG. 7, the cushion 1060 includes notches and/or protrusions (e.g., two notches 1067 and one protrusion 1069) adapted to engage with complementary features in the frame, e.g., interlocking relationship. 5.2.1 Co-Molding Frame and Cushion In an embodiment, as shown in FIGS. 27-30, the frame 40 and cushion 44 may be co-molded with one another to form a one-piece, integrated component. For example, the frame 40 may be molded of a first material adapted to interface with the shroud 20 and the cushion 44 may be co-molded onto the frame 40 of a second material adapted to interface with patient's face. In such embodiment, the cushion 44 may be constructed of a relatively soft elastomeric material (e.g., silicone) for sealing and the frame 40 may be constructed of a more rigid material than the cushion 44 (e.g., polycarbonate, polypropylene) for interfacing with the frame. Co-molding the frame 40 to the cushion 44 provides a chemical bond without necessarily forming a mechanical interlock. As a result, the connection includes no cracks, a gas tight seal, and clean interface. Moreover, such co-molded connection relaxes tolerances as the mold materials are sufficiently flexible to fill in any gaps at the interface between the frame 40 and the cushion 44. Also, the co-molded frame/cushion provides a reduced part count (reduced cost) and facilitates assembly/disassembly to the shroud 20. In an alternative embodiment, as shown in FIG. 33, the frame 40 and cushion 44 may be integrally formed in one piece, e.g., of a silicone material. That is, the frame 40 may have the same shape and structure as described above, but be integrally molded of the same material, e.g., silicone. In an embodiment, the integrally formed frame 40/cushion 44 may be co-molded to the shroud 20, e.g., constructed of polycarbonate or polypropylene. For example, the shroud 20 may be constructed of a relatively rigid material (e.g., polycarbonate or polypropylene) and the frame 40/cushion 44 may be co-molded onto the shroud 20 of a relatively soft elastomeric material (e.g., silicone). 5.3 Vent Arrangement In FIGS. 1, 1B, IC, 1D, and 2-5, the vent arrangement 1076 is provided to the frame and includes a plurality of holes 1077 (e.g., 5-100 holes, e.g., 20-50 holes, or about 35 holes) oriented at an angle (e.g., 45°) on the outer surface of the frame so as ensure the exhausted air is directed away from the patient and preferably their bed partner when the patient is sleeping. As shown in FIGS. 1C and 1D, each hole 1077 may include a contour or taper along its length. However, it should be appreciated that the vent arrangement may include other suitable arrangements, e.g., different number of holes, hole arrangement, positioning on frame, vent provides part pf interlocking structure with shroud, etc. FIG. 35-1 illustrates a vent arrangement 276 provided to the frame 240 for gas washout. In the illustrated embodiment, the vent arrangement 276 is in the form of a vent insert (e.g., elastomeric vent insert) that is adapted to be removably supported within an outlet opening in the frame 240. The vent insert may be similar those described in U.S. Pat. Nos. 6,561,190, 6,561,191, and 7,207,335, each of which is incorporated herein by reference in its entirety. However, it should be appreciated that the vent arrangement may have other suitable forms (e.g., vent holes in main body, etc.). FIGS. 37-3, 39-2, and 39-4 illustrate a frame 340 that includes a u-shaped slot 302 that receives a u-shaped plug-type vent 305 for gas washout. As illustrated, the plug-type vent 305 wraps around and under the opening in the frame 340 for the elbow 370. The plug-type vent 305 includes a plurality of tracks or grooves 307 on each side thereof. In use, the grooved plug-type vent 305 forms a seal with the slot 302 so that exhausted air can exit between the slot walls and the grooves 307 on the plug-type vent 305. In an embodiment, the port caps 347 may be integrated or incorporated into the plug-type vent 305 (e.g., integrally formed in one piece). Further details of such a plug-type vent arrangement are provided in U.S. patent application Ser. No. 12/230,120, filed Aug. 22, 2008, which is incorporated herein by reference in its entirety. FIGS. 39-2 to 39-6 show the frame 340 with the grooved plug-type vent 305 removed so as to more clearly illustrate the u-shaped slot 302 and auxiliary ports 343 on each side thereof. Also, it should be appreciated that the vent arrangement may be provided to the elbow. For example, a shown in FIGS. 27-30, the vent arrangement 76 is in the form of a vent insert that is adapted to be removably supported within an outlet opening in the elbow 70. In an embodiment, the vent arrangement 76 includes a base adapted to be supported within the outlet opening, one or more grill components or media (e.g., filter, membrane, or other porous material) provided to the base and structured to diffuse vent flow, and a cover to maintain the grill components/media within the base. Only the cover 77 of the vent arrangement 76 is visible in FIGS. 27-30. Exemplary embodiments of such a vent arrangement are disclosed in U.S. patent application Ser. No. 12/230,120, filed Aug. 22, 2008, which is incorporated herein by reference in its entirety. However, it should be appreciated that the vent arrangement may include other suitable arrangements, e.g., vent insert with one or more vent holes. Also, the elbow may provide an alternative venting arrangement to the vent insert. For example, as indicated in dashed lines in FIG. 30, the first end portion 74(1) of the elbow 70 (e.g., along the interfacing structure 75) may include one or more vent holes 276 for gas washout. The one or more holes 276 may be provided to a soft part (e.g., silicone seal as described below) and/or a hard part (e.g., polycarbonate, polypropylene) of the elbow. The holes 276 may extend around the entire perimeter of the first end portion 74(1) or may extend along one or more portions of the first end portion 74(1). It is noted that providing vent holes along the entire perimeter of the elbow may help to disperse the vent flow in use. However, other suitable hole arrangements, hole numbers, and/or hole shapes along the first end portion 74(1) and/or other portions of the elbow are possible. 5.4 Ports In FIGS. 1-5, the base of the frame 1040 includes two ports 1043 positioned so that in use, oxygen or other breathable gas can be delivered close to the patient's nares or pressure monitoring equipment can be attached. The ports 1043 may also be used to attach additional medical equipment such as pressure or flow sensors. The ports may be selectively closable or sealable by a ports cap. In an alternative embodiment, as shown in FIGS. 25 and 26, the frame 1040 may include a side port 1043.1, e.g., in addition to or as an alternative to the ports 1043. FIGS. 35-1 and 35-2 show a frame 240 that includes an auxiliary port or spigot 243 on an upper portion of the frame, e.g., for supplemental oxygen, measurement device, etc. In FIGS. 37-1 to 37-3 and 39-1 to 39-6, the frame 340 includes an auxiliary port or spigot 343 on each side thereof, e.g., for supplemental oxygen, measurement device, etc. Port caps 347 are provided to seal respective ports 343. 6. Interface Seal In an embodiment, a seal may be provided at the interface between the elbow and the shroud, at the interface between the frame and the shroud, and/or at the interface between the elbow and the frame. For example, a seal (e.g., elastomeric, ring-shaped seal) may be formed separately from the modules and attached at the interface (e.g., sandwiched between modules, adhesive, etc.). Alternatively, a seal may be co-molded with one or more of the modules. In an embodiment, a silicone lip seal may be provided to the frame to seal against the elbow, thereby reducing leak. In another embodiment, as shown in FIG. 27-30, the interfacing structure 75 of the elbow 70 may be constructed of a relatively soft, sealing material (e.g., silicone, which may be co-molded to the harder material of the elbow) that is structured to provide a seal at the interface between the elbow 70 and the shroud 20. Also, the relatively soft interfacing structure 75 (e.g., silicone) provides a “soft” attachment to the relatively hard shroud 20 (e.g., polycarbonate, polypropylene) which may allow an interference type fit. As noted above, one or more vent holes may be provided to the softer interfacing structure and/or the harder elbow. While the invention has been described in connection with what are presently considered to be the most practical and preferred embodiments, it is to be understood that the invention is not to be limited to the disclosed embodiments, but on the contrary, is intended to cover various modifications and equivalent arrangements included within the spirit and scope of the invention. Also, the various embodiments described above may be implemented in conjunction with other embodiments, e.g., aspects of one embodiment may be combined with aspects of another embodiment to realize yet other embodiments. Further, each independent feature or component of any given assembly may constitute an additional embodiment. Furthermore, each individual component of any given assembly, one or more portions of an individual component of any given assembly, and various combinations of components from one or more embodiments may include one or more ornamental design features. In addition, while the invention has particular application to patients who suffer from OSA, it is to be appreciated that patients who suffer from other illnesses (e.g., congestive heart failure, diabetes, morbid obesity, stroke, bariatric surgery, etc.) can derive benefit from the above teachings. Moreover, the above teachings have applicability with patients and non-patients alike in non-medical applications."},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE INVENTION <EOH>Patient interfaces, such as a full-face or nasal mask systems, for use with blowers and flow generators in the treatment of sleep disordered breathing (SDB), typically include a soft face-contacting portion, such as a cushion, and a rigid or semi-rigid shell or frame. In use, the interface is held in a sealing position by headgear so as to enable a supply of air at positive pressure (e.g., 2-30 cm H 2 O) to be delivered to the patient's airways. One factor in the efficacy of therapy and compliance of patients with therapy is the comfort and fit of the patient interface. The present invention provides alternative arrangements of mask systems to enhance the efficacy of therapy and compliance of patients with therapy."},"summary":{"kind":"string","value":"<SOH> SUMMARY OF THE INVENTION <EOH>One aspect of the invention relates to a mask system provided without a forehead support adapted to engage the patient's forehead. Another aspect of the invention relates to a mask system including a frame and a shroud removably connected to the frame and adapted to attach headgear. Another aspect of the invention relates to a mask system including a frame defining a breathing chamber, a cushion provided to the frame and adapted to form a seal with the patient's face, and a shroud provided to the frame. The shroud and the frame are co-molded with one another. The frame is constructed of a first, relatively soft, elastomeric material and the shroud is constructed of a second material that is more rigid than the frame. At least a portion of the frame includes a concertina section having a plurality of folds. Each of the folds has a side wall with the side walls of the folds becoming progressively longer away from the patient's face. Another aspect of the invention relates to a cushion module including a frame defining a breathing chamber and a cushion adapted to form a seal with the patient's face. The frame and the cushion are co-molded with one another. The cushion is constructed of a first, relatively soft, elastomeric material and the frame is constructed of a second material that is more rigid than the cushion. At least a portion of the frame includes a concertina section. Another aspect of the invention relates to a method for constructing a cushion module. The method includes molding a first part of the cushion module with a first, relatively soft, elastomeric material, co-molding a second part of the cushion module to the first part with a second material that is more rigid than the first material, and molding at least a portion of the second part to include a concertina section. Another aspect of the invention relates to a shroud for a mask system including a retaining portion structured to retain a frame, a pair of upper headgear connectors each including an elongated arm and a slot at the free end of the arm adapted to receive a headgear strap, and a pair of lower headgear connectors each adapted to attach to a headgear strap, wherein the retaining portion, the upper headgear connectors, and the lower headgear connectors are integrally formed as a one piece structure. Another aspect of the invention relates to a mask system including a frame defining a breathing chamber, a cushion provided to the frame and adapted to form a seal with the patient's face, a shroud provided to the frame and adapted to attach headgear, and an elbow provided to the frame and adapted to be connected to an air delivery tube that delivers breathable gas to the patient. The shroud includes a retaining mechanism structured to establish a positive connection between the shroud and the frame. Another aspect of the invention relates to a mask system including a frame defining a breathing chamber and a cushion provided to the frame. The cushion includes a main body and a cushion, wherein the cushion is adapted to engage at least a portion of the patient's face. The cushion includes a base wall connected to an undercushion layer and a membrane, wherein the membrane extends around the perimeter of the cushion and contacts the patient's face. The undercushion layer is positioned underneath the membrane and supports the membrane. The under cushion layer provides differential support to the membrane at predetermined regions of the face. Another aspect of the invention relates to a mask assembly for use in medical applications having a top and bottom ends defined by its position relative to a patient's face, wherein the mask assembly is connected to a plurality of flexible straps, which are adapted to engage the patient's head. The flexible straps engage at least two elongated rigid arms integrally molded to a portion of the mask assembly, and wherein the elongated arms are molded to the mask assembly proximal to the top end of the mask assembly. Another aspect of the invention relates to a mask assembly for use in medical applications including a main body connected to a cushion adapted to cover nose and/or mouth and wherein the mask assembly is attached by a force substantially perpendicular towards the face and wherein the force is approximately constant along the length of the mask and is balanced by a portion of the cushion engaging the patient's cheeks. Another aspect of the invention relates to a cushion for use with a medical mask including an outer membrane layer adapted to sealably engage a face and an undercushion layer adapted to support the membrane layer. The membrane or undercushion layer includes a surface positioned between the two layers adapted to allow the layers to slide against the respective surface. Another aspect of the invention relates to a mask system including a frame defining a breathing chamber, a cushion provided to the frame and adapted to form a seal with the patient's face, and a releasable shroud adapted to engage a portion of the outer surface of the frame, wherein the shroud is connected to straps to position the mask system. Another aspect of the invention relates to a mask assembly for use in medical applications including an upper end and a lower end wherein the upper end is adapted to cover the nose and the lower end is adapted to cover the mouth of a patient. The mask assembly includes no forehead support and includes two stiffened members attached to the upper end on opposed sides of the mask assembly, and wherein the stiffened members include a general curved shape and adapted to avoid covering the patient's field of vision. Another aspect of the invention relates to a cushion for attaching to a medical mask, wherein the cushion is flexible and includes a membrane attached to the circumference of the cushion adapted to seal against the face of a patient, and at least one undercushion adapted to support the membrane and positioned underneath the membrane to prevent collapse of the membrane, in use. The membrane is softer than the undercushion. The undercushion in the regions of nasal bridge or chin is between 0 mm and 30 mm in height as measured between the base and the tip of the undercushion. Another aspect of the invention relates to a mask assembly for use in medical applications including an upper end and a lower end wherein the upper end is adapted to cover the nose and the lower end is adapted to cover the mouth of a patient. The mask assembly includes no forehead support and includes two stiffened members attached to the upper end on opposed sides of the mask assembly, and wherein the stiffened members include a general curved shape and adapted to avoid covering the patient's field of vision. In an alternative embodiment, the mask system may include a headgear connector or rigidizer structured to attach to the frame with a snap-fit, mechanical interlock, friction fit, and/or grommet arrangement (e.g., constructed of rubber). In an alternative embodiment, the mask system may include headgear having an arrangement of straps constructed of silicone and/or Breath-O-Prene™ material. Other aspects, features, and advantages of this invention will become apparent from the following detailed description when taken in conjunction with the accompanying drawings, which are a part of this disclosure and which illustrate, by way of example, principles of this invention."},"cpc_label":{"kind":"string","value":"A61M160622"},"filing_date":{"kind":"string","value":"20171004"},"patent_issue_date":{"kind":"string","value":"20180508"},"date_published":{"kind":"string","value":"20180125"},"examiner_id":{"kind":"string","value":"65185.0"},"ipc_label":{"kind":"string","value":"A61M1606"},"npe_litigated_count":{"kind":"number","value":1,"string":"1"},"examiner_full_name":{"kind":"string","value":"DITMER, KATHRYN ELIZABETH"},"invention_title":{"kind":"string","value":"MASK SYSTEM WITH SNAP-FIT SHROUD"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"A61M"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32894,"cells":{"application_number":{"kind":"number","value":15725437,"string":"15,725,437"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"MACHINE LEARNING DEVICE AND MACHINE LEARNING METHOD FOR LEARNING CORRELATION BETWEEN SHIPMENT INSPECTION INFORMATION AND OPERATION ALARM INFORMATION FOR OBJECT"},"abstract":{"kind":"string","value":"A machine learning device which learns a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, includes a state observation unit which observes the shipment inspection information and the operation alarm information; and a learning unit which generates a learning model based on the shipment inspection information and the operation alarm information observed by the state observation unit."},"claims":{"kind":"string","value":"1. A machine learning device which learns a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, comprising: a state observation unit which observes the shipment inspection information and the operation alarm information; and a learning unit which generates a learning model based on the shipment inspection information and the operation alarm information observed by the state observation unit. 2. The machine learning device according to claim 1, wherein the learning unit generates a distribution correlation between the shipment inspection information and the operation alarm information as the learning model. 3. The machine learning device according to claim 1, further comprising: an output utilization unit which outputs an inspection item in shipping the object, which influences an alarm issued during the operation of the object, based on the learning model generated by the learning unit. 4. The machine learning device according to claim 1, wherein the learning unit generates the learning model by clustering the shipment inspection information and the operation alarm information. 5. The machine learning device according to claim 4, wherein the learning unit generates the learning model by hierarchical clustering in which the shipment inspection information and the operation alarm information are arithmetically processed in a hierarchical structure, and nonhierarchical clustering in which the shipment inspection information and the operation alarm information are arithmetically processed until a predetermined number is reached based on a distance between nodes. 6. The machine learning device according to claim 1, wherein the machine learning device further comprises a neural network. 7. The machine learning device according to claim 1, wherein the machine learning device is connectable to at least one different machine learning device and exchanges or shares the learning model generated by the learning unit of the machine learning device with the at least one different machine learning device. 8. The machine learning device according to claim 7, wherein the machine learning device is located on a first cloud server, and the different machine learning device is located on a second cloud server different from the first cloud server. 9. The machine learning device according to claim 1, wherein the object comprises a motor, and the shipment inspection information comprises inspection results of inspection items associated with a model of the motor and an inspection date of the motor. 10. The machine learning device according to claim 1, wherein the object comprises a servo amplifier which performs servo driving of a motor, and the shipment inspection information comprises inspection results of inspection items associated with a model of the servo amplifier and an inspection date of the servo amplifier. 11. The machine learning device according to claim 1, wherein the shipment inspection information comprises at least one of an insulation resistance value, an earth resistance value, a current value, and a switching surge voltage for the object, and the operation alarm information comprises at least one of an overcurrent alarm, a noise alarm, and an overload alarm for the object. 12. A machine learning method for learning a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, comprising: observing the shipment inspection information and the operation alarm information; and generating a learning model based on the observed shipment inspection information and operation alarm information. 13. The machine learning method according to claim 12, wherein the generating the learning model comprises generating a distribution correlation between the shipment inspection information and the operation alarm information as the learning model. 14. The machine learning method according to claim 12, further comprising: outputting an inspection item in shipping the object, which influences an alarm issued during the operation of the object, based on the generated learning model. 15. The machine learning method according to claim 12, wherein the generating the learning model comprises generation by clustering the shipment inspection information and the operation alarm information."},"description":{"kind":"string","value":"BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a machine learning device and a machine learning method for learning the correlation between shipment inspection information and operation alarm information for an object. 2. Description of the Related Art Conventionally, electric motors (motors: objects) have been used for a variety of electrical machines and devices including, e.g., machine tools and robots controlled by computer numerical control (CNC) devices. Such motors normally undergo shipment inspection in shipping products such as machine tools or robots, which are then delivered to users. This shipment inspection is conducted in shipping not only products which use motors but also, e.g., the motors themselves, both of which are then delivered to users. In this specification, information obtained by inspecting a motor or a product which uses the motor in shipment will be referred to as shipment inspection information hereinafter. After being delivered to users, products (motors) such as machine tools or robots are used (operated) in, e.g., actual fields, but alarms may be issued during the operation of the machine tools or the like. The alarms are issued during the operation due to various factors including, e.g., electrical problems based on, e.g., motor insulation failure or servo amplifier failure or mechanical (structural) problems based on, e.g., bearing failure or metal fatigue. In this specification, information concerning an alarm issued during the operation of a motor or a product which uses the motor will be referred to as operation alarm information hereinafter. In this specification, a motor (a product which uses the motor) will be mainly taken as an example of an object targeted for learning the correlation between shipment inspection information and operation alarm information by machine learning, but the object is not limited to a motor, and various objects whose shipment inspection information and operation alarm information may be acquired, including, e.g., a servo amplifier which performs servo driving of a motor, may be applicable. The correlation between shipment inspection information and operation alarm information for an object (motor), as described above, has conventionally attracted little attention, and even if the shipment inspection information and the operation alarm information for the motor have a certain correlation, persons may expend enormous efforts to analyze (organize) this correlation. In addition, since, for example, the use conditions (e.g., the ambient temperature or humidity, the running time, and the magnitude of the load in use) of each individual motor (including motors used for a variety of electrical machines and devices) significantly vary for each field of actual use, it is difficult for persons to comprehend the actual use conditions and elucidate the correlation between shipment inspection information and operation alarm information for this motor. Incidentally, hitherto, for example, Japanese Laid-Open Patent Publication No. H07-174616 discloses an inspection device which inspects an object such as a compact motor for abnormalities on the basis of vibration of the object or a sound emitted by the object. The inspection device detects vibration of the object or a sound emitted by the object using a sensor, performs envelope detection and Fourier transformation, calculates a certainty factor for the presence of an abnormality of the object using an arithmetic unit, further calculates a certainty factor for the presence of an abnormality of the object by inputting a feature vector signal representing the features of Fourier transform signals to a neural network, performs fuzzy computation based on the certainty factors calculated by both the arithmetic unit and the neural network, and determines the presence or absence of an abnormality of the object. Further, Japanese National Publication of International Patent Application No. 2007-528985, for example, discloses a technique for optically measuring a structure formed on a semiconductor wafer, using a machine learning system. In other words, in a method for inspecting a structure formed on a semiconductor wafer, a first diffraction signal measured using a measurement device is obtained, and at least one parameter which features the profile of the structure is received as input to obtain a second diffraction signal generated using the machine learning system. The first diffraction signal and the second diffraction signal are compared with each other, and when they match each other within the range of matching criteria, the shape of the structure is obtained on the basis of the profile or the at least one parameter used by the machine learning system to generate the second diffraction signal. In addition, Japanese Laid-Open Patent Publication No. 2004-354250, for example, discloses as a defect inspection device capable of processing an image obtained by capturing an object to efficiently, accurately classify defects, a defect inspection device which uses a neural network provided in correspondence with each specific defect to be classified occurring in the process of manufacturing an object, allows learning of each neural network for each defect to be classified, and detects the presence or absence of a defect in the object for each defect to be classified by each learned neural network. The neural network includes a neural network for shot defocus defects for classifying defocus defects occurring shot by shot in the process of exposing the object, and the image size is converted in correspondence with the input layer size as preprocessing input to the neural network. Some patent literatures of the related art conventionally disclose techniques for calculating a certainty factor for the presence of an abnormality of a motor using a neural network, or techniques for inspecting a semiconductor wafer or the like on the basis of a machine learning model, as described above. However, no particular attention has been focused on the correlation between shipment inspection information and operation alarm information for a motor, and even though the shipment inspection information and the operation alarm information for the motor have a certain correlation, it is difficult for persons to analyze this correlation because they may expend enormous efforts, as described earlier. In addition, since the use conditions of each individual motor significantly vary for each field of actual use, it may be very difficult for persons to comprehend the actual use conditions and elucidate the correlation between shipment inspection information and operation alarm information for this motor, and the correlation between shipment inspection information and operation alarm information for a motor, taking such actual use conditions into consideration, is evaluated on the basis of only experiences or intuitions of skilled engineers or users who have used the motor in the field for a long period of time. In consideration of the above-described conventional problems, it is an object of the present invention to obtain a correlation between shipment inspection information and operation alarm information for an object. Obtaining a correlation between shipment inspection information and operation alarm information for an object in this manner leads to solutions to various problems such as improvements in shipment inspection items, and structural upgrading, life determination, and an improvement in quality of the object. SUMMARY OF INVENTION According to a first aspect of the present invention, there is provided a machine learning device which learns a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, including a state observation unit which observes the shipment inspection information and the operation alarm information; and a learning unit which generates a learning model based on the shipment inspection information and the operation alarm information observed by the state observation unit. The learning unit may generate a distribution correlation between the shipment inspection information and the operation alarm information as the learning model. The machine learning device may further include an output utilization unit which outputs an inspection item in shipping the object, which influences an alarm issued during the operation of the object, based on the learning model generated by the learning unit. The learning unit may generate the learning model by clustering the shipment inspection information and the operation alarm information. The learning unit may generate the learning model by hierarchical clustering in which the shipment inspection information and the operation alarm information are arithmetically processed in a hierarchical structure, and nonhierarchical clustering in which the shipment inspection information and the operation alarm information are arithmetically processed until a predetermined number is reached based on a distance between nodes. The machine learning device may further include a neural network. The machine learning device may be connectable to at least one different machine learning device and exchange or share the learning model generated by the learning unit of the machine learning device with the at least one different machine learning device. The machine learning device may be located on a first cloud server, and the different machine learning device may be located on a second cloud server different from the first cloud server. The object may include a motor, and the shipment inspection information may include inspection results of inspection items associated with a model of the motor and an inspection date of the motor. The object may include a servo amplifier which performs servo driving of a motor, and the shipment inspection information may include inspection results of inspection items associated with a model of the servo amplifier and an inspection date of the servo amplifier. The shipment inspection information may include at least one of an insulation resistance value, an earth resistance value, a current value, and a switching surge voltage for the object, and the operation alarm information may include at least one of an overcurrent alarm, a noise alarm, and an overload alarm for the object. According to a second aspect of the present invention, there is provided a machine learning method for learning a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, including observing the shipment inspection information and the operation alarm information; and generating a learning model based on the observed shipment inspection information and operation alarm information. The generating the learning model may include generating a distribution correlation between the shipment inspection information and the operation alarm information as the learning model. The machine learning method may further include outputting an inspection item in shipping the object, which influences an alarm issued during the operation of the object, based on the generated learning model. The generating the learning model may include generation by clustering the shipment inspection information and the operation alarm information. BRIEF DESCRIPTION OF THE DRAWINGS The present invention will be understood more clearly by referring to the following accompanying drawings. FIG. 1 is a block diagram schematically illustrating an embodiment of a machine learning device according to the present invention; FIG. 2 is a plot for explaining exemplary arithmetic processing applied to the machine learning device illustrated in FIG. 1; and FIG. 3 is a diagram for explaining another exemplary arithmetic processing applied to the machine learning device illustrated in FIG. 1. DETAILED DESCRIPTION Hereinafter, embodiments of a machine learning device and a machine learning method according to the present invention will be described in detail below with reference to the accompanying drawings. A motor will be mainly taken hereinafter as an example of an object targeted for learning the correlation between shipment inspection information and operation alarm information by machine learning, but the object is not limited to a motor, and various objects whose shipment inspection information and operation alarm information may be acquired, including, e.g., a servo amplifier which performs servo driving of a motor, may be applicable. FIG. 1 is a block diagram schematically illustrating an embodiment of a machine learning device according to the present invention. A machine learning device 2 according to this embodiment includes a state observation unit 21, a learning unit 22, and an output utilization unit 23, as illustrated in FIG. 1. The state observation unit 21 observes, e.g., shipment inspection information (X1n) obtained by inspection in shipping a motor (object) and operation alarm information (X2n) issued during the operation of the motor, as data input from an environment 1. The environment 1 includes, e.g., a motor inspection device 11 which inspects a motor in its shipment and outputs shipment inspection information (X1n), and a motor controller 12 which issues an alarm during the operation of the motor and outputs operation alarm information (X2n). The shipment inspection information (X1n) and the operation alarm information (X2n) observed by the state observation unit 21 are input to the learning unit 22, which generates a distribution correlation between the shipment inspection information (X1n) and the operation alarm information (X2n) as a learning model. The output utilization unit 23 outputs, for example, an inspection item in shipping a motor, which influences an alarm issued during the operation of the motor, based on the learning model generated by the learning unit 22. The output utilization unit 23 may be located outside the machine learning device 2, and even the output of the output utilization unit 23 based on the learning model generated by the learning unit 22 is not limited to the above-mentioned inspection item in shipping a motor, which influences an alarm issued during the operation of the motor. The learning unit 22 applies “unsupervised learning” to the shipment inspection information (X1n) and the operation alarm information (X2n) to generate a learning model by, e.g., clustering. In other words, the learning unit 22 generates a learning model by hierarchical clustering in which the shipment inspection information (X1n) and the operation alarm information (X2n) are arithmetically processed in a hierarchical structure, or nonhierarchical clustering in which the shipment inspection information (X1n) and the operation alarm information (X2n) are arithmetically processed until a predetermined number is reached based on the distance between nodes. FIG. 2 is a plot for explaining exemplary arithmetic processing applied to the machine learning device illustrated in FIG. 1, i.e., explaining nonhierarchical clustering (clustering based on the k-means method). FIG. 3 is a diagram for explaining another exemplary arithmetic processing applied to the machine learning device illustrated in FIG. 1, and illustrates an exemplary neural network applied to an auto-encoder for dimensional compression in hierarchical clustering. The machine learning device (machine learning method) according to this embodiment employs “unsupervised learning” to perform clustering, and thus extracts, e.g., a useful rule, a knowledge representation, and a determination criterion by analysis from input data of shipment inspection information (X1n) and operation alarm information (X2n), outputs the determination results, and learns knowledge (machine learning). The machine learning device 2 uses, e.g., a neural network, but in actually implementing the machine learning device 2, a general-purpose computer or processor may be used, while the use of general-purpose computing on graphics processing units (GPGPU) or large-scale PC clusters allows higher-speed processing. In unsupervised learning, only input data are fed into the machine learning device 2 in large amounts to learn the distribution of the input data to, e.g., compress, classify, and shape the input data without corresponding teacher output data, unlike “supervised learning.” This allows, e.g., clustering of features seen in sets of input data into similar features, and on the basis of the obtained result, any norm may be defined and outputs are allocated to optimize it, thus predicting output. “Unsupervised learning” in this specification refers to broadly-defined “unsupervised learning” including, e.g., an intermediate between “supervised learning” and “unsupervised learning,” called “semi-supervised learning.” More specifically, as illustrated in FIG. 2, the machine learning device 2 (learning unit 22) may receive shipment inspection information (X1n) and operation alarm information (X2n) and perform, e.g., clustering until a predetermined number (e.g., k=3) is reached based on the distance between nodes (the distance between dots in FIG. 2) to obtain clusters A, B, and C. In other words, clusters A, B, and C based on the correlation between shipment inspection information (X1n) and operation alarm information (X2n) for a motor (object) may be obtained. As illustrated in FIG. 3, when, for example, input shipment inspection information (X1n) and operation alarm information (X2n) for a motor are hierarchized and clustered, a neural network 3 is applicable as an auto-encoder for dimensional compression. Shipment inspection information (X1n) and operation alarm information (X2n) for a motor, for example, are used as input X (input data Xn) of the neural network (auto-encoder) 3, and hierarchically clustered output data Yn is output as output Y. The nonhierarchical clustering represented in FIG. 2 and the hierarchical clustering represented in FIG. 3 are merely examples, and various known “unsupervised learning” methods are naturally applicable to the machine learning device 2 according to this embodiment. The machine learning device 2 according to this embodiment may be located on, e.g., a server of a manufacturer, as will be described in detail later, but the machine learning device 2 is connectable to at least one different machine learning device and may exchange or share a learning model generated by the learning unit (22) of each machine learning device (2) with the at least one different machine learning device. The servers equipped with these machine learning devices 2 may be implemented as, e.g., different cloud servers accessible via a communication line such as the internet. In this manner, with the machine learning device (machine learning method) according to this embodiment, a correlation (e.g., clusters A, B, and C in FIG. 2) between shipment inspection information and operation alarm information for an object (motor) may be obtained. Examples of the obtained correlation may include various correlations such as that between the surge voltage in the shipment inspection information and a noise alarm (an alarm for a communication error) in the operation alarm information, and that between the earth resistance in the shipment inspection information and an alarm for a communication error in the operation alarm information. Obtaining a correlation between shipment inspection information and operation alarm information for an object may result in solutions to various problems such as improvements in shipment inspection items, and structural upgrading, life determination, and an improvement in quality of the object. An application example of the machine learning device (machine learning method) according to this embodiment will be described below. First, the motor inspection device 11 conducts shipment inspection of a motor in its shipment to obtain information (X1n) concerning the inspection conducted in shipment. Examples of the shipment inspection information (X1n) of each motor may include the type (model), the inspection date, the insulation resistance value, the winding resistance value, the back electromotive force value, and the current value and the shaft friction torque value during driving for this motor, and the shipment inspection information (X1n) is recorded in a storage device (e.g., a nonvolatile storage device such as a hard disk drive or a flash memory). After the motors are shipped, operation alarm information (X2n) during the operation of each motor is acquired. Examples of the operation alarm information (X2n) of each motor may include the details of an alarm, the time until the occurrence of the alarm, and the velocity, the torque, the current, and the temperature upon the occurrence of the alarm, and the operation alarm information (X2n) is recorded in a storage device. Examples of the types of alarms may include an overcurrent alarm, a noise alarm (an alarm issued when noise is present at a predetermined level or more or an alarm issued upon the occurrence of a communication error), an overload alarm (an alarm issued upon motor overheating), and an excessive error upon movement. The shipment inspection information (X1n) of each individual motor is stored in, e.g., a server (server storage device) of a manufacturer of a motor or a product which uses the motor. The operation alarm information (X2n) of each individual motor is temporarily stored in, e.g., a storage device of the controller 12 that controls the motor, and is copied from the controller 12 to the server of the manufacturer by the service engineer of the manufacturer and stored. Alternatively, the operation alarm information (X2n) of each individual motor may be configured to be, e.g., directly uploaded from the motor controller 12 to the server of the manufacturer via a communication line such as the internet. Hence, the machine learning device 2 located on the server of the manufacturer, for example, may perform learning (processing) using the shipment inspection information (X1n) and the operation alarm information (X2n) of each individual motor as input. Processing by the machine learning device according to this embodiment located on the server of the manufacturer, for example, will be described below. First, from shipment inspection information (X1n) and operation alarm information (X2n) for a motor, a correlation between (X1n) and (X2n) is generated as a learning model, and shipment inspection items (a1, a2, a3, a4, . . . ) belonging to the shipment inspection information (X1n) for the motor that influences the operation alarm information (X2n) are output from the learning model. For faults involving specific alarms (e.g., a ground fault of a motor involving an overcurrent alarm, and demagnetization of the motor involving an overheat alarm), the rate of occurrence of faults may be predicted on the basis of, e.g., information (shipment inspection information) concerning the shipment inspection items of motors still operating without any problem from shipment inspection information (X1n) for the motor which influences an alarm. In other words, the rate of occurrence of faults of a certain motor in operation may be predicted on the basis of, e.g., the shipment inspection information of the certain motor from the correlation between shipment inspection information (X1n) and operation alarm information (X2n) for the motor. The effects obtained from the correlation between shipment inspection information and operation alarm information for a motor (object) are not limited to such prediction of the rate of occurrence of faults of the motor, and various effects may be obtained, as a matter of course. Regarding, e.g., demagnetization of a motor involving an overheat alarm, its cause may be estimated and a prompt measure may be taken as follows: when the back electromotive force in the shipment inspection information (shipment inspection) is concerned, magnet selection in design or magnet magnetization, for example, may be estimated to be responsible; when the winding resistance in the shipment inspection information is concerned, winding in the manufacture, for example, may be estimated to be responsible; or when the shaft friction resistance value in the shipment inspection information is concerned, an increase in friction resistance because of damage inflicted on the bearing in the manufacture, for example, may be estimated to be responsible. When the rate of occurrence of a specific alarm increases after a certain shipment date, a point of change in a component used, a manufacturing facility, or the like, for example, may be estimated to be responsible. When the rate of occurrence of alarms increases for a specific model, factors unique to the model in design, for example, may be estimated to be responsible. In any case, confirming the correlation between shipment inspection information and operation alarm information allows prediction of the rate of occurrence of faults for each individual motor operating in the field, and even allows effective limitation or the like of a target for a measure against the faults when such a measure is taken. Although a motor has been taken as an example of the object in the foregoing description, a servo amplifier which performs servo driving of a motor will be exemplified as the object below. In this case, the shipment inspection information (X1n) of the servo amplifier includes the model of the servo amplifier, and the inspection results of inspection items associated with the inspection date of the servo amplifier. More specifically, the shipment inspection information (X1n) of the servo amplifier includes, e.g., the insulation resistance value, the earth resistance value, the current value, and the switching surge voltage for the servo amplifier, and the operation alarm information (X2n) of the servo amplifier includes, e.g., an overcurrent alarm, a noise alarm, and an overload alarm (overheating amplifier) for the servo amplifier. Examples of the correlation obtained by the machine learning device (machine learning method) according to this embodiment may include various correlations such as that between the surge voltage in the shipment inspection information and an alarm for a communication error (noise alarm) in the operation alarm information, and that between the earth resistance in the shipment inspection information and an alarm for a communication error in the operation alarm information, as in the case where a motor is assumed as the object. Obtaining a correlation between shipment inspection information and operation alarm information for an object leads to solutions to various problems such as improvements in shipment inspection items, and structural upgrading, life determination, and an improvement in quality of the object, as described earlier. The machine learning device and the machine learning method according to the present invention have the effect of obtaining a correlation between shipment inspection information and operation alarm information for an object. All examples and conditional language provided herein are intended for the pedagogical purposes of aiding the reader in understanding the invention and the concepts contributed by the inventor to further the art, and are not to be construed as limitations to such specifically recited examples and conditions, nor does the organization of such examples in the specification relate to a showing of the superiority and inferiority of the invention. Although one or more embodiments of the present invention have been described in detail, it should be understood that various changes, substitutions, and alterations could be made hereto without departing from the spirit and scope of the invention."},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE INVENTION <EOH>"},"summary":{"kind":"string","value":"<SOH> SUMMARY OF INVENTION <EOH>According to a first aspect of the present invention, there is provided a machine learning device which learns a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, including a state observation unit which observes the shipment inspection information and the operation alarm information; and a learning unit which generates a learning model based on the shipment inspection information and the operation alarm information observed by the state observation unit. The learning unit may generate a distribution correlation between the shipment inspection information and the operation alarm information as the learning model. The machine learning device may further include an output utilization unit which outputs an inspection item in shipping the object, which influences an alarm issued during the operation of the object, based on the learning model generated by the learning unit. The learning unit may generate the learning model by clustering the shipment inspection information and the operation alarm information. The learning unit may generate the learning model by hierarchical clustering in which the shipment inspection information and the operation alarm information are arithmetically processed in a hierarchical structure, and nonhierarchical clustering in which the shipment inspection information and the operation alarm information are arithmetically processed until a predetermined number is reached based on a distance between nodes. The machine learning device may further include a neural network. The machine learning device may be connectable to at least one different machine learning device and exchange or share the learning model generated by the learning unit of the machine learning device with the at least one different machine learning device. The machine learning device may be located on a first cloud server, and the different machine learning device may be located on a second cloud server different from the first cloud server. The object may include a motor, and the shipment inspection information may include inspection results of inspection items associated with a model of the motor and an inspection date of the motor. The object may include a servo amplifier which performs servo driving of a motor, and the shipment inspection information may include inspection results of inspection items associated with a model of the servo amplifier and an inspection date of the servo amplifier. The shipment inspection information may include at least one of an insulation resistance value, an earth resistance value, a current value, and a switching surge voltage for the object, and the operation alarm information may include at least one of an overcurrent alarm, a noise alarm, and an overload alarm for the object. According to a second aspect of the present invention, there is provided a machine learning method for learning a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, including observing the shipment inspection information and the operation alarm information; and generating a learning model based on the observed shipment inspection information and operation alarm information. The generating the learning model may include generating a distribution correlation between the shipment inspection information and the operation alarm information as the learning model. The machine learning method may further include outputting an inspection item in shipping the object, which influences an alarm issued during the operation of the object, based on the generated learning model. The generating the learning model may include generation by clustering the shipment inspection information and the operation alarm information."},"cpc_label":{"kind":"string","value":"G06Q5028"},"filing_date":{"kind":"string","value":"20171005"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180412"},"examiner_id":{"kind":"string","value":"58717.0"},"ipc_label":{"kind":"string","value":"G06Q5028"},"npe_litigated_count":{"kind":"number","value":0,"string":"0"},"examiner_full_name":{"kind":"string","value":"SECK, ABABACAR"},"invention_title":{"kind":"string","value":"MACHINE LEARNING DEVICE AND MACHINE LEARNING METHOD FOR LEARNING CORRELATION BETWEEN SHIPMENT INSPECTION INFORMATION AND OPERATION ALARM INFORMATION FOR OBJECT"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":0,"string":"0"},"decision_as_of_2020":{"kind":"string","value":"PENDING"},"main_ipcr_label_subclass":{"kind":"string","value":"G06Q"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32895,"cells":{"application_number":{"kind":"number","value":15725505,"string":"15,725,505"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"CONSIGNMENT BOOKING APPARATUSES, METHODS, AND SYSTEMS"},"abstract":{"kind":"string","value":"Implementations for consignment booking include actions of providing a user interface including a plurality of consignment data entry fields that include a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment, and a content entry field configured to receive data identifying a content of the consignment to be delivered, retrieving the data identifying the pickup location, the delivery destination and the content, transmitting a call signal to be transmitted to a mobile computing device of each agent in a plurality of agents, determining a respective location of each agent in the plurality of agents based on a response to each call signal, and selecting an agent from the plurality of agents based at least in part on the respective agent locations with respect to the pickup location."},"claims":{"kind":"string","value":"1. A computing system for consignment booking, the system comprising: a user interface module configured to cause a display of a plurality of consignment data entry fields on a computer display, the consignment data entry fields comprising: a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment, and a content entry field configured to receive data identifying a content of the consignment to be delivered; and an agent selection module configured to determine respective agent locations for each agent in a plurality of agents and to select an agent from the plurality of agents based at least in part on the respective agent locations, the pickup location, the delivery destination, and the content of the consignment. 2. The system of claim 1, wherein the agent selection module is configured to select the agent having a closest proximity to the pickup location. 3. The system of claim 1, wherein the agent selection module is configured to determine an estimated time to travel to the pickup location of each agent in the plurality of agents and to select the agent having a shortest estimated time to travel to the pickup location. 4. The system of claim 1, wherein the agent selection module is configured to determine an estimated time of pickup for each agent in the plurality of agent s and to select the agent with the earliest estimated pickup time. 5. The system of claim 4, wherein the estimated time of pickup is determined based on an estimate of the time to travel from the agent location to the pickup location with a traffic delay estimate. 6. The system of claim 4, wherein the estimated time of pickup is determined based on an estimate of an average speed of the agent along a route from the agent location to the pickup location. 7. The system of claim 1, wherein the agent location is determined by receiving a location signal from a global positioning system of a mobile electronic device in response to a positioning call to each agent in the plurality of agent s. 8. The system of claim 1, further comprising an agent location module is configured to identify an un-located agent position as a last known agent position in response to the mobile electronic device failing to respond to the positioning call. 9. The system of claim 1, wherein the agent selection module is configured to determine an estimated time of drop off at the delivery destination. 10. The system of claim 9, wherein the estimated time of drop off is determined based on at least one subsequent consignment pickup that the selected agent is scheduled to make after picking up the consignment. 11. The system of claim 1, wherein the agent selection module is configured to select the agent having a closest proximity to the pickup location and a highest a rating. 12. The system of claim 1, wherein the agent selection module is configured to generate an alert communication for transmission to the agent based on the agent selection. 13. The system of claim 12, wherein the agent selection module is configured to track the agent based on transmission of the alert communication. 14. The system of claim 1, further comprising a classification module configured to retrieve one or more of the pickup location, the deliver destination and the content based on data entered into the consignment data entry fields and to identify a classification of the consignment based on a comparison of the data with a classification database. 15. A computer-implemented method executed by one or more processors of an electronic computing device, the method comprising: providing a computer display to display a user interface comprising a plurality of consignment data entry fields, the consignment data entry fields comprising: a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment, and a content entry field configured to receive data identifying a content of the consignment to be delivered; retrieving the data identifying the pickup location, the delivery destination and the content; transmitting a call signal to be transmitted to a mobile computing device of each agent in a plurality of agents; determining a respective location of each agent in the plurality of agents based on a response to each call signal; and selecting an agent from the plurality of agents based at least in part on the respective agent locations with respect to the pickup location. 16. The method of claim 15, further comprising selecting an agent based at least in part on the delivery destination. 17. The method of claim 15, further comprising selecting an agent based at least in part on the content of the consignment. 18. The method of claim 15, further comprising determining an estimated time to travel to the pickup location of each agent in the plurality of agent s and selecting the agent having a shortest estimated time to travel to the pickup location. 19. The method of claim 14, further comprising classifying the content of the consignment based on the data entered into the consignment data entry fields. 20. A non-transitory computer-readable storage medium coupled to one or more processors and having instructions stored thereon which, when executed by the one or more processors, cause the one or more processors to: cause a computer display to display a user interface comprising a plurality of consignment data entry fields, the consignment data entry fields comprising: a pickup location entry field configured to receive data identifying a pickup location for a consignment a delivery destination entry field configured to receive data identifying a delivery destination for the consignment and a content entry field configured to receive data identifying a content of the consignment to be delivered; retrieve the data identifying the pickup location, the delivery destination and the content; cause a call signal to be transmitted to a mobile computing device of each agent in a plurality of agents; determine a respective location of each agent in the plurality of agents based on a response to each call signal; select an agent from the plurality of agents based at least in part on the respective agent locations with respect to the pickup location."},"description":{"kind":"string","value":"CROSS-REFERENCE TO RELATED APPLICATION This application claims priority to Indian Patent Application No. 201641034044, filed on Oct. 5, 2016, entitled “Consignment Booking Apparatuses, Methods, And Systems,” the entirety of which is hereby incorporated by reference. TECHNICAL FIELD The present application is related to consignment bookings in particular to computer systems configured to facilitate consignment bookings. BACKGROUND Present systems for booking consignments involve customers traveling to consignment agency locations to book the consignment. The customer fills out a hand written form at the booking agency location and provides it to an agency associate to book the consignment. The agency associate uses written information to book an agent for picking up the consignment. Once the consignment is booked a delivery agent picks up the consignment and delivers the consignment to the delivery address. Because the consignment request is commonly provided via a hand written form and because the handwriting of a customer and a driver varies widely from person to person and region to region, the details of the consignment request such as the pickup location, the delivery location, the contents, and any other related information are not conducive to an automated approach such as scanning. Additionally, determining the status and location of a consignment during interim periods can be difficult and time consuming, if not indeterminable. SUMMARY The inventors have appreciated that computer implemented systems and methods can improve the accuracy and efficiency of booking and delivering consignments. Accordingly, various implementations of the present disclosure are directed to methods, systems, and apparatuses, for booking and delivering consignments. Certain implementations provide a computing system for consignment booking. The system includes a user interface module configured to cause a display of a plurality of consignment data entry fields. The consignment data entry fields include a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment and a content entry field configured to receive data identifying a content of the consignment to be delivered. The system includes an agent selection module configured to determine respective agent locations for each agent in a plurality of agents and to select an agent from the plurality of agents based at least in part on the respective agent locations, the pickup location, the delivery destination, and the content of the consignment. In some implementations, the agent selection module is configured to select the agent having a closest proximity to the pickup location. In some implementations, the agent selection module is configured to determine an estimated time to travel to the pickup location of each agent in the plurality of agents and to select the agent having a shortest estimated time to travel to the pickup location. In some implementations, the agent selection module is configured to determine an estimated time of pickup for each agent in the plurality of agent s and to select the agent with the earliest estimated pickup time. In some implementations, the estimated time of pickup is determined based on an estimate of the time to travel from the agent location to the pickup location with a traffic delay estimate. In some implementations, the estimated time of pickup is determined based on an estimate of an average speed of the agent along a route from the agent location to the pickup location. In some implementations, the agent location is determined by receiving a location signal from a global positioning system of a mobile electronic device in response to a positioning call to each agent in the plurality of agents. In some implementations, the system includes an agent location module is configured to identify an un-located agent position as a last known agent position in response to the mobile electronic device failing to respond to the positioning call. In some implementations, the agent selection module is configured to determine an estimated time of drop off at the delivery destination. In some implementations, the estimated time of drop off is determined based on at least one subsequent consignment pickup that the selected agent is scheduled to make after picking up the consignment. In some implementations, the agent selection module is configured to select the agent having a closest proximity to the pickup location and a highest a rating. In some implementations, the agent selection module is configured to generate an alert communication for transmission to the agent based on the agent selection. In some implementations, the agent selection module is configured to track the agent based on transmission of the alert communication. In some implementations, the system includes a classification module configured to retrieve one or more of the pickup location, the deliver destination and the content based on data entered into the consignment data entry fields and configured to identify a classification of the consignment based on a comparison of the data with a classification database. Certain implementations provide a computer-implemented method executed by one or more processors of an electronic computing device for booking and delivering consignments. The computer implemented method includes causing a computer display to display a user interface comprising a plurality of consignment data entry fields. The consignment data entry fields displayed include a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment, and a content entry field configured to receive data identifying a content of the consignment to be delivered. The method includes retrieving the data identifying the pickup location, the delivery destination and the content. The method includes causing a call signal to be transmitted to a mobile computing device of each agent in a plurality of agents. The method includes determining a respective location of each agent in the plurality of agents based on a response to each call signal. The method includes selecting an agent from the plurality of agents based at least in part on the respective agent locations with respect to the pickup location. In some implementations, the method includes selecting an agent based at least in part on the delivery destination. In some implementations, the method includes selecting an agent based at least in part on the content of the consignment. In some implementations, the method includes determining an estimated time to travel to the pickup location of each agent in the plurality of agents and selecting the agent having a shortest estimated time to travel to the pickup location. In some implementations, the method includes classifying the content of the consignment based on the data entered into the consignment data entry fields. Certain implementations provide a non-transitory computer-readable storage medium coupled to one or more processors and having instructions stored thereon for booking and delivering consignments. When the instructions are executed by the one or more processors, the instructions cause the one or more processors to cause a computer display to display a user interface comprising a plurality of consignment data entry fields. The consignment data entry fields displayed include a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment and a content entry field configured to receive data identifying a content of the consignment to be delivered. The instructions cause the one or more processors to retrieve the data identifying the pickup location, the delivery destination and the content. The instructions cause the one or more processors to cause a call signal to be transmitted to a mobile computing device of each agent in a plurality of agents. The instructions cause the one or more processors to determine a respective location of each agent in the plurality of agents based on a response to each call signal. The instructions cause the one or more processors to select an agent from the plurality of agents based at least in part on the respective agent locations with respect to the pickup location. Implementations disclosed herein advantageously facilitate easy and reliable tracking of a consignment, provides customers with more certainty on pickup expectations, and allow efficient management of agent resources by administration systems. It is appreciated that such implementations in accordance with the present disclosure can include any combination of the aspects and features described herein. That is, implementations in accordance with the present disclosure are not limited to the combinations of aspects and features specifically described herein, but also include any combination of the aspects and features provided. The details of one or more implementations of the present disclosure are set forth in the accompanying drawings and the description below. Other features and advantages of the present disclosure will be apparent from the description and drawings, and from the claims. BRIEF DESCRIPTION OF DRAWINGS The drawings primarily are for illustrative purposes and are not intended to limit the scope of the inventive subject matter described herein. The drawings are not necessarily to scale; in some instances, various aspects of the inventive subjection matter disclosed herein may be shown enlarged in the drawings to facilitate an understanding of different features. In the drawings, like reference characters generally refer to like features (e.g. functionally similar and/or structurally similar elements). FIG. 1 is a flow diagram of operations of a customer system for booking a consignment pickup. FIG. 2 shows an information architecture of customer system application for booking a consignment pickup. FIG. 3 illustrates a user interface of a customer system application for booking a consignment pickup. FIG. 4 is a flow diagram of operations of an administration system for accepting a consignment pickup request. FIG. 5 shows an information architecture of an administration system application for accepting a consignment pickup request. FIG. 6 illustrates a user interface of an administration application for accepting a consignment pickup request. FIG. 7 is a flow diagram of operations of an agent system for coordinating consignment pickup requests from customers with agents. FIG. 8 shows an information architecture of an agent system application for coordinating consignment pickup requests from customers with agents. FIG. 9 illustrates a user interface of an agent application for coordinating consignment pickup requests from customers with agents. FIG. 10 is a flow diagram illustrating the interoperations of a customer system, an administration system, and an agent system for consignment booking and delivery. The features and advantages of implementations of the inventive subject matter disclosed herein will become more apparent from the detailed description set forth below when taken in conjunction with the drawings. DETAILED DESCRIPTION Implementations of the present disclosure are generally directed to computing systems and methods for booking consignment pickups and deliveries. As described in further detail herein, the systems and methods provide a system architecture configured to determine location information related to a consignment requests in order to accurately and efficiently book the consignment and track the delivery of the consignment. FIG. 1 is a flow diagram of operations of a customer system 100 for booking a consignment pickup. At 101, a customer wanting to request a consignment pickup signs into a consignment booking application. The consignment booking application can include an application programming interface operating a computing device, such as a mobile electronic computing device. The customer can enter a user name and a password to log into the application programming interface. The user name and password may automatically populate information related to the customer such as a common pickup location(s), common content shipped, and/or common destination(s). At 102, the application requests the pickup location from the customer. The pickup location can be entered for a new customer or changed, for example for a returning customer, if a pickup location is not stored or a new pickup location is desired. At 103, the application requests a delivery destination, for example by displaying a destination field. At 104, the application can request a pickup date and a pickup time. At 105, the application requests that the user enter a description of the contents of the consignment. The application can also request a quantity, weight, volume, etc. in connection with requesting the description. As discussed in further detail herein, the content information can be used by a classification module to identify a specific classification identification and/or to guide particular handling instructions or determine fees associated with moving the goods. These instructions may be facilitated in part by the destination of the consignment. The description of the contents can also be factored into the agent selection. For example, certain consignment contents may require a certain amount of room or a particular type of vehicle. If a delivery agent has already picked up one or more other consignments he or she may not have the cargo room to pick up another consignment depending on the volume required. The application can automatically determine the capacity of an agent based on tracked consignments of the agent and based on profile information maintained about the agent in a central database. FIG. 2 shows an information architecture of a customer system application for booking a consignment pickup. The customer system includes customer system application 200. The customer application 200 allows a customer 202 to either sign in, if they have an existing account, or to sign-up, if they are a new user, via selector 204. Based upon the selection of the customer 202, the user interface of the application 200 takes the customer to either the sign-in interface 206 or the sign-up interface 208. Once the customer 202 has logged in, the system 200 presents a homepage interface 210. From the homepage interface 210, the customer 202 can search for a consignment that has already been booked by entering a unique shipment identification number for the consignment. From the homepage interface 210, the customer 202 can also create a new consignment. In response to selecting an option to create a new consignment from the homepage interface 210, the application 200 launches a consignment creation window 212 where the customer 202 can enter information to request the consignment. The information entered into the consignment creation window 212 includes the pickup location, the destination, and the contents. The window 212 can be a separate window or may include a modified version of the homepage interface 210. The information can also include a date or time of pickup, information such as weight or size, and/or any special handling instructions. After the consignment is requested, the customer 202 can schedule the pickup via scheduling window 226. The scheduling window 226 will access an administrator module and an agent module to select an agent for pickup, as discussed in further detail herein. The agent selection can be optimized based on the preferences of the customer 202 and/or based on the information provided in the consignment request. At window 214, the customer 202 can proceed to check-out to complete the transaction, and at window 216, the customer 202 can select and/or enter payment information for the consignment request. Consummation of the payment process can be facilitated via an online payment 220 or via a payment gateway 224, which can link to a 3rd party payment application. Alternatively, the user can designate a cash payment 218. Once the payment information is complete, the application 200 will provide a confirmation 222, which can include the unique shipment identification information for the customer 202 to retrieve and check the status of their consignment. A navigation window 232 permits the customer 202 to browse their account to check on a myriad of functions. For example, the navigation window 232 includes an option that allows the customer 202 to open a profile window 234. The profile window 234 permits the customer 202 to update account information, such as their address or pickup location, to review their payment history, to update their account username or password, to update their contact information, such as their e-mail address or telephone number, and to review any feedback or ratings provided on their account. The navigation window 232 also permits the customer 202 to review any consignments that they have booked via a consignment window 236. Through the consignment window 236, the customer 202 can view both active consignments that are in transit as well as archived consignments that have already been picked up and delivered. The customer 202 can provide feedback on an agent based on consignments that have been delivered or picked up and that are viewable in the consignment window 236. The customer 202 can also access active consignments via the consignment window 236 to track and trace the consignments that are in progress. In response to the customer checking in on the tracking status of an active consignment, a tracking window 228 is opened. The tracking window 228 receives updates from the agent either directly or indirectly via the administrator to determine where the package is or has been and/or to provide an expected time of arrival. The updates may be provided via a global positioning system (GPS) associated with a mobile computing device of the agent. The customer 202 may be permitted to change certain aspects of the delivery via a delivery option adjustment window 230 depending on where the consignment is located at in transit, as indicated by the tracking window 228. The updates can be sent to the agent to redirect the agent, for example by modifying the navigation system on the mobile computing device of the agent automatically. In some implementations, the agent can be provided with the option to accept or reject the modifications. The navigation window 232 also permits the customer to access information such as the transit rates and estimated timing via a rates window 238 and facility location information via a location window 240. The facility location information can be based on a location of the customer 202 as indicated by the customer, by the customer's profile, and/or by a location of the device upon which the application 200 is running. The navigation window 232 also provides access to a customer support module 242, an account settings module 244, and a sign out module 246. FIG. 3 illustrates an application programming interface 301 of the customer system application 200 for booking a consignment pickup. The customer system application 200 operates on a computing device 300 and includes a search field 302 in the user interface 301 for searching for a consignment based on the shipment ID. A new consignment icon 304 can be selected to generate a new consignment. A schedule pickup icon 306 can be selected to schedule a pickup of a new consignment. As discussed in connection with window 226 of FIG. 2, selecting to schedule a pickup causes the application 200 to initiate a protocol that gets real-time or near real-time information about the status and location of one or more agents or couriers that are available or that are signed on and are within a certain proximity to the pickup location. For example, this protocol can cause an administration application, to initiate transmission of a call sequence to determine the location of agents by requesting a GPS or location signal from the mobile computing device of the agent. If, for example, there are no agents within a first proximity a larger second proximity may be queried automatically. The administration application can then optimize the agent selection based, at least in part on the location of the agent with respect to the pickup location. The customer 202 can in certain implementations be permitted to select a particular agent identified, for example based on agent reviews. Consignment status bars 308a and 308b are provided in the user interface 301 of the customer system application 200. As demonstrated, the status bars 308a and 308 provide information regarding what action has taken place, a current status 310a, 310b, graphically illustrated by a progress bar 311a, 311b, a pickup date 312a, 312b, an expected delivery date 313a, 313b, a consignment content or description 314a, 314b (provided by the customer 202), and a shipment identification number 315a, 315b. In particular embodiments, a customer can request a consignment through the implementation of an image capture device of a mobile computing device and through an image recognition system operating on the data obtained through the image capture device. Consignment creation through an image capture device can be implemented via a portal to a customer system opening, for example, through an agent interface discussed in greater detail in FIG. 9. For example, if a customer requests a consignment from a remote location by calling into a shipping administrator via telephone, the shipping administrator can dispatch a particular agent to a pick-up location (for example via using an agent system as shown in FIGS. 7-9). At the pick-up location, the agent can obtain a handwritten consignment request directly from the customer. The agent can then use a camera of the mobile computing device, such as a mobile telephone, to capture an image of the handwritten consignment. The captured image of the handwritten consignment can be uploaded to the consignment booking application. The consignment booking application can be used to scan the image of the handwritten consignment in order to obtain information such as the drop-off location, the contents of the consignment, the customer information, the classification information, and other delivery parameters. The information can be obtained by text recognition software configured to translate the handwritten request into typed text. The text recognition software can be configured based on the layout of the handwritten request forms, such that the text recognition software identifies information in certain locations of the image as corresponding to certain data fields. For example, the software can be configured to identify information in uppermost right corner of the image as the delivery location. The handwritten request forms can be laid out in the same format as the data entry fields on the mobile application, in certain implementation, to efficiently mange correlating the translated text into the appropriate data entry fields. The text recognition software can be running directly on the mobile computing device or the image can be transmitted over the internet to a remote server where a remote computing device operating the text recognition software analyzes the image, obtains the shipping information, and then automatically uploads the shipping information into the consignment request of the consignment booking application on the mobile computing device. If the agent needs to pick up the consignment from another location different than the location of the image scanning, the scan of the image of the handwritten information can also obtain the pick-up location from the handwritten form. In certain embodiments, if the agent indicates, by selection or by default, that the consignment pick-up location corresponds to the location of the image capture, the mobile computing device can obtain location information of the mobile computing device at the time of image capture, for example via a global positioning system, and automatically upload the pick-up information into the consignment request. If the agent obtaining the consignment request via the image capture device is picking-up the consignment at the time of the image capture, the agent's information will be obtained from the mobile computing device and will be automatically entered into the consignment request of the consignment booking application. Once the information for the consignment request is entered into the appropriate data fields, the consignment is booked and location information obtained from the mobile computing device is used to track the status of the package as the agent leaves the pick-up location and heads to the delivery location, just as at 109. The tracking information can include a predictive analysis of the arrival time of the consignment at the delivery location. The mobile computing device can engage a mapping or navigation application operating on the device to determine the fastest route to the delivery location and this information can be provided to the administrator and/or to the customer to provide real-time status information on the tracking and progress of the package once the agent leaves the pick-up location. FIG. 4 is a flow diagram of operations of an administration system for accepting a consignment pickup request. At 401, the administration system receives a consignment request. The consignment request is received in response to a customer 202 scheduling an assignment request at 105, for example via window 220. In response to receiving the consignment request, the administration system automatically transmits call signals to a group of agents, for example to agents who are generally located within a particular region, at 402. The call signal requests a GPS response from the agents so that the administration system can determine where each agent in the group of agents are currently located with respect to the pickup area identified by the customer 202 in the consignment request 212. At 403, the administration system determines the proximity of each responding agent with respect to the pickup location. The response can come from a mobile device such as a mobile telephone, a smart watch, a tablet, or another computing device carried by the agent. The response can be automatically provided by the computing device if the agent is currently running the agent application or logged into the application (discussed in more detail in connection with FIGS. 7-9). The administration system can produce a graphical display of the agents' locations and/or provide a listing of the agents with respect to the pickup location sorted, for example listed in ascending order by proximity to the pickup location. At 404, the administration system selects an agent for an assignment to the consignment request. In some implementations, the administration system may automatically select the agent closest to the pickup location or the agent projected to be closest to the pickup location at the appropriate time of pickup. In other embodiments, the administration system can factor in other aspects before assigning an agent, which can include, but are not limited to, a rating of an agent by prior customers, the agents availability in view of other scheduled consignment assignments, the agents capacity based on the size of their transportation and other assignments, the estimated time of travel based on the traffic (actual or projected) from an agent location (actual or projected) to the pickup location, and type of transportation. This information can be provided in the agent's profile and updated as the agent accepts consignment assignments, as discussed in further detail herein. At 405, the administration system sends a request to the computing device of the selected agent. If the agent accepts the consignment assignment, the administration system receives a confirmation at 406. If the first agent automatically selected does not accept the consignment assignment, the administration system can automatically send a request to the next agent in the queue until an agent accepts the consignment assignment. At 407, the administration system sends the confirmation to the customer system, providing the customer with tracking information and estimated time of pickup. At 408, the administration system adds the tracking information to a composite tracking system where all of the agent assignments are collectively tracked. This composite tracking system can be provided in an active map format illustrating the package locations in real-time or near real-time. At 409, the administration system transmits updates to the customer 202 based on updates received on the status of the package from the agent device. For example, the agent device, such as a mobile phone can provide location information via a global positioning system of the device as the agent is in route to the customer 202 to provide the customer with an estimated time of arrival. The agent can provide an indication of pickup upon arrival at the pickup location and the device can continue to provide location information via the global positioning system once the agent leaves the pickup location and is in route to the delivery location for tracking the progress of the package. The agent can confirm pickup by obtaining an image of the consignment, which image can be uploaded to the administration system for verification. The agent can confirm pickup by scanning a label or a barcode on a pre-printed label to be affixed to the consignment upon pick-up. FIG. 5 shows an information architecture of an administration system application for accepting a consignment pickup request. The administration system includes an administration application 500. The administration application 500 allows an administrator 502 to sign in to the system via selector 504. The administration application 500 provides a sign-in portal 506 for the administrator to enter his or her credentials. After the administrator 502 has successfully entered his or her administrator credentials, the administration application 500 opens a dashboard 508 that allows the administrator 502 to search for consignments, request new consignments assignments (in response to customer requests), view new request, and view scheduled consignments. If a new request has been received, the administrator 502 can open the request and facilitate an assignment of the request via request portal 510. The request portal sends the call request to the agents (as discussed in connection with phase 402 in FIG. 4. The call request can send a text or short messaging service communication, an e-mail communication or other notification to the agents to obtain information about their existing location (GPS) or planned location within a time period of the pickup request. The administration dashboard 508 can include a link to the account setting 512 of the system or a sign-out link 514. The administration dashboard 508 can also provide a portal a consignment tracking and update window 516, where the administrator can view the status of a particular consignment assignment. The administration dashboard 508 allow the administrator to manage the administration system users via management window 518 or to generate reports via report window 520. The report window can provide statistics on efficiency by comparing the requested and estimated pickup and delivery times to the actual times as reflected by the tracking information. The efficiency statics can confirm that an agent was at a location at the time that a pickup or delivery is confirmed via the agent application. The management window 518 can allow the administrator to view information about the customers via customer window 522 and allow the administrator to add new agents via the new agent window 524. The new agent window 524 can have a Tillable form that receives the agent's mobile telephone number so that when a call request is transmitted the agent's information is automatically pulled up. FIG. 6 illustrates an application programming interface 601 of the administration application 500 for accepting a consignment pickup request. The application programming interface 601 is presented on a computing device 600 and provides access to the administration dashboard, reports, consignment assignment management, settings, alerts, etc. via the associated icons including dashboard icon 631, report icon 632, consignment assignment management icon 633, settings icon 634, and alert icon 635 displayed in the application interface. The interface 601 includes a new consignment creation tool 602 for creating new consignment assignments. The consignments are created based on the consignment request 604a, 604b, and 604c that are in the request queue. The interface 601 shows the active consignment 608a, 608b, and 608c that have been scheduled including an active and updating status of those active consignments. A new consignment window 640 shows the agent selection process for agent assignment, in response to the administrator assigning the assignment request 604a. The new consignment window indicates the consignment request delivery tune 610, contents 612 of the consignment, a pickup location 614, and a delivery location 615. A geographic map 616 shows the pickup location, the delivery location, the projected route and the location of the potential agents 618b-618g. The administration system has automatically selected a potential agent 618a, based at least in part on the location of the agent 618a. Upon approval of the agent via approval icon 622, a confirmation a request will be sent to the agent for acceptance. If the agent accepts, the consignment will be assigned and schedule accordingly. If the agent does not accept, the assignment the administrator can send a request to another agent on the list. The administration system, can also be configured to generate alerts, for example if an agent is scheduled to make a pickup at a certain time, but the location of the agent indicates an estimated arrival time that is a predetermined time beyond the requested pickup time. In response to generating such an alert, for example indicated via the alert icon 635, the administrator can re-assign attempt to re-assign the request to a new agent. Such a re-assignment can be facilitated in a similar manner as the original assignment (e.g. locating real-time position of agents) and selected the optimal agent based on proximity to the pickup location and/or estimated time to arrive at the pickup location. In certain embodiments, the administration system includes a classification module configured to classify the contents of the consignment based on the description provided by the customer. The classification can be based on one or more of the pickup location, the delivery location, and the transit route. This information can be used and compared against information in a classification database to automatically determine a classification of the consignment, which may vary for region to region and may dictate any additional fees or transit instructions that may be warranted. FIG. 7 is a flow diagram of operations of an agent system for coordinating consignment pickup requests from customers with agents. At 701, the agent system receives a consignment assignment request on the mobile electronic device of the agent. The consignment assignment request is received in response to an administrator 502 sending a call request at 402. In response to receiving the call request, the agent mobile computing device sends a location signal (actual or projected based on itinerary) at 702. At 703, the agent system receives an assignment request, if in response to the location signal sent at 702 the administration system selects the agent for the assignment. At 704, the agent transmits an acceptance of the request to the administration system. At 705, a calendar or itinerary of the agent can be updated to reflect the assignment in conjunction with any other assignments. At 706, the agent's location information is used to determine the status of the consignment. This information can be requested for a period of time before the pickup time. At 707, the agent confirms the pickup. Confirmation of the pickup can be facilitated, at least in part, by arrival of the agent at the pickup site (automatically based on GPS or manually by confirmation that is verified by GPS). At 708, the agent's itinerary for any further pickup s or delivery of the package is updated for the customer and the administration to track the status of the consignment. FIG. 8 shows an information architecture of agent system application for coordinating consignment pickup requests from customers with agents. The agent system includes an agent application 800. The agent application 800 facilitates an agent 802 signing into the application via selector 804 and sign-in portion 806 so that the agent can send location information, accept consignments, and send transit updates. An agent home page 808 allows an agent to view consignment requests and active consignments. For a selected consignment, the agent can open a consignment detail window 810 to view customer information, to confirm pickup, to confirm delivery, to obtain directions through a navigation system, to contact the customer, and to confirm the consignment contents. A status update window 812 may be selected in response to the user updating the status information for a specific consignment. The status update window 812 allows the agent to confirm specific actions, which will update the tracking information in the customer system and the administration system. A delivery and pickup confirmation window 814 can be provided. A navigation window 816 allows the agent to move through various areas in the agent application. An agent can access his or her profile information via a profile window 818. The profile window 818 can indicate the rating of the agent, can include specific feedback provided to the agent, can list the agent's history, can allow the agent to update login information or account or contact information. The navigation window 816 provides access to the agent's consignments including active consignment assignments and completed consignment assignments. The navigation window 816 also provides access to the agent's calendar, which is automatically populated in response to the agent accepting a consignment assignment and updated based on the estimated time of travel and based on the progress of the agent. The navigation window 816 also provides access to the account settings of the agent via icon 524 and allows the agent to sign out via sign out icon 526, which will prevent further tracking of the agent, for example if the agent is off and/or on break. If an agent signs out during transport of an active consignment or loses reception during transport of an active consignment, the last known location of the agent can be transported to the administration system and an update request can be repeatedly transmitted to the agent until a new location signal is received. The agent system can also be updated with information such as the agent transport vehicle or available cargo volume, which can account for any active consignments. FIG. 9 illustrates an application programming interface 901 of the agent application 800 for coordinating consignment pickup requests from customers with agents. The agent interface 901 is running on a computing device, such as a mobile phone 900. The agent interface 901 provides information of daily scheduled deliveries 902 and pickups 903. Status bars 904a and 904b provide information regarding particular consignments and include information such as, a current status 905a 905b an estimated delivery time 906a, 906b, a consignment content or description 907a, 907b and a shipment identification number 908a, 908b. FIG. 10 is a flow diagram illustrating the interoperations of a customer system, an administration system, and an agent system for consignment booking and delivery. The present disclosure describes an agent system, administration system, and an agent system. The operation of these systems depends on inputs derived or received from their counterparts. A customer system 1002 analyzes a request at 1011 and creates a new requests entry at 1012, which request is transmitted at 1013 to the administration system 1004. The requests that are determined to be old request at 1014 are archived at 1015 and can be viewed in the customer system as desired by the customer for status information. In response to receipt of the request at 1020, the administration module analyzes the request and for valid requests assigns them to an agent by transmitting the request to an agent system 1008. If there is a problem with the request analyzed at 1020, the administration system 1004 sends a notification to the customer system 1002 so that the request can be corrected. The agent system 1008, provides updates once the agent picks up packages for valid requests. The agent updates verified at 1031 are transmitted to the administration system 1004 at 1023, which notification can be sent to the customer system 1002. The administration system 1004 can further track the progress of the consignment. For example, the administration system 104 is updated at 1024 as the consignment is transmitted by the agent to the closest delivery location. In some implementations, the delivery system can be an interim between the final destination and the administration system can assign a new agent to deliver the consignment to its final location at 1025. The system of the new agent will track the delivery of the consignment to the shipment address at 1032. At 1033, if the document has been delivered a verification will be produced at 1034 and sent to the customer system 1002, via the administration system 1004. If the consignment has not been delivered, tracking information of the agent system 1008 will be sent to the administration system 1004 and to the customer system 1002 until the package is delivered at 1036. A number of implementations have been described. Nevertheless, it will be understood that various modifications may be made without departing from the spirit and scope of the disclosure. For example, various forms of the flows shown above may be used, with steps re-ordered, added, or removed. Accordingly, other implementations are within the scope of the following claims. Implementations and all of the functional operations described in this specification may be realized in digital electronic circuitry, or in computer software, firmware, or hardware, including the structures disclosed in this specification and their structural equivalents, or in combinations of one or more of them. Implementations may be realized as one or more computer program products, i.e., one or more modules of computer program instructions encoded on a computer readable medium for execution by, or to control the operation of, data processing apparatus. The computer readable medium may be a machine-readable storage device, a machine-readable storage substrate, a memory device, a composition of matter effecting a machine-readable propagated signal, or a combination of one or more of them. The term “computing system” encompasses all apparatus, devices, and machines for processing data, including by way of example a programmable processor, a computer, or multiple processors or computers. The apparatus may include, in addition to hardware, code that creates an execution environment for the computer program in question, e.g., code that constitutes processor firmware, a protocol stack, a database management system, an operating system, or a combination of one or more of them. A propagated signal is an artificially generated signal, e.g., a machine-generated electrical, optical, or electromagnetic signal that is generated to encode information for transmission to suitable receiver apparatus. A computer program (also known as a program, software, software application, script, or code) may be written in any appropriate form of programming language, including compiled or interpreted languages, and it may be deployed in any appropriate form, including as a stand-alone program or as a module, component, subroutine, or other unit suitable for use in a computing environment. A computer program does not necessarily correspond to a file in a file system. A program may be stored in a portion of a file that holds other programs or data (e.g., one or more scripts stored in a markup language document), in a single file dedicated to the program in question, or in multiple coordinated files (e.g., files that store one or more modules, sub programs, or portions of code). A computer program may be deployed to be executed on one computer or on multiple computers that are located at one site or distributed across multiple sites and interconnected by a communication network. The processes and logic flows described in this specification may be performed by one or more programmable processors executing one or more computer programs to perform functions by operating on input data and generating output. The processes and logic flows may also be performed by, and apparatus may also be implemented as, special purpose logic circuitry, e.g., an FPGA (field programmable gate array) or an ASIC (application specific integrated circuit). Processors suitable for the execution of a computer program include, by way of example, both general and special purpose microprocessors, and any one or more processors of any appropriate kind of digital computer. Generally, a processor will receive instructions and data from a read only memory or a random access memory or both. Elements of a computer can include a processor for performing instructions and one or more memory devices for storing instructions and data. Generally, a computer will also include, or be operatively coupled to receive data from or transfer data to, or both, one or more mass storage devices for storing data, e.g., magnetic, magneto optical disks, or optical disks. However, a computer need not have such devices. Moreover, a computer may be embedded in another device, e.g., a mobile telephone, a personal digital assistant (PDA), a mobile audio player, a Global Positioning System (GPS) receiver, to name just a few. Computer readable media suitable for storing computer program instructions and data include all forms of non-volatile memory, media and memory devices, including by way of example semiconductor memory devices, e.g., EPROM, EEPROM, and flash memory devices; magnetic disks, e.g., internal hard disks or removable disks; magneto optical disks; and CD ROM and DVD-ROM disks. The processor and the memory may be supplemented by, or incorporated in, special purpose logic circuitry. To provide for interaction with a user, implementations may be realized on a computer having a display device, e.g., a CRT (cathode ray tube) or LCD (liquid crystal display) monitor, for displaying information to the user and a keyboard and a pointing device, e.g., a mouse or a trackball, by which the user may provide input to the computer. Other kinds of devices may be used to provide for interaction with a user as well; for example, feedback provided to the user may be any appropriate form of sensory feedback, e.g., visual feedback, auditory feedback, or tactile feedback; and input from the user may be received in any appropriate form, including acoustic, speech, or tactile input. Implementations may be realized in a computing system that includes a back end component, e.g., as a data server, or that includes a middleware component, e.g., an application server, or that includes a front end component, e.g., a client computer having a graphical user interface or a Web browser through which a user may interact with an implementation, or any appropriate combination of one or more such back end, middleware, or front end components. The components of the system may be interconnected by any appropriate form or medium of digital data communication, e.g., a communication network. Examples of communication networks include a local area network (“LAN”) and a wide area network (“WAN”), e.g., the Internet. The computing system may include clients and servers. A client and server are generally remote from each other and typically interact through a communication network. The relationship of client and server arises by virtue of computer programs running on the respective computers and having a client-server relationship to each other. While this specification contains many specifics, these should not be construed as limitations on the scope of the disclosure or of what may be claimed, but rather as descriptions of features specific to particular implementations. Certain features that are described in this specification in the context of separate implementations may also be implemented in combination in a single implementation. Conversely, various features that are described in the context of a single implementation may also be implemented in multiple implementations separately or in any suitable sub-combination. Moreover, although features may be described above as acting in certain combinations and even initially claimed as such, one or more features from a claimed combination may in some cases be excised from the combination, and the claimed combination may be directed to a sub-combination or variation of a sub-combination. Similarly, while operations are depicted in the drawings in a particular order, this should not be understood as requiring that such operations be performed in the particular order shown or in sequential order, or that all illustrated operations be performed, to achieve desirable results. In certain circumstances, multitasking and parallel processing may be advantageous. Moreover, the separation of various system components in the implementations described above should not be understood as requiring such separation in all implementations, and it should be understood that the described program components and systems may generally be integrated together in a single software product or packaged into multiple software products. Thus, particular implementations have been described. Other implementations are within the scope of the following claims. For example, the actions recited in the claims may be performed in a different order and still achieve desirable result."},"background":{"kind":"string","value":"<SOH> BACKGROUND <EOH>Present systems for booking consignments involve customers traveling to consignment agency locations to book the consignment. The customer fills out a hand written form at the booking agency location and provides it to an agency associate to book the consignment. The agency associate uses written information to book an agent for picking up the consignment. Once the consignment is booked a delivery agent picks up the consignment and delivers the consignment to the delivery address. Because the consignment request is commonly provided via a hand written form and because the handwriting of a customer and a driver varies widely from person to person and region to region, the details of the consignment request such as the pickup location, the delivery location, the contents, and any other related information are not conducive to an automated approach such as scanning. Additionally, determining the status and location of a consignment during interim periods can be difficult and time consuming, if not indeterminable."},"summary":{"kind":"string","value":"<SOH> SUMMARY <EOH>The inventors have appreciated that computer implemented systems and methods can improve the accuracy and efficiency of booking and delivering consignments. Accordingly, various implementations of the present disclosure are directed to methods, systems, and apparatuses, for booking and delivering consignments. Certain implementations provide a computing system for consignment booking. The system includes a user interface module configured to cause a display of a plurality of consignment data entry fields. The consignment data entry fields include a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment and a content entry field configured to receive data identifying a content of the consignment to be delivered. The system includes an agent selection module configured to determine respective agent locations for each agent in a plurality of agents and to select an agent from the plurality of agents based at least in part on the respective agent locations, the pickup location, the delivery destination, and the content of the consignment. In some implementations, the agent selection module is configured to select the agent having a closest proximity to the pickup location. In some implementations, the agent selection module is configured to determine an estimated time to travel to the pickup location of each agent in the plurality of agents and to select the agent having a shortest estimated time to travel to the pickup location. In some implementations, the agent selection module is configured to determine an estimated time of pickup for each agent in the plurality of agent s and to select the agent with the earliest estimated pickup time. In some implementations, the estimated time of pickup is determined based on an estimate of the time to travel from the agent location to the pickup location with a traffic delay estimate. In some implementations, the estimated time of pickup is determined based on an estimate of an average speed of the agent along a route from the agent location to the pickup location. In some implementations, the agent location is determined by receiving a location signal from a global positioning system of a mobile electronic device in response to a positioning call to each agent in the plurality of agents. In some implementations, the system includes an agent location module is configured to identify an un-located agent position as a last known agent position in response to the mobile electronic device failing to respond to the positioning call. In some implementations, the agent selection module is configured to determine an estimated time of drop off at the delivery destination. In some implementations, the estimated time of drop off is determined based on at least one subsequent consignment pickup that the selected agent is scheduled to make after picking up the consignment. In some implementations, the agent selection module is configured to select the agent having a closest proximity to the pickup location and a highest a rating. In some implementations, the agent selection module is configured to generate an alert communication for transmission to the agent based on the agent selection. In some implementations, the agent selection module is configured to track the agent based on transmission of the alert communication. In some implementations, the system includes a classification module configured to retrieve one or more of the pickup location, the deliver destination and the content based on data entered into the consignment data entry fields and configured to identify a classification of the consignment based on a comparison of the data with a classification database. Certain implementations provide a computer-implemented method executed by one or more processors of an electronic computing device for booking and delivering consignments. The computer implemented method includes causing a computer display to display a user interface comprising a plurality of consignment data entry fields. The consignment data entry fields displayed include a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment, and a content entry field configured to receive data identifying a content of the consignment to be delivered. The method includes retrieving the data identifying the pickup location, the delivery destination and the content. The method includes causing a call signal to be transmitted to a mobile computing device of each agent in a plurality of agents. The method includes determining a respective location of each agent in the plurality of agents based on a response to each call signal. The method includes selecting an agent from the plurality of agents based at least in part on the respective agent locations with respect to the pickup location. In some implementations, the method includes selecting an agent based at least in part on the delivery destination. In some implementations, the method includes selecting an agent based at least in part on the content of the consignment. In some implementations, the method includes determining an estimated time to travel to the pickup location of each agent in the plurality of agents and selecting the agent having a shortest estimated time to travel to the pickup location. In some implementations, the method includes classifying the content of the consignment based on the data entered into the consignment data entry fields. Certain implementations provide a non-transitory computer-readable storage medium coupled to one or more processors and having instructions stored thereon for booking and delivering consignments. When the instructions are executed by the one or more processors, the instructions cause the one or more processors to cause a computer display to display a user interface comprising a plurality of consignment data entry fields. The consignment data entry fields displayed include a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive data identifying a delivery destination for the consignment and a content entry field configured to receive data identifying a content of the consignment to be delivered. The instructions cause the one or more processors to retrieve the data identifying the pickup location, the delivery destination and the content. The instructions cause the one or more processors to cause a call signal to be transmitted to a mobile computing device of each agent in a plurality of agents. The instructions cause the one or more processors to determine a respective location of each agent in the plurality of agents based on a response to each call signal. The instructions cause the one or more processors to select an agent from the plurality of agents based at least in part on the respective agent locations with respect to the pickup location. Implementations disclosed herein advantageously facilitate easy and reliable tracking of a consignment, provides customers with more certainty on pickup expectations, and allow efficient management of agent resources by administration systems. It is appreciated that such implementations in accordance with the present disclosure can include any combination of the aspects and features described herein. That is, implementations in accordance with the present disclosure are not limited to the combinations of aspects and features specifically described herein, but also include any combination of the aspects and features provided. The details of one or more implementations of the present disclosure are set forth in the accompanying drawings and the description below. Other features and advantages of the present disclosure will be apparent from the description and drawings, and from the claims."},"cpc_label":{"kind":"string","value":"G06Q100835"},"filing_date":{"kind":"string","value":"20171005"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180405"},"examiner_id":{"kind":"string","value":"63528.0"},"ipc_label":{"kind":"string","value":"G06Q1008"},"npe_litigated_count":{"kind":"number","value":0,"string":"0"},"examiner_full_name":{"kind":"string","value":"WALSH, EMMETT K"},"invention_title":{"kind":"string","value":"CONSIGNMENT BOOKING APPARATUSES, METHODS, AND SYSTEMS"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":0,"string":"0"},"decision_as_of_2020":{"kind":"string","value":"PENDING"},"main_ipcr_label_subclass":{"kind":"string","value":"G06Q"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32896,"cells":{"application_number":{"kind":"number","value":15726165,"string":"15,726,165"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"Stable Aqueous Formulations of Adalimumab"},"abstract":{"kind":"string","value":"The invention provides aqueous pharmaceutical adalimumab compositions suitable for long-term storage of adalimumab, methods of manufacture of these compositions, methods of administration, and kits containing same."},"claims":{"kind":"string","value":"1. A stable aqueous pharmaceutical composition comprising: i) adalimumab; ii) a buffer; and iii) a stabilizer; wherein the composition is free of polyol and has a pH of about 5 to about 6. 2. The composition of claim 1, wherein the composition is free of citrate buffer. 3. The composition of claim 1, wherein the composition further comprises a surfactant. 4. The composition of claim 1, wherein the composition has osmolality of about 180 to 420 mOsM; the composition is suitable for administration to a subject as a single dose; and the dose contains about 40 mg of adalimumab. 5. The composition of claim 1, wherein the composition is free of sodium chloride. 6. The composition of claim 5, wherein the composition further comprises a surfactant. 7. The composition of claim 6, wherein the composition has osmolality of about 180 to 420 mOsM; the composition is suitable for administration to a subject as a single dose; and the dose contains about 40 mg of adalimumab. 8. A stable aqueous pharmaceutical composition comprising adalimumab and a citrate-free buffer, wherein the composition is free of polyol and has a pH of about 5 to about 6. 9. The composition of claim 8, wherein the composition further comprises a surfactant. 10. The composition of claim 8, wherein the composition has osmolality of about 180 to 420 mOsM; the composition is suitable for administration to a subject as a single dose; and the dose contains about 40 mg of adalimumab. 11. The composition of claim 8, wherein the composition is free of sodium chloride. 12. The composition of claim 11, wherein the composition further comprises a surfactant. 13. The composition of claim 12, wherein the composition has osmolality of about 180 to 420 mOsM; the composition is suitable for administration to a subject as a single dose; and the dose contains about 40 mg of adalimumab."},"description":{"kind":"string","value":"FIELD OF THE INVENTION The present invention relates to aqueous pharmaceutical compositions suitable for long-term storage of adalimumab (including antibody proteins considered or intended as “biosimilar” or “bio-better” variants of commercially available adalimumab), methods of manufacture of the compositions, methods of their administration, and kits containing the same. BACKGROUND OF THE INVENTION Tumor necrosis factor alpha (TNFα) is a naturally occurring mammalian cytokine produced by various cell types, including monocytes and macrophages in response to endotoxin or other stimuli. TNFα is a major mediator of inflammatory, immunological, and pathophysiological reactions (Grell, M., et al. (1995) Cell, 83: 793-802). Soluble TNFα is formed by the cleavage of a precursor transmembrane protein (Kriegler, et al. (1988) Cell 53: 45-53), and the secreted 17 kDa polypeptides assemble to soluble homotrimer complexes (Smith, et al. (1987), J. Biol. Chem. 262: 6951-6954; for reviews of TNF, see Butler, et al. (1986), Nature 320:584; Old (1986), Science 230: 630). These complexes then bind to receptors found on a variety of cells. Binding produces an array of pro-inflammatory effects, including (i) release of other pro-inflammatory cytokines such as interleukin (IL)-6, IL-8, and IL-1, (ii) release of matrix metalloproteinases and (iii) up-regulation of the expression of endothelial adhesion molecules, further amplifying the inflammatory and immune cascade by attracting leukocytes into extravascular tissues. There are many disorders associated with elevated levels of TNFα. For example, TNFα has been shown to be up-regulated in a number of human diseases, including chronic diseases such as rheumatoid arthritis (RA), inflammatory bowel disorders, including Crohn's disease and ulcerative colitis, sepsis, congestive heart failure, asthma bronchiale and multiple sclerosis. TNFα is also referred to as a pro-inflammatory cytokine. Physiologically, TNFα is also associated with protection from particular infections (Cerami. et al. (1988), Immunol. Today 9:28). TNFα is released by macrophages that have been activated by lipopolysaccharides of Gram-negative bacteria. As such, TNFα appears to be an endogenous mediator of central importance involved in the development and pathogenesis of endotoxic shock associated with bacterial sepsis. Adalimumab (Humira®, AbbVie, Inc.) is a recombinant human IgG1 monoclonal antibody specific for human TNF. This antibody is also known as D2E7. Adalimumab consists of 1330 amino acids and has a molecular weight of approximately 148 kilodaltons. Adalimumab has been described and claimed in U.S. Pat. No. 6,090,382, the disclosure of which is hereby incorporated by reference in its entirety. Adalimumab is usually produced by recombinant DNA technology in a mammalian cell expression system, such as, for example, Chinese Hamster Ovary cells. Adalimumab binds specifically to TNFα and neutralizes the biological function of TNF by blocking its interaction with the p55 and p75 cell surface TNF receptors. Various formulations of adalimumab are known in the art. See, for example, U.S. Pat. Nos. 8,216,583 and 8,420,081. There is still need for stable liquid formulations of adalimumab that allow its long term storage without substantial loss in efficacy. SUMMARY OF THE INVENTION The invention provides stable aqueous formulations comprising adalimumab that allow its long term storage. In a first embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab; a stabilizer comprising at least one member selected from the group consisting of a polyol and a surfactant; and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said buffer does not comprise a combination of citrate and phosphate, and preferably does not comprise any citrate buffer. In this embodiment, the stabilizer preferably comprises both polyol and surfactant. In a second embodiment, utilizing a single buffer system, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer system comprising a single buffering agent, said single buffering agent being selected from citrate, phosphate, succinate, histidine, tartrate or maleate, but not including combinations of the foregoing; wherein the formulation has a pH of about 4 to 8, and preferably about 5 to about 6. Histidine and succinate are particularly preferred for use as single buffering agents. As used herein the term buffer, buffer system, or buffering agent, and like terminology, is intended to denoted buffer components that introduce buffer capacity in the formulation in addition to any buffering capacity offered by the protein itself, hence the term “buffer”, etc, is not intended to include the protein itself as a self buffering entity. In a third embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a stabilizer comprising at least one member selected from a polyol and a surfactant, wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said composition is substantially free of a buffer. In a fourth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said composition is free or substantially free of a surfactant. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate; and (iii) the polyol is selected from the group consisting of mannitol, sorbitol and trehalose. In a fifth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to 8 and preferably about 5 to about 6, and wherein said composition is substantially free of polyol. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate, including combinations thereof. In each of the five embodiments discussed above, the composition may optionally further comprise a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid stabilizer may be selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. The salt stabilizer may be selected from the group consisting of sodium chloride and sodium sulfate. The metal ion stabilizer may be selected from the group consisting of zinc, magnesium and calcium. Preferably, adalimumab formulations containing the stabilizers mentioned above also do not contain buffer systems in which phosphate buffer and citrate buffer are present in combination, and, most preferably contains buffer systems free or substantially free of citrate buffer. In particularly preferred embodiments, (i) the optional additional stabilizer present in this embodiment is not sodium chloride, or comprises sodium chloride present in amounts not to exceed about 100 mM, and comprises at least one of arginine and glycine, including combinations of the two amino acids; (ii) the buffer, when present, contains no citrate, or at least no citrate and phosphate combination, but is instead at least one of histidine and succinate, including combinations thereof; and (iii) the stabilizer when it includes a polyol is preferably mannitol in amounts exceeding about 150 mM. In further embodiments the invention is directed to an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of a buffer combination that comprises both a citrate buffer and a phosphate buffer; and (ii) the composition exhibits long term stability. Another embodiment of the invention concerns an aqueous, buffered pharmaceutical composition exhibiting long term stability, said composition comprising: (i) adalimumab; (ii) a buffer selected from the group consisting of histidine buffer, succinate buffer, and combinations thereof; (iii) a polysorbate or poloxamer surfactant, or combinations thereof; and (iv) one or both of the following: (a) a stabilizer selected from the group consisting of glycine, alanine, glutamate, arginine, methionine, EDTA, sodium chloride, sodium sulfate, metal ions, and combinations thereof; and (b) a polyol selected from sorbitol, mannitol, and trehalose, or combinations thereof. Optionally, the formulation may also include a sugar, such as sucrose. In a further embodiment the invention is an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of a polyol; and (ii) the composition exhibits long term stability. In still a further embodiment the invention is directed to an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of surfactant; and (ii) the composition exhibits long term stability. Another embodiment of the inventions concerns an aqueous pharmaceutical composition comprising adalimumab wherein: (i) the composition is free or substantially free of buffer; and (ii) the composition exhibits long term stability. In another embodiment, the adalimumab formulation of the present invention comprises, consists of, or consists essentially of, adalimumab, histidine buffer as the sole buffer in the formulation, glycine (or arginine, or combinations thereof) as the sole stabilizer among the non-surfactant stabilizers referenced earlier, and polysorbate 80. In this formulation, the amount of adalimumab is 20 to 150 mg/ml, the amount of histidine buffer is up to about 50 mM; the amount of glycine is up to about 300 mM; and the amount of polysorbate 80 is in the range of about 0.01 to about 0.2 wt %. Optionally, this formulation may include up to about 100 mM NaCl. The present invention also contemplates modification of this formulation to combine the histidine buffer with one or more of citrate, acetate, phosphate, maleate, tartrate buffers. In yet another embodiment, the adalimumab formulation of the present invention comprises, consists of, or consists essentially of, adalimumab, histidine buffer as the sole buffer, mannitol (or sorbitol or trehelose), and polysorbate 80, and further being free or substantially free of the non-surfactant stabilizers (e.g. glycine, arginine, etc.) referenced above. In this formulation, the amount of adalimumab is 20 to 150 mg/ml; the amount of histidine buffer is up to about 50 mM; the amount of polyol is up to about 300 mM; and the amount of polysorbate 80 is in the range of about 0.01 to about 0.2 wt %. Optionally, this formulation may include up to about 100 mM NaCl. The present invention also contemplates modification of this formulation to combine the histidine buffer with one or more of citrate, acetate, phosphate, maleate, tartrate buffers. In a method aspect, the invention is directed to a method for enhancing long term stability in an aqueous, buffered adalimumab formulation, comprising one or more of the steps of: (a) incorporating histidine buffer, succinate buffer, or a combination thereof, in the formulation based on empirical data indicating that such buffers contribute to the stability of the formulation to a greater extent than other buffers or buffer combinations; or (b) incorporating glycine, arginine or a combination thereof as stabilizers in the formulation, based upon empirical data indicating that such stabilizer contribute to the stability of the formulation to a greater extent than other stabilizers; or (c) substantially excluding the presence of buffer or buffer combinations comprising citrate buffer (especially buffer combinations comprising both citrate and phosphate) based upon empirical data indicating that such buffer or buffer combinations perform poorly in terms of stabilizing the formulation in comparison to other buffers. The method may further comprise the selection of PS 80 as a surfactant based on empirical data indicating that PS 80 imparts better thermal stability to the adalimumab formulation than other surfactants, including PS 20. The method is useful to obtain a formulation of adalimumab that exhibits long term stability comparable to or better than commercially available adalimumab formulations marketed under the trademark Humira®. In a further method aspect, the invention is directed to a method for treating an inflammatory condition in a subject which comprises administering to such subject any of the adalimumab formulation embodiments as described herein. In the foregoing embodiments, where the above referenced stabilizers may be included in the formulations, it is further discovered that satisfactory stabilization can be attained when such stabilizers are used in place of both polyol and surfactant and hence stabilized formulations of the present invention can be free or substantially free of both polyol and surfactant. Accordingly, in a sixth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, optionally a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, EDTA, and a metal ion, and wherein said composition has a pH of about 4 to about 8, and preferably 5 to about 6, and wherein said composition is either substantially free of both polyol and surfactant. When buffer is present in this embodiment, it is especially preferred that (i) the buffer not include the combination of citrate and phosphate; (ii) the buffer is selected from the group consisting of histidine and succinate; and (iii) the stabilizer does not comprise sodium chloride, but instead is at least one member selected from the group consisting of arginine and glycine. Important aspects of the present invention in certain embodiments include (i) that sorbitol and trehalose are discovered to be significantly better stabilizers of adalimumab formulations than mannitol, unless mannitol is used at concentrations in excess of about 200-300 mM in which case the three are generally equivalent; (ii) arginine and glycine (and combinations) are discovered to be significantly better stabilizers of adalimumab formulations than sodium chloride; and; (iii) when buffers are used in the formulation, it is discovered that the combination of citrate and phosphate is surprisingly significantly poorer in stabilizing adalimumab than other buffers such as succinate, histidine, phosphate and tartrate. The relatively poor performance of the buffer combination of citrate and phosphate is rather unexpected considering the apparent importance attributed to the use of a citrate/phosphate combined buffer in U.S. Pat. No. 8,216,583. To the contrary, we have now found that a phosphate/citrate buffer combination is not an optimal choice for obtaining a stabilized adalimumab formulation, and in fact, an element of our invention is the discovery that this combination should be avoided altogether in favor of other buffer systems. Preferably, a polyol is a sugar alcohol; and even more preferably, the sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. However, as between mannitol and sorbitol, the invention has discovered, as noted above, a distinct stabilization advantage in using sorbitol or trehalose instead of mannitol, unless mannitol is used at concentrations in excess of about 200 mM, in which case mannitol, sorbitol and trehalose are generally equivalent. At concentrations below about 200 mM, mannitol has been found to be a poorer stabilizer than sorbitol or trehalose in an adalimumab formulation. Preferably, a surfactant is a polysorbate or poloxamer; and even more preferably PS 80, PS 40, PS20, Pluronic F-68 and combinations. We have discovered a distinct and surprising thermal stabilization advantage in selecting PS 80 instead of PS-20. These and other aspects will become apparent from the following description of the various embodiments, although variations and modifications therein may be affected without departing from the spirit and scope of the novel concepts of the disclosure. It is to be understood that both the foregoing general description and the following detailed description are exemplary and explanatory only and are not restrictive of the invention, as claimed. Further representative embodiments are set forth in the numerous formulation studies reported in the detailed description, as well as the various embodiments listed in Appendices A, B and C attached hereto and made a part hereof. BRIEF DESCRIPTION OF THE DRAWINGS The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee. FIG. 1 is a bar chart of stability of various adalimumab formulations as determined by size exclusion chromatography (SEC). FIG. 2 is a bar chart of stability of various adalimumab formulations as determined by reversed phase (RP) high performance liquid chromatography (HPLC). FIG. 3 is a graph of a partial least squares (PLS) model 1 demonstrating effect of citrate/phosphate on stability. FIG. 4 is a graph of a PLS model 2 demonstrating effect of citrate/phosphate on stability. FIG. 5 is a graph of a PLS model 1 demonstrating effect of histidine/glycine on stability. FIG. 6 is a graph of a PLS model 1 demonstrating effect of arginine/sorbitol on stability. FIG. 7 is a graph of a PLS model 1 demonstrating effect of pH/histidine on stability. FIG. 8 is a graph of a PLS model 2 demonstrating effect of pH/histidine on stability. FIG. 9 is a graph of a PLS model 2 demonstrating effect of trehalose/PS80 on stability. FIG. 10 is a graph of a PLS model 2 demonstrating effect of mannitol/PS80 on stability. FIG. 11 is a graph of a PLS model 1 demonstrating effect of mannitol/NaCl on stability. FIG. 12 is a graph of a PLS model 1 demonstrating effect of EDTA/methionine on stability. FIG. 13 is a graph of a PLS model A demonstrating effect of citrate and phosphate on stability. FIG. 14 is a graph of a PLS model A demonstrating effect of pH and histidine buffer on stability. FIG. 15 is a graph of a PLS model A demonstrating effect of glycine and arginine on stability. FIG. 16 is a graph of a PLS model A demonstrating effect of NaCl and polysorbate 80 (PS 80) on stability. FIG. 17 is a graph of a PLS model B demonstrating effect of citrate and phosphate on stability. FIG. 18 is a graph of a PLS model B demonstrating effect of pH and histidine buffer on stability. FIG. 19 is a graph of a PLS model B demonstrating effect arginine and glycine on stability. FIG. 20 is a graph of a PLS model B demonstrating effect of PS80 and mannitol on stability. FIG. 21 is a graph of a PLS model B demonstrating effect of EDTA and NaCl on stability. FIG. 22 is a graph of a PLS model B demonstrating effect of succinate buffer and histidine buffer on stability. FIG. 23 is a graph of a PLS model C demonstrating effect of citrate and phosphate on stability. FIG. 24 is a graph of a PLS model C demonstrating effect of pH and histidine buffer on stability. FIG. 25 is a graph of a PLS model C demonstrating effect of arginine and glycine on stability. FIG. 26 is a graph of a PLS model C demonstrating effect of mannitol and PS 80 on stability. FIG. 27 is a graph of a PLS model C demonstrating effect of PS 80 and NaCl on stability. FIG. 28 is a graph of a PLS model C demonstrating effect of pH and protein concentration on stability. DETAILED DESCRIPTION OF THE INVENTION Various embodiments of the invention are now described in detail. As used in the description and throughout the claims, the meaning of “a”, “an”, and “the” includes plural reference unless the context clearly dictates otherwise. Also, as used in the description and throughout the claims, the meaning of “in” includes “in” and “on” unless the context clearly dictates otherwise. Additionally, some terms used in this specification are more specifically defined below. Definitions The terms used in this specification generally have their ordinary meanings in the art, within the context of the invention, and in the specific context where each term is used. Certain terms that are used to describe the invention are discussed below, or elsewhere in the specification, to provide additional guidance to the practitioner regarding the description of the invention. Synonyms for certain terms are provided. A recital of one or more synonyms does not exclude the use of other synonyms. The use of examples anywhere in this specification including examples of any terms discussed herein is illustrative only, and in no way limits the scope and meaning of the invention or of any exemplified term. The invention is not limited to the various embodiments given in this specification. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains. In the case of conflict, the present document, including definitions will control. “Around,” “about” or “approximately” shall generally mean within 20 percent, within 10 percent, within 5, 4, 3, 2 or 1 percent of a given value or range. Numerical quantities given are approximate, meaning that the term “around,” “about” or “approximately” can be inferred if not expressly stated. The term “adalimumab” is synonymous with the active pharmaceutical ingredient in Humira® as well as protein considered or intended as biosimilar or bio-better variants thereof. Adalimumab is a recombinant human IgG1 monoclonal antibody specific for human TNF. Adalimumab is also known as D2E7. Adalimumab has two light chains, each with a molecular weight of approximately 24 kilodaltons (kDa) and two IgG1 heavy chains each with a molecular weight of approximately 49 kDa. Each light chain consists of 214 amino acid residues and each heavy chain consists of 451 amino acid residues. Thus, adalimumab consists of 1330 amino acids and has a total molecular weight of approximately 148 kDa. The term adalimumab is also intended to encompass so-called bio-similar or bio-better variants of the adalimumab protein used in commercially available Humira®. For example, a variant of commercial Humira® may be acceptable to the FDA when it has essentially the same pharmacological effects as commercially available Humira®, even though it may exhibit certain physical properties, such as glycosylation profile, that may be similar if not identical to Humira®. For the purposes of the present application, the term “adalimumab” also encompasses adalimumab with minor modifications in the amino acid structure (including deletions, additions, and/or substitutions of amino acids) or in the glycosylation properties, which do not significantly affect the function of the polypeptide. The term “adalimumab” encompasses all forms and formulations of Humira®, including but not limited to concentrated formulations, injectable ready-to-use formulations; formulations reconstituted with water, alcohol, and/or other ingredients, and others. The term “human TNFα” (which may be abbreviated as hTNFα, or simply hTNF), as used herein, is intended to refer to a human cytokine that exists as a 17 kD secreted form and a 26 kD membrane associated form, the biologically active form of which is composed of a trimer of noncovalently bound 17 kD molecules. The structure of hTNFα is described further in, for example, Pennica, D., et al. (1984) Nature 312:724-729; Davis, J. M., et al. (1987) Biochemistry 26:1322-1326; and Jones, E. Y., et al. (1989) Nature 338:225-228. The term human TNFα is intended to include recombinant human TNFα (rhTNFα), which can be prepared by standard recombinant expression methods or purchased commercially (R & D Systems, Catalog No. 210-TA, Minneapolis, Minn.). The term “antibody”, as used herein, refers to immunoglobulin molecules comprised of four polypeptide chains, two heavy (H) chains and two light (L) chains inter-connected by disulfide bonds. Each heavy chain is comprised of a heavy chain variable region (abbreviated herein as HCVR or VH) and a heavy chain constant region. The heavy chain constant region is comprised of three domains, CH1, CH2 and CH3. Each light chain is comprised of a light chain variable region (abbreviated herein as LCVR or VL) and a light chain constant region. The light chain constant region is comprised of one domain, CL. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FR). Each VH and VL is composed of three CDRs and four FRs, arranged from amino-terminus to carboxy-terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. In one embodiment of the invention, the formulation contains an antibody with CDR1, CDR2, and CDR3 sequences like those described in U.S. Pat. Nos. 6,090,382; 6,258,562, and 8,216,583. An antibody or antigen-binding portion thereof may be part of a larger immunoadhesion molecule, formed by covalent or noncovalent association of the antibody or antibody portion with one or more other proteins or peptides. Examples of such immunoadhesion molecules include use of the streptavidin core region to make a tetrameric scFv molecule (Kipriyanov, S. M., et al. (1995) Human Antibodies and Hybridomas 6:93-101) and use of a cysteine residue, a marker peptide and a C-terminal polyhistidine tag to make bivalent and biotinylated scFv molecules (Kipriyanov, S. M., et al. (1994) Mol. Immunol. 31:1047-1058). Antibody portions, such as Fab and F(ab′)2 fragments, can be prepared from whole antibodies using conventional techniques, such as papain or pepsin digestion, respectively, of whole antibodies. Moreover, antibodies, antibody portions and immunoadhesion molecules can be obtained using standard recombinant DNA techniques, as described herein. The term “isolated antibody”, as used herein, refers to an antibody that is substantially free of other antibodies having different antigenic specificities (e.g., an isolated antibody that specifically binds hTNFα is substantially free of antibodies that specifically bind antigens other than hTNFα). An isolated antibody that specifically binds hTNFα may, however, have cross-reactivity to other antigens, such as TNFα molecules from other species. Moreover, an isolated antibody may be substantially free of other cellular material and/or chemicals. The term “glycine” refers to an amino acid whose codons are GGT, GGC, GGA, and GGG. The term “arginine” refers to an α-amino acid whose codons are CCU, CCC, CCA, and CCG. The term “alanine” refers to an amino acid whose codons are GCT, GCC, GCA, and GCG. The term “methionine” refers to an amino acid whose codon is ATG. The term “glutamate” refers to an amino acid whose codons are GAA and GAG. The term “sugar” refers to monosaccharides, disachharides, and polysaccharides. Examples of sugars include, but are not limited to, sucrose, glucose, dextrose, and others. The term “polyol” refers to an alcohol containing multiple hydroxyl groups. Examples of polyols include, but are not limited to, mannitol, sorbitol, and others. The term “metal ion” refers to a metal atom with a net positive or negative electric charge. For the purposes of the present application, the term “metal ion” also includes sources of metal ions, including but not limited to metal salts. The term “long-term storage” or “long term stability” is understood to mean that the pharmaceutical composition can be stored for three months or more, for six months or more, and preferably for one year or more, most preferably a minimum stable shelf life of at least two years. Generally speaking, the terms “long term storage” and “long term stability” further include stable storage durations that are at least comparable to or better that the stable shelf typically required for currently available commercial formulations of adalimumab, without losses in stability that would render the formulation unsuitable for its intended pharmaceutical application. Long-term storage is also understood to mean that the pharmaceutical composition is stored either as a liquid at 2-8° C., or is frozen, e.g., at −20° C., or colder. It is also contemplated that the composition can be frozen and thawed more than once. The term “stable” with respect to long-term storage is understood to mean that adalimumab contained in the pharmaceutical compositions does not lose more than 20%, or more preferably 15%, or even more preferably 10%, and most preferably 5% of its activity relative to activity of the composition at the beginning of storage. The term “substantially free” means that either no substance is present or only minimal, trace amounts of the substance are present which do not have any substantial impact on the properties of the composition. If reference is made to no amount of a substance, it should be understood as “no detectable amount”. The term “mammal” includes, but is not limited to, a human. The term “pharmaceutically acceptable carrier” refers to a non-toxic solid, semisolid or liquid filler, diluent, encapsulating material, formulation auxiliary, or excipient of any conventional type. A pharmaceutically acceptable carrier is non-toxic to recipients at the dosages and concentrations employed and is compatible with other ingredients of the formulation. The term “composition” refers to a mixture that usually contains a carrier, such as a pharmaceutically acceptable carrier or excipient that is conventional in the art and which is suitable for administration into a subject for therapeutic, diagnostic, or prophylactic purposes. It may include a cell culture in which the polypeptide or polynucleotide is present in the cells or in the culture medium. For example, compositions for oral administration can form solutions, suspensions, tablets, pills, capsules, sustained release formulations, oral rinses or powders. The terms “pharmaceutical composition” and “formulation” are used interchangeably. The term “treatment” refers to any administration or application of remedies for disease in a mammal and includes inhibiting the disease, arresting its development, relieving the disease, for example, by causing regression, or restoring or repairing a lost, missing, or defective function; or stimulating an inefficient process. The term includes obtaining a desired pharmacologic and/or physiologic effect, covering any treatment of a pathological condition or disorder in a mammal. The effect may be prophylactic in terms of completely or partially preventing a disorder or symptom thereof and/or may be therapeutic in terms of a partial or complete cure for a disorder and/or adverse affect attributable to the disorder. It includes (1) preventing the disorder from occurring or recurring in a subject who may be predisposed to the disorder but is not yet symptomatic, (2) inhibiting the disorder, such as arresting its development, (3) stopping or terminating the disorder or at least its associated symptoms, so that the host no longer suffers from the disorder or its symptoms, such as causing regression of the disorder or its symptoms, for example, by restoring or repairing a lost, missing or defective function, or stimulating an inefficient process, or (4) relieving, alleviating or ameliorating the disorder, or symptoms associated therewith, where ameliorating is used in a broad sense to refer to at least a reduction in the magnitude of a parameter, such as inflammation, pain and/or tumor size. The term “disease” refers to any condition, infection, disorder or syndrome that requires medical intervention or for which medical intervention is desirable. Such medical intervention can include treatment, diagnosis and/or prevention. The term “therapeutically effective amount” refers to an amount which, when administered to a living subject, achieves a desired effect on the living subject. For example, an effective amount of the polypeptide of the invention for administration to the living subject is an amount that prevents and/or treats an integrin αvβ3-mediated disease. The exact amount will depend on the purpose of the treatment, and will be ascertainable by one skilled in the art using known techniques. As is known in the art, adjustments for systemic versus localized delivery, age, body weight, general health, sex, diet, time of administration, drug interaction and the severity of the condition may be necessary, and will be ascertainable with routine experimentation by those skilled in the art. Embodiments of the Invention When pharmaceutical compositions containing adalimumab (Humira®), including aqueous and lyophilized formulations of adalimumab are stored on a long-term basis, the activity of adalimumab can be lost or decreased due to aggregation and/or degradation. Thus, the present invention provides aqueous formulations of adalimumab that allow stable long-term storage of adalimumab, so that adalimumab is stable over the course of storage either in liquid or frozen states. The provided formulations do not require any extra steps such as rehydrating. Numerous embodiments of the present invention are explained in a greater detail below. Adalimumab All of the compositions of the present invention comprise adalimumab. As explained in the Background section of this application, adalimumab is a recombinant human IgG1 monoclonal antibody specific for human tumor necrosis factor (TNF). This antibody is also known as D2E7. Adalimumab consists of 1330 amino acids and has a molecular weight of approximately 148 kilodaltons. Adalimumab has been described and claimed in U.S. Pat. No. 6,090,382. The term “adalimumab” is also intended to mean so-called “bio-similar” and “bio-better” versions of the active adalimumab protein present in commercially available Humira®. Adalimumab suitable for storage in the present pharmaceutical composition can be produced by standard methods known in the art. For example, U.S. Pat. Nos. 6,090,382 and 8,216,583 describe various methods that a skilled artisan could use to prepare adalimumab protein for use in the formulations of the present invention. These methods are incorporated by reference herein. For example, adalimumab can be prepared by recombinant expression of immunoglobulin light and heavy chain genes in a host cell. Purification of the expressed adalimumab can be performed by any standard method. When adalimumab is produced intracellularly, the particulate debris is removed, for example, by centrifugation or ultrafiltration. When adalimumab is secreted into the medium, supernatants from such expression systems can be first concentrated using standard polypeptide concentration filters. Protease inhibitors can also be added to inhibit proteolysis and antibiotics can be included to prevent the growth of microorganisms. Adalimumab can be purified using, for example, hydroxyapatite chromatography, gel electrophoresis, dialysis, and affinity chromatography, and any combination of known or yet to be discovered purification techniques, including but not limited to Protein A chromatography, fractionation on an ion-exchange column, ethanol precipitation, reverse phase HPLC, chromatography on silica, chromatography on heparin SEPHAROSET®, an anion or cation exchange resin chromatography (such as a polyaspartic acid column), chromatofocusing, SDS-PAGE, and ammonium sulfate precipitation. I Formulations of Adalimumab with a Polyol and/or Surfactant, but without a Citrate/Phosphate Buffer In a first embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab; a stabilizer comprising at least one member selected from the group consisting of a polyol and a surfactant; and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said buffer does not comprise a combination of citrate and phosphate. In this embodiment, the stabilizer preferably comprises both polyol and surfactant. The pharmaceutical composition can comprise one, or any combination of two or more buffers, as long as it does not comprise both citrate and phosphate. The surfactant may be any pharmaceutically acceptable surfactant, preferably polysorbates (e.g., polysorbate 80) or poloxamers (e.g., Pluronic F-68). II Formulations of Adalimumab Using a Single Buffer System In a second embodiment, utilizing a single buffer system, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer system comprising a single buffering agent, said single buffering agent being selected from citrate, phosphate, succinate, histidine, tartrate or maleate, but not including combinations of the foregoing; wherein the formulation has a pH of about 4 to 8, and preferably about 5 to about 6. Histidine and succinate are particularly preferred for use as single buffering agents. It was surprisingly discovered that adalimumab compositions which comprise only one buffer (as opposed to two or more buffers) are more stable than adalimumab compositions comprising both a citrate buffer and a phosphate buffer. In the single buffer embodiment, adalimumab can be present at a concentration from about 20 to about 150 mg/ml, more preferably from about 20 to about 100 mg/ml, and even more preferably from about 30 to about 50 mg/ml. The buffer is present at a concentration from about 5 mM to about 50 mM. The pH of the compositions is between about 5 and about 6. The single buffer compositions of the invention may further comprise a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine, most preferably glycine, arginine and methionine. The salt is selected from the group consisting of sodium chloride and sodium sulfate. The metal ion is selected from the group consisting of zinc, magnesium and calcium. The compositions of the invention may further comprise a surfactant. The surfactant is a polysorbate surfactant or a poloxamer surfactant. Polysorbate surfactants include polysorbate 80, polysorbate 40 and polysorbate 20. A preferred polysorbate surfactant is polysorbate 80. Poloxamer surfactants include poloxamer 188 (also available commercially as Pluronic F-68). Most preferably, the surfactant is polysorbate 80. The single buffer composition may further comprise a polyol. Preferably, the polyol is a sugar alcohol; and even more preferably, the sugar alcohol is mannitol, sorbitol or trehalose. The single buffer adalimumab composition may also comprise a sugar, preferably sucrose, glucose or dextrose. In one embodiment of a single buffer adalimumab formulation, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to 50 μM, and succinate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. In another embodiment of a single buffer adalimumab formulation, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to 50 μM, and histidine at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. In a further embodiment of a single buffer adalimumab formulation, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to 50 μM, and either tartrate, maleate or acetate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. III Formulations of Adalimumab which Exclude Buffer In a third embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a stabilizer comprising at least one member selected from a polyol and a surfactant, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said composition is substantially free of a buffer. The term “free of buffer” should be understood to allow inclusion of the inherent buffering effect of the protein itself. In a buffer free formulation, the stabilizers referenced above may also be present (e.g. glycine, arginine and combinations thereof). IV Formulations of Adalimumab which Exclude Surfactant In a fourth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said composition is free or substantially free of a surfactant. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate; and (iii) the polyol is not mannitol at concentrations less than about 150 mM, but instead is selected from the group consisting of mannitol at concentrations exceeding about 150 mM, sorbitol and trehalose. V Formulations of Adalimumab which Exclude Polyol In a fifth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said composition is substantially free of polyol. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate. Additional Stabilizers Useful in Embodiments I Through V. Optionally, in each of the five embodiments summarized above, the composition may further comprise a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid stabilizer may be selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. The salt stabilizer may be selected from the group consisting of sodium chloride and sodium sulfate. The metal ion stabilizer may be selected from the group consisting of zinc, magnesium and calcium. Preferably, adalimumab formulations containing the stabilizers mentioned above also do not contain buffer systems in which phosphate buffer and citrate buffer are present in combination. Most preferably (i) the optional additional stabilizer present in this embodiment is not sodium chloride, and comprises at least one or both of arginine and glycine; (ii) the buffer, when present, contains no citrate and phosphate combination but is instead at least one of histidine and succinate; and (iii) the stabilizer when it includes a polyol is not mannitol unless in amounts greater than about 150 mM, and may also include trehalose and sorbitol. Preferably the amount of mannitol is greater than about 150 mM, and most preferably greater than about 200 mM. VI Formulations of Adalimumab Replacing Both Surfactant and Polyol with Other Stabilizers It has been further discovered that satisfactory stabilization can be attained when the stabilizers mentioned above are used in place of both polyol and surfactant, accordingly, in a sixth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, optionally a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, EDTA, and a metal ion, and wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said composition is free or substantially free of a polyol and surfactant. When buffer is present in this embodiment, it is especially preferred that (i) the buffer not include the combination of citrate and phosphate; (ii) the buffer is selected from the group consisting of histidine and succinate; and (iii) the stabilizer does not comprise sodium chloride, but instead is at least one member selected from the group consisting of arginine and glycine. It is also preferred that the buffer is free or substantially free of citrate buffer, as we have discovered that it is generally poorer in terms of stability contribution than other buffers, such as histidine and succinate. In each of the embodiments above at least one of the following advantageous conditions can be optionally present (unless stated as being required): (i) the buffer preferably does not contain a combination of citrate and phosphate, or is free or substantially free of citrate buffer (ii) the buffer preferably is at least one member selected from the group consisting of histidine and succinate; and (iii) the stabilizer preferably does not include sodium chloride, or if present is controlled to levels less than about 100 mM; (iv) the stabilizer is at least one member selected from the group consisting of arginine and glycine, including combinations thereof; and (v) the polyol is preferably not mannitol (unless mannitol is present in amounts greater than about 150 mM and preferably greater than about 200 mM) but may include sorbitol and trehalose. When using polyols for stabilization, mannitol is discovered herein to be destabilizing in comparison to sorbitol and trehalose unless the mannitol is present in amounts generally above about 150 to 200 mM. When using other stabilizers, it is discovered herein that sodium chloride is destabilizing compared to arginine or glycine, but we observe some stabilization when the levels of sodium chloride are controlled to less than about 100 mM and preferably less than about 75 mM. Preferably, adalimumab is present in the composition of the present invention at a concentration from about 20 to about 150 mg/ml, more preferably from about 20 to about 100 mg/ml, and even more preferably from about 30 to about 50 mg/ml. Buffer, if present, is present at a concentration from about 5 mM to about 50 mM. Surfactant, if present, is preferably a polysorbate (PS). In an even more preferred embodiment, the polysorbate is polysorbate 80 (PS 80). Poloxamer surfactants are also suitable (e.g., Pluronic® F-68). The polyol, if present, is a sugar alcohol. In an even more preferred embodiment, the sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose, and most preferably sorbitol and trehalose. Preferably, the polyol is at a concentration from about 1 to about 10%, more preferably, from about 2 to about 6%, and even more preferably from about 3 to 5%, wherein said values are weight by volume (w/v) of the total composition. A stabilizer, when present, can be selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid can be selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. The salt may be selected from the group consisting of sodium chloride and sodium sulfate. The metal ion may be selected from the group consisting of zinc, magnesium and calcium. Glycine and arginine are particularly preferred stabilizers. Zinc, magnesium and calcium, when present for stabilization, may be at a concentration from about 1 mM to about 100 mM, and more preferably from about 1 to about 10 mM. Glycine, or arginine, or combinations thereof, if present for stabilization, is at a total concentration of up to about 300 mM, and preferably about 150 to 300 mM. Methionine, if present for stabilization, is present at a concentration from about 1 to about 10 mg/ml, more preferably from about 1 mg/ml to about 5 mg/ml. Sodium chloride, if present for stabilization, is at a concentration from about 5 to about 150 mM, more preferably, from about 20 to about 140 mM, and even more preferably less than about 100 mM. Sodium sulfate, if present if present for stabilization, is at a concentration from about 5 to about 150 mM, more preferably, from about 20 to about 120 mM, and even more preferably from about 60 to about 100 mM. EDTA, if present for stabilization, is present at a concentration from about 0.01% to about 0.05%, more preferably from about 0.05% to about 0.25%, and even more preferably from about 0.08% to about 0.2%. Preferably, the pH of the composition is from about 5 to about 5.5; and even more preferably is about 5.2 to 5.4. In an example of Embodiment I and II, above, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sorbitol or trehalose at a concentration from about 1 to 10% weight by volume, polysorbate 80 at a concentration from about 1 to 50 μM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM to about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and provided said composition is free or substantially free of citrate/phosphate buffer combination. Further, we rank citrate as the poorest of buffers, and preferably avoid it although it is still within the scope of the invention to formulate stable formulations of adalimumab that include citrate buffer, if not the combination thereof with phosphate. In an example of Embodiment IV, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sorbitol or trehalose at a concentration from about 1 to 10% weight by volume, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM to about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a surfactant and, optionally, and preferably, free or substantially free of citrate/phosphate buffer combination. In an example of Embodiment VI, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, glycine at a concentration from about 20 to about 200 mM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM to about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is free or substantially free polyol; surfactant (e.g. PS8) is preferably, but optionally present; and the composition is, optionally, and preferably, free or substantially free of citrate/phosphate buffer combination. In a further example of Embodiment VI, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, arginine or glycine at a concentration from about 1 to about 250 mM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of polyol. Surfactant (e.g. PS80) is preferably but optionally present, and the composition is, optionally, and preferably, free or substantially free of citrate/phosphate buffer combination. In a further example of Embodiment VI, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is free or substantially free of a polyol. Surfactant (e.g. PS80) is preferably but optionally present; and the composition is, optionally, and preferably, free or substantially free of citrate/phosphate buffer combination. In an example of Embodiment V, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, polysorbate 80 at a concentration from about 1 to 50 μM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is free or substantially free of a polyol and, optionally, and preferably, free or substantially free of citrate/phosphate buffer. In an example of Embodiments I and II, with additional stabilization, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, sorbitol or trehalose at a concentration from about 1 to about 10% weight by volume, EDTA at a concentration from about 0.01% to about 0.5%, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate, as a sole buffer, at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, and wherein the composition is free, or substantially free of citrate/phosphate buffer combination. In a further example of Embodiments I and II, with additional stabilization, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, sorbitol or trehalose at a concentration from about 1 to about 10% weight by volume, methionine at a concentration from about 1 to about 10 mg/ml, %, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, wherein the composition is free or substantially free of any citrate/phosphate buffer combination. In a further example of Embodiments I and II, with additional amino acid stabilization, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol, sorbitol or trehalose (preferably sorbitol) at a concentration from about 1 to about 10% weight by volume, and amino acid that is preferably one and not both of (a) arginine at a concentration from about 1 to about 250 mg/ml, and (b) glycine at a concentration of about 20 to 200 mg/ml, and histidine buffer or succinate buffer at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5; and wherein the composition is free or substantially free of any citrate/phosphate buffer combination. In a further example of Embodiment IV, with additional amino acid stabilization, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, arginine at a concentration from about 1 to about 250 mg/ml, glycine at a concentration of about 20 to 200 mg/ml, and histidine buffer or succinate buffer at a concentration from about 5 mM to about 50 mM, and wherein said composition has a pH of about 5 to about 5.5 and is free or substantially free of polyol; and, optionally, wherein the composition is preferably free of any citrate/phosphate buffer combination. Numerous embodiments of the adalimumab formulations of the present invention were prepared in eight separate blocks of experiments, referred to herein as “Block A” through “Block H.” Each block had 12 to 16 different formulations that were exposed to accelerated storage conditions, 1 week at 40° C. and 2 weeks at 25° C. For each time point the chemical and physical stability of the adalimumab protein was measured by SEC, RP, UV, pH, CE-IEF and CE-SDS. Materials and Methods 1. Equipment Used in the Formulation Studies Equipment Manufacture Model Serial Number Balance Sartorius CPA124S 23350022 pH meter Denver Model 250 E25006B100 Instrument UV Cary Bio 100 EL07103025 HPLC Dionex 3 Ultimate 3000 8047439 UPLC HPLC Dionex 2 Ultimate 3000, 8036991 UPLC Beckman Beckman P/ACE 455436 CE Agilent CE Agilent 3DCE 1600A 3546G00736 Rocker Labnet Orbit P4 8091840 Plate 2. Chemicals and Materials Used in the Formulation Studies Chemical/Materials Producer Purity Lot Number: Citrate Mallinckrodt ACS H28475 Phosphate Fisher FCC 103372 Fisher ACS 113670 Succinate Spectrum Reagent ZM0462 Histidine Spectrum USP XV0239 Spectrum USP ZG0216 Tartrate Spectrum FCC 1BC0152 Maleate TCI >99% 206-738-1 Mannitol BDH USP 57910 Glycine Spectrum FCC YM3312 Spectrum FCC 1BJ0243 Fisher Tissue Grade 070082 Arginine Spectrum USP 2AK0238 Spectrum USP 1CB0771 Sodium Chloride Mallinckrodt ACS J52619 Macron USP 26434 Polysorbate 80 Sigma-Aldrich Low Peroxide 028K5309 Sorbitol Spectrum NF 1AH0521 Trehalose Spectrum N/A 1AE0739 Acetate Mallinckrodt FCC H31613 EDTA Sigma 98.5% 057K00071 Methionine Spectrum USP ZF0377 F-68 Sigma Cell Culture 057K00331 Polysorbate 20 Spectrum NF 1AE0882 Sodium dodecyl Fluka ACS 1344034 sulfate Tris base Fisher ACS S61374 2-mercaptoethanol Fisher Electrophoresis 107667 Material/Reagents Part Number Supplier Slide-A-Lyzers 7K cutoff 66373 Thermo Mini Dialysis Units 69550 Thermo Millex ®-GV 0.22 μM, SLGV004SL Millipore Filter 1 mL Vials 4500050375 SCHOTT cIEF Gel Polymer Solution 477497 Beckman Coulter pI Marker Kit A58481 Beckman Coulter Pharmalyte 3-10 ampholyte 17-0456-01 GE Healthcare Fused silica capillary TSP050375 Polymicro (50 μm i.d.) SDS-MW gel buffer A10663 Beckman 10 kD internal standard A26487 Beckman 3. HPLC Columns Used in the Formulation Studies Column Company Part # Lot Poroshell 300SB- Agilent 660750-906 USZW003083 C8, 2.1 × 75 mm, 5 um Poroshell 300SB- Agilent 660750-906 USZW003073 C8, 2.1 × 75 mm, 5 um ACQUITY UPLC Waters 186005225 138123331 BEH200 SEC, 1.7 um Column, 4.6 × 150 mm ACQUITY UPLC Waters 186005225 01471130951 BEH200 SEC, 1.7 um Column, 4.6 × 150 mm Processing of Humira®. Block A experiments used adalimumab present in commercially available Humira®. Humira® material was dialyzed as follows: 100 μL of Humira® was placed into Mini Dialysis units with a 3.5 MWCO and dialyzed in 1 L of formulation buffer for 24 hours at 4 to 8° C. A few samples did experience a small increase in volume due to the dialysis, but never to extent that the concentration of the polysorbate 80 dropped below the CMC (critical micelle concentration). The protein concentration for each formulation was measured by UV absorbance spectroscopy, using an calculated experimental molar absorptivity based on reported concentration of Humira®, 50 mg/mL. For a number of the formulations the protein concentration was adjusted by using a spin concentrator. The sample was placed in the spin concentrator and rotated at 14,000 RPM for 30 to 60 secs. The protein concentration was then checked with UV. After the targeted protein concentration around 50 mg/mL was reached the samples were filtered through a 0.22 μM sterile filter into sterile vials in a biosafety hood. The samples were then placed on stability at 40° C. for one and two weeks. Processing of a Proprietary Adalimumab Protein. The formulation studies described herein used a proprietary adalimumab biosimilar protein which did not contain polysorbate 80. The material was dialyzed using 7,000 MWCO Slide-A-Lyzers in different formulation buffers for 24 hours at a temperature range between 4 to 8° C. After dialysis the protein concentration was measured by UV and sample pH was measured. The target concentration of samples was 50±2.5 mg/mL, which was adjusted if the sample concentration fell out of the above range. Some of the samples did experience an increase in sample volume do to dilution, requiring the concentration of the protein to increase. For these samples the protein concentration was increased by using spin concentrators, usually at 14,000 rpm for 30 to 60 secs. The pH of a number of samples were adjusted using 1M NaOH or 1M HCl to reach the target pH of 5.2. After the targeted protein concentration and pH of the samples were determined to be within experimental parameters, the samples were filtered through a 0.22 μM sterile filter into sterile vials in a biosafety hood. The samples were then placed on stability at 40° C. for one week and 25° C. for two weeks. Freeze-Thaw Conditions: The freeze thaw samples were prepared on the day of analysis to match with t=0. The samples were frozen at −80° C. between 3 to 7 minutes. The frozen sample was then thawed at room temperature until all the ice had thawed. The freeze and thaw cycle was repeated 5 times for each sample. Agitation Studies. The samples were aggregated at 150 rpm for 24 hours at 4° C. on a rockerplate. A control was prepared and placed next to the rocker plate for each sample that underwent agitation. pH Measurements. The pH each sample was measured using a micro-pH probe. Before the start of analysis the pH probe was calibrated with three pH standards ordered from fisher. The pH values of the stability samples were measured by transferring 604 of each stability sample to 100 μL PCR tube. The micro-pH probe was then submerged into the sample and after the value stabilized it was recorded. UV Absorbance Spectroscopy. UV spectroscopy was used to measure the protein concentration in the samples. The mole extinction coefficient at 280 nm for bulk substance was 1.6355 mg/mL, which was determined experiential. The protein concentrations of the all formulations for LB-140 were measured using a cell path length of 0.0096 cm. Below is the analysis parameters used for LB-140. Scan Range: 400 to 200 nm Average Time (min): 0.1 Date Interval (nm): 1 Scan Rate (nm/min): 600 Cycle Count: 5 Size Exclusion Chromatography (SEC) Method. The SEC method used to analyze the LB-140 stability samples was developed at Legacy BioDesign. Below is a brief summary of the SEC method parameter used for the analysis of the LB-140 samples. Method Parameters Column Information: ACQUITY UPLC BEH200 SEC, 1.7 um Column, 4.6×150 mm Analysis Buffer: 50 mM Phosphate, 250 mM NaCl, pH 6.8 Flow rate: 0.3 mL/min Column temperature: 30° C. Detection: 280 nm Injection volume: 2 μL Sample temperature: Approx. 5° C. RP HPLC Method. The RP HPLC method was found to be stability indicating and was used to analyze LB-140 stability samples. Below is a summary of the RP method parameter used for the analysis of the LB-140. Method Parameters Column Information: Poroshell 300SB-C8, 2.1×75 mm, 5 um Mobile Phase A: 98% (v/v) H2O/2% (v/v) IPA/0.1% (v/v) TFA Mobile Phase B: 10% (v/v) H2O/70% (v/v) IPA/20% (v/v) ACN/0.1% (v/v) TFA Flow rate: 0.25 mL/min Column temperature: 80° C. Detection: 225 nm Injection volume: 1 μL Sample temperature: Approx. 5° C. Run time: 15 minutes Gradient: Time % A % B 0 100 0 10 50 50 10.1 100 0 15 100 0 CE-IEF Analysis. Capillary isoelectric focusing (cIEF) was conducted as described in the PA 800 plus Application Guide published by Beckman Coulter. A more detailed description can be found in a research article published by Mack et al1. All analyses were conducted using a Beckman Coulter P/ACE MDQ system (Beckman Coulter, Inc.; Brea, Calif.) operated at ambient temperature with a 30 cm total length (20 cm effective) neutral capillary. The neutral capillary was prepared by immobilizing poly(acrylamide) to the capillary wall using a method described by Gao et al.2 cIEF samples were prepared by mixing the protein of interest at 0.25 mg/mL with a mixture of 3M urea-cIEF gel containing ampholyte, cathodic stabilizer, anodic stabilizer, and pI markers. Sample was pressure injected at 9.5 psi into the capillary for 4.1 min, after which time it was focused by applying a voltage of 25 kV for 15 min between analyte and catholyte. This step was followed by chemical mobilization at 30 kV for 30 min between analyte and chemical mobilizer. The pI markers and the protein of interest were detected with absorbance at 280 nm during the mobilization step. The pI of the protein was calculated from the resultant regression equation of pI vs. first peak moment obtained from the pI standards. CE-SDS Analysis. Analysis by CE-SDS was conducted under reducing conditions utilizing a method adapted from the SOP published by Beckman-Coulter for determining IgG purity/heterogeneity. Briefly, the antibody was diluted with DDI water to 6 mg/mL, denatured by adding sample buffer (0.1 M Tris/1.0% SDS, pH 8.0), and reduced via addition of 2-mercaptoethanol; the final antibody concentration was 1.2 mg/mL. Denaturing and reduction was facilitated by heating the sample at 70° C. for 10 min. The sample was cooled for 10 min at room temperature prior to analysis. A centrifuge step (300 g, 5 min) was employed prior to heating the sample and directly after the cooling it. CE analysis was conducted using a Beckman Coulter P/ACE MDQ system operated at ambient temperature with a 30 cm total length (20 cm effective, 50 μm i.d.) capillary. Prior to sample introduction, the capillary was sequentially rinsed with 0.1 M NaOH, 0.1M HCL, DDI water, and SDS-gel buffer solution. Sample was injected electrokinetically at 5 kV for 30 s followed by separation at 30 kV for 30 min. For both injection and separation, the instrument was operated in reverse polarity mode. Antibody fragments were detected using absorbance at 214 nm (4 Hz acquisition) and time-normalized areas reported for measured peaks. Block A Formulation Studies The Block A studies examined different buffer systems and used a commercially available adalimumab material which was reprocessed for these studies. We note that U.S. Pat. No. 8,216,583 references stability of an adalimumab formulation in relation to use of a citrate/phosphate buffer system at pH 5.2, and in fact the patent required the use of such a buffer combination. The work we have done, reflected here, indicates that citrate/phosphate is in fact a rather poor buffer choice in comparison to others such as histidine and succinate. In the Block A studies below, pH was kept constant at 5.2. The concentrations of mannitol and polysorbate 80 were also held constant. Samples were kept at 40° C. for two weeks. The study design is summarized in the Table below. TABLE A BLOCK A STUDY DESIGN PS Form Citrate Phosphate Succinate Histidine Tartrate Maleate Mannitol 80 No. API (mM) (mM) (mM) (mM) (mM) (mM) (mM) (%) 1 Humira ® 8 18 0 0 0 0 12 0.1 2 Humira ® 10 0 0 0 0 0 12 0.1 3 Humira ® 0 10 0 0 0 0 12 0.1 4 Humira ® 0 0 10 0 0 0 12 0.1 5 Humira ® 0 0 0 10 0 0 12 0.1 6 Humira ® 0 0 0 0 10 0 12 0.1 7 Humira ® 0 0 0 0 0 10 12 0.1 Analysis by SEC showed that the formulation with citrate alone performed more poorly than the buffer combination (Table A), indicating that the phosphate was the primary stabilizer in that combination. This was surprising and unexpected, as this pH is outside of the nominal buffering capacity range of phosphate, but well within the buffering range for citrate. Furthermore, succinate, histidine, and tartrate did as well or better than the citrate/phosphate combination, indicating that other buffer systems would provide equal or superior stability for adalimumab. Accordingly, the present invention in one of its embodiments is directed to adalimumab formulations exhibiting long term stability, wherein a buffer combination of citrate and phosphate is avoided in favor of at least one buffer selected from the group consisting of histidine, phosphate, succinate and tartrate. Acetate is also a suitable replacement for the citrate phosphate buffer combination. The purity of these stored samples was checked using RP HPLC (FIG. 2). As with SEC, the citrate formulation exhibited the poorest stability, while all of the other buffers did as well or better than the buffer combination found in commercially available adalimumab (Humira®). These results demonstrate our discovery that changing the buffer (i.e. avoiding the citrate/phosphate buffer combination of the commercial adalimumab) could improve the stability profile of adalimumab. Block B Formulation Studies A second study (“BLOCK B”) was conducted examining just changes in the buffer species, where the pH (5.2) was not changed, as outlined in the table below labeled “BLOCK B Study Design. In this case, the commercially available formulation for Humira® was used as a control, while all of the other formulations employed a proprietary adalimumab biosimilar protein. Table B-1, below summarizes the percent monomer for the Block B formulations (as well the percentage amount of an impurity determined to be a fragment of the adalimumab protein). TABLE B BLOCK B STUDY DESIGN PS Form Citrate Phosphate Succinate Histidine Tartrate Maleate Mannitol 80 No. API (mM) (mM) (mM) (mM) (mM) (mM) (mM) (%) 1 Humira ® 8 18 0 0 0 0 12 0.1 2 Adalimumab 10 0 0 0 0 0 12 0.1 biosimilar 3 Adalimumab 0 10 0 0 0 0 12 0.1 biosimilar 4 Adalimumab 0 0 10 0 0 0 12 0.1 biosimilar 5 Adalimumab 0 0 0 10 0 0 12 0.1 biosimilar 6 Adalimumab 0 0 0 0 10 0 12 0.1 biosimilar 7 Adalimumab 0 0 0 0 0 10 12 0.1 biosimilar TABLE B-1 Percent monomer for Block B formulations at t0 and after two weeks at 40 C. (t2) Form Monomer Monomer Fragment Fragment No. API Buffer (t0) (t2) (t0) (t2) 1 Humira ® Citrate/phosphate 99.34 0.26 2 Adalimumab citrate 98.71 97.92 0.62 0.40 biosimilar 3 Adalimumab phosphate 99.21 98.07 0.05 0.30 biosimilar 4 Adalimumab succinate 99.19 98.04 0.04 0.31 biosimilar 5 Adalimumab histidine 99.19 98.41 0.07 0.23 biosimilar 6 Adalimumab tartrate 99.13 98.10 0.04 0.29 biosimilar 7 Adalimumab maleate 98.91 97.90 0.36 0.76 biosimilar As can be seen from Table B-1 above, upon storage for two weeks at 40 C, the monomer content decreases by more than 1% for all of the samples in Block B, except for the one containing histidine (His) buffer (Table B-1). From this study we discovered the likelihood that His would be a superior buffer system for adalimumab. (We note that the fragment level measured by SEC reported for Formulation 2 appears to be incorrect as all of the other initial fragment s levels are less than 0.1%.) Block C Formulation Studies A large-scale formulation screening study was carried out in the studies conducted in Block C (See Table C, below). Samples were stored for one week at 40 C (hereinafter referenced as “t1”) or two weeks at 25 C (hereinafter referenced as “t2”). These conditions were used throughout the remainder of our studies, so this terminology will be employed throughout the present detailed discussion. Block C was designed to expand on the buffer assessment conducted in Block B. In addition, it examined glycine (Gly) and/or arginine (Arg) as possible stabilizers in place of mannitol and/or NaCl (Table C). Note that the buffer system used in the Humira® product employs the 8 mM citrate/18 mM phosphate buffer, which is the composition of Formulation 1 of Block C. In this case, a proprietary adalimumab biosimilar protein was used for formulation 1 of Block C, instead of adalimumab protein obtained from commercially available Humira®. TABLE C BLOCK C STUDY DESIGN Form No. API citrate phosphate succinate histidine glycine arginine mannitol NaCl 1 Adalimumab 8 18 0 0 0 0 65 100 biosimilar 2 Adalimumab 18 8 0 0 0 0 65 100 biosimilar 3 Adalimumab 20 0 0 0 0 0 65 100 biosimilar 4 Adalimumab 20 0 0 0 65 0 0 100 biosimilar 5 Adalimumab 0 20 0 0 65 0 0 100 biosimilar 6 Adalimumab 20 0 0 0 0 65 0 100 biosimilar 7 Adalimumab 0 20 0 0 0 65 0 100 biosimilar 8 Adalimumab 0 0 20 0 65 0 0 100 biosimilar 9 Adalimumab 0 0 20 0 0 65 0 100 biosimilar 10 Adalimumab 0 0 0 20 65 0 0 100 biosimilar 11 Adalimumab 0 0 0 20 0 65 0 100 biosimilar 12 Adalimumab 0 20 0 0 0 130 0 35 biosimilar 13 Adalimumab 0 0 20 0 0 130 0 35 biosimilar 14 Adalimumab 0 0 0 20 0 130 0 35 biosimilar 15 Adalimumab 0 20 0 0 130 0 0 60 biosimilar 16 Adalimumab 0 20 0 20 130 0 0 60 biosimilar TABLE C-1 Measured pH for Block C formulations at t0 and t1 (one week, 40° C.) Form pH pH No. citrate phosphate succinate histidine glycine arginine mannitol NaCl t0 t2 1 8 18 0 0 0 0 65 100 5.51 5.57 2 18 8 0 0 0 0 65 100 5.46 5.43 3 20 0 0 0 0 0 65 100 5.28 5.27 4 20 0 0 0 65 0 0 100 5.27 5.24 5 0 20 0 0 65 0 0 100 5.43 5.44 6 20 0 0 0 0 65 0 100 5.29 5.29 7 0 20 0 0 0 65 0 100 5.28 5.32 8 0 0 20 0 65 0 0 100 5.22 5.17 9 0 0 20 0 0 65 0 100 5.19 5.16 10 0 0 0 20 65 0 0 100 5.28 5.30 11 0 0 0 20 0 65 0 100 5.26 5.29 12 0 20 0 0 0 130 0 35 5.24 5.24 13 0 0 20 0 0 130 0 35 5.18 5.16 14 0 0 0 20 0 130 0 35 5.28 5.35 15 0 20 0 0 130 0 0 60 5.31 5.31 16 0 20 0 20 130 0 0 60 5.36 5.40 TABLE C-2 Monomer content by SEC for formulations in Block C at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. citrate phosphate succinate His Gly Arg mannitol NaCl t0 t1 t2 1 8 18 0 0 0 0 65 100 98.75 97.90 98.06 2 18 8 0 0 0 0 65 100 99.26 98.22 98.80 3 20 0 0 0 0 0 65 100 99.28 98.32 98.78 4 20 0 0 0 65 0 0 100 99.36 98.45 99.03 5 0 20 0 0 65 0 0 100 99.25 98.20 98.77 6 20 0 0 0 0 65 0 100 99.42 98.68 99.10 7 0 20 0 0 0 65 0 100 99.39 98.59 99.13 8 0 0 20 0 65 0 0 100 99.41 98.51 99.04 9 0 0 20 0 0 65 0 100 99.36 98.52 98.96 10 0 0 0 20 65 0 0 100 99.41 98.66 99.15 11 0 0 0 20 0 65 0 100 99.37 98.70 99.15 12 0 20 0 0 0 130 0 35 99.41 98.66 99.14 13 0 0 20 0 0 130 0 35 99.42 98.71 99.17 14 0 0 0 20 0 130 0 35 99.40 98.75 99.26 15 0 20 0 0 130 0 0 60 99.32 98.53 99.05 16 0 20 0 20 130 0 0 60 99.40 98.66 99.19 TABLE C-3 Percent purity by RP HPLC for formulations in Block C at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. citrate phosphate succinate His Gly Arg mannitol NaCl t0 t1 t2 1 8 18 0 0 0 0 65 100 98.04 97.92 98.10 2 18 8 0 0 0 0 65 100 97.94 97.83 98.03 3 20 0 0 0 0 0 65 100 98.03 97.92 98.00 4 20 0 0 0 65 0 0 100 97.94 97.75 97.98 5 0 20 0 0 65 0 0 100 97.98 97.69 97.95 6 20 0 0 0 0 65 0 100 97.89 97.72 97.92 7 0 20 0 0 0 65 0 100 97.80 97.70 97.91 8 0 0 20 0 65 0 0 100 97.98 97.77 98.01 9 0 0 20 0 0 65 0 100 97.98 97.73 97.94 10 0 0 0 20 65 0 0 100 97.98 97.76 98.00 11 0 0 0 20 0 65 0 100 97.87 97.78 97.97 12 0 20 0 0 0 130 0 35 97.88 97.71 97.95 13 0 0 20 0 0 130 0 35 97.95 97.62 97.93 14 0 0 0 20 0 130 0 35 97.98 97.72 98.04 15 0 20 0 0 130 0 0 60 97.91 97.72 97.96 16 0 20 0 20 130 0 0 60 98.00 97.79 97.78 TABLE C-4 Percentage of main bands seen in the cIEF profile of formulations in Block C at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. pH t0 t1 t2 1 8.59 1.94 1.97 1.82 8.43 11.76 11.30 12.49 8.27 58.29 49.88 51.54 8.20 7.18 7.59 8.05 21.49 22.38 19.79 7.86 6.53 5.35 4.66 2 8.60 1.96 1.84 8.44 12.08 10.89 8.29 51.70 47.63 8.22 9.74 12.32 8.09 16.29 18.25 7.91 3.50 3.64 3 8.60 1.83 1.82 1.12 8.43 11.58 9.67 10.40 8.27 45.80 32.99 44.04 8.20 12.44 22.27 18.68 8.01 17.57 16.21 14.40 7.86 4.39 3.61 4 8.57 2.31 2.04 2.13 8.41 12.94 11.51 12.62 8.25 33.37 59.98 61.97 8.20 23.03 8.02 15.21 18.33 16.07 7.88 3.45 5.32 3.70 5 8.58 2.40 2.00 2.30 8.41 13.01 11.02 12.34 8.25 42.09 46.32 37.30 8.21 15.58 10.65 15.80 8.03 18.48 20.58 16.80 7.86 3.74 6.13 4.83 6 8.57 2.83 8.38 13.17 13.23 8.23 32.66 31.18 8.18 17.52 18.54 8.02 17.48 13.82 7.91 5.30 5.83 7 8.58 2.08 2.41 2.64 8.44 13.42 12.64 12.63 8.27 56.79 52.48 54.76 8.16 5.36 6.16 6.38 8.04 16.91 20.09 18.45 7.94 5.44 4.12 5.15 8 8.57 1.76 2.37 1.55 8.44 14.41 12.13 11.61 8.29 60.01 48.87 52.94 8.19 7.07 10.66 8.10 16.22 16.55 17.10 7.95 7.61 5.02 4.55 9 8.58 2.19 2.06 0.99 8.41 11.69 10.64 12.73 8.26 50.07 44.21 60.33 8.19 10.66 10.39 8.01 15.62 21.51 17.79 7.87 4.67 5.37 8.16 10 8.57 1.78 2.64 1.62 8.41 10.55 10.95 8.11 8.25 43.82 42.93 36.11 8.21 15.96 15.24 17.66 8.02 14.63 14.58 14.22 7.88 3.82 4.21 3.95 11 8.58 1.59 1.81 1.89 8.41 12.98 11.58 12.86 8.23 62.74 29.63 12.00 8.19 22.86 34.77 8.02 17.15 19.52 17.06 7.87 5.54 5.56 4.77 12 8.61 0.35 1.57 1.47 8.35 13.24 13.41 8.83 8.19 43.18 60.12 26.52 8.15 15.43 20.46 25.60 7.98 16.74 17.38 7.88 4.96 4.44 4.99 13 8.58 1.71 1.67 8.41 11.63 10.01 8.26 49.19 42.65 8.20 14.25 16.64 8.03 17.35 18.12 7.86 4.28 4.18 14 8.56 1.64 1.79 1.73 8.39 13.17 10.45 10.96 8.25 58.68 46.06 45.60 8.21 11.03 13.34 8.07 14.10 20.24 14.50 7.92 2.10 5.13 4.28 15 8.57 1.74 1.22 1.60 8.41 10.49 15.21 10.78 8.25 46.06 55.05 44.98 8.20 14.46 13.79 8.02 13.90 20.31 10.79 7.89 4.23 4.90 3.43 16 8.56 1.96 1.08 8.40 9.25 12.23 12.58 8.24 38.08 31.03 58.61 8.20 19.02 22.08 21.50 8.03 12.00 13.24 7.31 7.89 4.73 4.82 TABLE C-5 Percentage of bands for light chain (LC), heavy chain (HC), non- glycosylated HC, and other species for formulations in Block C at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 35.87 63.20 0.51 0.42 t1 29.71 63.08 0.37 6.84 t2 31.01 67.83 0.54 0.61 2 t0 29.50 69.57 0.56 0.37 t1 30.51 67.28 0.56 1.65 t2 32.32 65.51 0.56 1.61 3 t0 32.53 66.45 0.54 0.47 t1 33.04 65.34 0.55 1.07 t2 31.94 66.60 0.57 0.90 4 t0 33.40 64.90 0.46 1.24 t1 30.96 67.16 0.52 1.36 t2 32.08 65.84 0.56 1.52 5 t0 34.17 63.89 0.49 1.45 t1 33.60 64.27 0.56 1.57 t2 32.15 66.20 0.48 1.17 6 t0 37.91 60.35 0.54 1.19 t1 34.80 62.88 0.73 1.59 t2 32.90 65.62 0.50 0.99 7 t0 32.17 66.80 0.55 0.49 t1 29.83 68.33 0.59 1.25 t2 33.32 65.97 0.55 0.15 8 t0 33.83 65.51 0.49 0.17 t1 30.37 68.48 0.58 0.57 t2 32.86 66.40 0.55 0.19 9 t0 30.69 69.31 0.00 0.00 t1 34.30 64.24 0.52 0.94 t2 29.08 69.87 0.62 0.43 10 t0 38.68 59.95 0.57 0.80 t1 36.52 58.65 0.00 4.83 t2 43.68 54.39 1.92 0.00 11 t0 35.25 59.00 1.75 4.00 t1 30.71 67.58 0.66 1.05 t2 30.18 67.14 0.47 2.21 13 t0 44.58 55.42 0.00 0.00 t1 37.73 60.75 0.25 1.28 t2 38.05 61.44 0.52 0.00 14 t0 32.50 66.66 0.60 0.24 t1 30.91 67.77 0.61 0.70 t2 29.14 70.32 0.23 0.31 15 t0 30.07 68.95 0.63 0.35 t1 30.14 68.49 0.62 0.75 t2 31.57 67.55 0.62 0.26 16 t0 30.54 68.61 0.63 0.22 t1 29.81 68.81 0.63 0.75 t2 29.46 69.14 0.59 0.81 Discussion of Block C Results Referring to Table C-1 above, the pH was measured and found to be relatively stable for all of the formulations. However, the initial pH values were slightly higher for the citrate/phosphate formulations. The least stable formulation by SEC analysis appears to be Formulation 1, the one using the Humira® buffer system. By comparison we discovered that formulations using His as the buffer and/or formulations containing Gly or Arg exhibited the greatest stability (See Table C-2). Similar trends are seen when the purity by RP HPLC is considered (See Table C-3). It appears that SEC may be a better stability-indicating method than RP HPLC, although, when taken as a whole, the RP HPLC method does appear to be stability-indicating. Based on the Block C data summarized above, we have discovered that Histidine is suitable as a preferred buffer in terms of formulation stability, and that glycine or arginine, or combinations thereof, are also stability enhancing components for inclusion in an adalimumab formulation. The stored samples were further analyzed by cIEF at t1 and t2 (Table C-4 above). A proprietary adalimumab material exhibit four to five peaks with integrated intensities above 1% or so. In general, there are some small decreases in the intensity of the main peak upon storage. These losses are usually greater at t1 than at t2. Still, no significant new peaks are observed, suggesting that there is minimal chemical degradation occurring that would lead to changes in the overall charge on the protein. The variance in the data indicates that this method, while useful for characterization, does not appear to be stability-indicating. The final analytical method used to evaluate the stability of adalimumab formulation is CE-SDS, which is essentially the CE version of SDS-PAGE slab gels. This method indicates that the relative areas of the LC peak do decrease when stored at elevated temperatures (Table C-5), while the amount of new peaks (cumulatively called ‘Other’) increases. Altogether, these changes are usually less than 2% for any of the formulations. There are some samples where the percentage of ‘Other’ is in the 4-6% range, but these are likely artifacts. Block D Formulation Studies Another set of formulations were evaluated as “Block D.” Sixteen formulations were designed to evaluate other stabilizers as alternatives to mannitol, such as sorbitol and trehalose (See Table D). Block D also examined using mannitol or NaCl as the sole tonicity agent, instead of using a mixture of the two excipients. The pH stability of the formulations was quite good, although the actual initial pH values were slightly lower than the target values for some formulations (Table D-1). TABLE D BLOCK D STUDY DESIGN Form PS No. API citrate phosphate sorbitol trehalose mannitol NaCl 80 1 Adalimumab 8 18 0 0 65 100 0.1 biosimilar 2 Adalimumab 8 18 0 0 65 100 0 biosimilar 3 Adalimumab 20 0 0 0 65 100 0.1 biosimilar 4 Adalimumab 20 0 0 0 65 100 0 biosimilar 5 Adalimumab 0 20 0 0 65 100 0.1 biosimilar 6 Adalimumab 0 20 0 0 65 100 0 biosimilar 7 Adalimumab 8 18 65 0 0 100 0.1 biosimilar 8 Adalimumab 8 18 0 65 0 100 0.1 biosimilar 9 Adalimumab 0 20 65 0 0 100 0.1 biosimilar 10 Adalimumab 0 10 0 0 240 0 0.1 biosimilar 11 Adalimumab 0 10 240 0 0 0 0.1 biosimilar 12 Adalimumab 0 10 0 240 0 0 0.1 biosimilar 13 Adalimumab 10 0 0 0 0 150 0.1 biosimilar 14 Adalimumab 10 0 0 0 0 150 0 biosimilar 15 Adalimumab 0 10 0 0 0 150 0.1 biosimilar 16 Adalimumab 0 10 0 0 0 150 0 biosimilar TABLE D-1 Measured pH for Block D formulations at t0 and t1 (one week, 40° C.) Form PS No. API citrate phosphate sorbitol trehalose mannitol NaCl 80 t0 t1 t2 1 Adalimumab 8 18 0 0 65 100 0.1 5.09 5.17 5.12 biosimilar 2 Adalimumab 8 18 0 0 65 100 0 5.12 5.16 5.16 biosimilar 3 Adalimumab 20 0 0 0 65 100 0.1 5.11 5.16 5.14 biosimilar 4 Adalimumab 20 0 0 0 65 100 0 5.13 5.17 5.18 biosimilar 5 Adalimumab 0 20 0 0 65 100 0.1 5.19 5.25 5.24 biosimilar 6 Adalimumab 0 20 0 0 65 100 0 5.16 5.24 5.17 biosimilar 7 Adalimumab 8 18 65 0 0 100 0.1 5.14 5.17 5.18 biosimilar 8 Adalimumab 8 18 0 65 0 100 0.1 5.15 5.21 5.16 biosimilar 9 Adalimumab 0 20 65 0 0 100 0.1 5.19 5.29 5.28 biosimilar 10 Adalimumab 0 10 0 0 240 0 0.1 5.23 5.28 5.27 biosimilar 11 Adalimumab 0 10 240 0 0 0 0.1 5.45 5.35 5.33 biosimilar 12 Adalimumab 0 10 0 240 0 0 0.1 5.44 5.32 5.31 biosimilar 13 Adalimumab 10 0 0 0 0 150 0.1 5.30 5.25 5.23 biosimilar 14 Adalimumab 10 0 0 0 0 150 0 5.39 5.20 5.18 biosimilar 15 Adalimumab 0 10 0 0 0 150 0.1 5.35 5.30 5.22 biosimilar 16 Adalimumab 0 10 0 0 0 150 0 5.41 5.33 5.28 biosimilar TABLE D-2 Monomer content by SEC for formulations in Block D at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. API citrate phosphate sorbitol trehalose mannitol NaCl 80 t0 t1 t2 1 Adalimumab 8 18 0 0 65 100 0.1 99.28 98.21 98.96 biosimilar 2 Adalimumab 8 18 0 0 65 100 0 99.25 98.11 98.85 biosimilar 3 Adalimumab 20 0 0 0 65 100 0.1 99.25 98.16 98.86 biosimilar 4 Adalimumab 20 0 0 0 65 100 0 99.27 98.26 98.92 biosimilar 5 Adalimumab 0 20 0 0 65 100 0.1 99.24 98.16 98.84 biosimilar 6 Adalimumab 0 20 0 0 65 100 0 99.21 98.23 98.82 biosimilar 7 Adalimumab 8 18 65 0 0 100 0.1 99.30 98.19 98.94 biosimilar 8 Adalimumab 8 18 0 65 0 100 0.1 99.28 98.14 98.85 biosimilar 9 Adalimumab 0 20 65 0 0 100 0.1 99.29 98.23 98.90 biosimilar 10 Adalimumab 0 10 0 0 240 0 0.1 97.93 98.54 biosimilar 11 Adalimumab 0 10 240 0 0 0 0.1 99.32 98.65 99.00 biosimilar 12 Adalimumab 0 10 0 240 0 0 0.1 99.32 98.53 98.96 biosimilar 13 Adalimumab 10 0 0 0 0 150 0.1 99.29 98.12 98.84 biosimilar 14 Adalimumab 10 0 0 0 0 150 0 99.28 98.28 98.90 biosimilar 15 Adalimumab 0 10 0 0 0 150 0.1 99.26 97.99 98.83 biosimilar 16 Adalimumab 0 10 0 0 0 150 0 99.20 97.76 98.62 biosimilar TABLE D-3 Percent purity by RP HPLC for formulations in Block D at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. API citrate phosphate sorbitol trehalose mannitol NaCl 80 t0 t1 t2 1 Adalimumab 8 18 0 0 65 100 0.1 98.17 97.75 98.02 biosimilar 2 Adalimumab 8 18 0 0 65 100 0 98.09 97.84 98.08 biosimilar 3 Adalimumab 20 0 0 0 65 100 0.1 98.03 97.81 98.19 biosimilar 4 Adalimumab 20 0 0 0 65 100 0 98.17 97.85 98.06 biosimilar 5 Adalimumab 0 20 0 0 65 100 0.1 98.11 97.88 98.18 biosimilar 6 Adalimumab 0 20 0 0 65 100 0 98.21 97.77 98.10 biosimilar 7 Adalimumab 8 18 65 0 0 100 0.1 98.11 97.80 98.14 biosimilar 8 Adalimumab 8 18 0 65 0 100 0.1 98.06 97.73 98.03 biosimilar 9 Adalimumab 0 20 65 0 0 100 0.1 98.09 97.80 98.07 biosimilar 10 Adalimumab 0 10 0 0 240 0 0.1 98.13 97.82 98.08 biosimilar 11 Adalimumab 0 10 240 0 0 0 0.1 98.10 97.90 98.06 biosimilar 12 Adalimumab 0 10 0 240 0 0 0.1 98.13 97.95 98.14 biosimilar 13 Adalimumab 10 0 0 0 0 150 0.1 98.07 97.79 98.02 biosimilar 14 Adalimumab 10 0 0 0 0 150 0 98.13 97.78 98.14 biosimilar 15 Adalimumab 0 10 0 0 0 150 0.1 98.17 97.80 98.10 biosimilar 16 Adalimumab 0 10 0 0 0 150 0 98.14 97.79 98.06 biosimilar TABLE D-4 Percentage of main bands seen in the cIEF profile of formulations in Block D at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. pH t0 t1 t2 1 8.56 2.26 1.81 8.41 13.84 12.88 11.73 8.25 62.27 59.80 56.15 8.14 6.48 8.04 15.71 22.93 13.73 7.99 5.92 4.39 4.13 2 8.55 2.08 1.58 8.40 12.89 12.58 8.24 60.15 53.24 8.14 5.98 6.69 8.03 11.92 9.72 7.98 3.65 5.67 3 8.57 1.58 2.10 1.89 8.41 11.87 11.83 11.99 8.26 54.93 54.45 54.51 8.16 9.10 6.31 8.24 8.05 9.21 11.16 10.22 7.91 7.60 4.16 5.26 4 8.57 3.57 1.82 1.05 8.40 11.12 10.66 10.83 8.24 49.37 47.85 42.34 8.14 3.01 1.83 3.68 8.03 10.11 10.06 17.12 7.90 2.78 4.72 3.84 5 8.55 2.30 2.18 2.13 8.40 7.63 8.86 8.63 8.25 33.90 14.41 16.64 8.20 23.41 33.90 33.75 8.03 10.14 20.39 19.42 7.99 6.76 5.42 4.63 6 8.59 1.87 1.39 8.42 11.25 11.18 11.89 8.27 50.07 61.72 64.17 8.20 12.43 22.08 19.18 8.03 10.20 7.91 2.70 5.01 3.38 7 8.55 8.40 8.25 8.20 8.03 7.99 8 8.59 1.46 2.64 1.16 8.39 13.52 13.62 7.37 8.22 60.79 50.83 55.40 8.08 5.21 11.28 9.78 8.02 15.24 8.55 11.94 7.91 3.79 3.02 5.18 9 8.53 2.64 3.25 1.94 8.38 13.83 12.72 11.67 8.25 64.97 51.32 54.14 8.17 8.33 11.21 8.61 8.06 11.75 9.98 9.03 8.01 5.79 4.80 7.31 10 8.54 1.78 3.26 8.38 13.04 11.19 8.21 60.53 44.83 8.15 19.60 10.95 7.99 9.41 7.90 5.05 4.27 11 8.52 1.95 2.11 1.89 8.36 11.24 12.43 12.43 8.21 48.64 54.10 59.90 8.13 11.69 6.31 8.00 10.30 21.14 11.14 8.01 5.27 5.64 8.32 12 8.51 1.85 8.29 11.31 11.38 8.18 63.11 45.14 8.14 2.54 8.05 16.16 22.03 7.94 5.03 6.88 13 8.62 3.51 3.05 8.44 12.44 12.30 8.29 65.10 51.44 8.21 12.18 8.06 15.37 17.25 7.91 3.58 3.77 14 8.61 2.74 1.73 8.43 10.60 12.19 8.27 46.23 41.11 8.21 13.97 10.49 8.05 18.56 17.52 7.91 5.15 15 8.62 8.35 12.40 10.91 8.34 8.21 31.87 30.32 36.39 8.20 41.14 25.57 30.62 8.02 12.42 13.72 18.26 7.89 2.18 5.44 3.86 16 8.61 8.48 12.96 12.86 13.19 8.34 34.40 31.45 39.25 8.31 27.74 20.29 18.81 8.05 22.76 19.35 7.89 8.17 7.69 4.83 TABLE D-5 Percentage of bands for light chain (LC), heavy chain (HC), non- glycosylated HC, and other species for formulations in Block D at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 t1 34.11 62.58 0.58 2.73 t2 33.19 64.28 0.60 1.92 2 t0 30.25 66.81 0.64 2.31 t1 30.61 65.79 0.54 3.07 t2 29.22 67.04 0.64 3.10 3 t0 27.48 68.51 0.59 3.42 t1 30.84 67.27 0.54 1.35 t2 30.30 68.13 0.58 0.99 4 t0 30.88 68.33 0.60 0.19 t1 29.76 68.32 0.57 1.34 t2 31.49 66.95 0.55 1.01 5 t0 33.77 64.50 0.56 1.17 t1 31.59 66.54 0.52 1.34 t2 29.19 69.16 0.59 1.06 6 t0 30.90 68.08 0.56 0.47 t1 29.32 69.88 0.54 0.26 t2 31.08 67.58 0.54 0.79 7 t0 30.41 68.60 0.56 0.43 t1 30.87 66.95 0.55 1.63 t2 30.14 68.28 0.55 1.03 8 t0 31.68 67.41 0.60 0.31 t1 t2 9 t0 29.62 68.12 0.51 1.75 t1 t2 29.46 68.10 0.61 1.83 10 t0 29.80 67.99 0.58 1.64 t1 30.04 65.53 0.45 3.98 t2 30.41 66.27 0.53 2.80 11 t0 29.85 67.63 0.61 1.91 t1 29.02 68.18 0.60 2.20 t2 30.44 67.14 0.58 1.84 12 t0 29.38 68.11 0.55 1.96 t1 30.16 65.55 0.49 3.80 t2 28.20 69.19 0.59 2.02 13 t0 31.38 66.28 0.55 1.79 t1 33.67 64.10 0.56 1.67 t2 29.72 67.99 0.58 1.71 14 t0 37.34 60.53 0.52 1.62 t1 33.03 63.46 0.53 2.97 t2 34.39 63.62 0.54 1.45 15 t0 30.20 68.42 0.59 0.79 t1 28.67 69.42 0.58 1.33 t2 29.96 68.24 0.56 1.24 16 t0 31.62 66.95 0.58 0.85 t1 30.48 66.36 0.55 2.61 t2 27.94 70.17 0.60 1.29 Results of Block D The pH stability was quite good for these formulations (Table D-1). Once again, the commercial adalimumab (Humira®) formulation was used as a control (but using a proprietary adalimumab biosimilar protein as the API). The commercial formulation again showed poorer stability by SEC than those using single buffers like phosphate and His (See Table D-2). Of the two buffers used in Humira®, we have now discovered that phosphate is the better stabilizer. This is surprising, as phosphate has virtually no buffer capacity at pH 5.2, while citrate buffers well at this pH. This suggests that the differences in stability profile may be due to direct interaction of the buffer with the protein, a phenomenon that, in the case of the commercial Humira® formulation, we believe was not previously understood or appreciated. Accordingly, the comparative benefit of selecting phosphate as a buffer in an adalimumab formulation, due to superior stability in the formulation versus the selection of a citrate/phosphate combination constitutes one of the important aspects of our invention. Both sorbitol and trehalose display better stability profiles than mannitol when used as the sole tonicity agent in these formulations. It also appears that removal of the polysorbate 80 (PS 80) decreases stability somewhat. The best stability profile by SEC appears to be for Formulations 10 and 11, which contain high concentrations of sorbitol or trehalose in place of mannitol/NaCl (Table D-2). These results indicate to us that removing NaCl from the formulation, or limiting its concentration below certain targeted levels (for example less than about 100 mM), will be beneficial for stability. (We note that mannitol does appear to be a stabilizing ingredient, but at levels preferably above 150.) The RP data indicates that either citrate or phosphate provides better stability than the combination used in Humira® (Table D-3). Again, the avoidance of the citrate/phosphate combination represents an important feature of our invention. It could not have been known or predicted that citrate alone, or phosphate alone would provide better formulation stability than the commercial buffer system comprising a combination of citrate and phosphate. The cIEF analyses were run for Block D samples (Table D-4 above). As before, there is some decrease in the intensity of the main peak, but no new peaks are observed. In some cases, there is some small increase in the intensity of the more acidic peaks. The decreases in the main peak appear to be greater at t1 than at t2, suggesting that degradation at 5° C. would be almost imperceptible. Still, overall it looks like less than 5% (and probably much less than 5%) is degrading as measured by cIEF (Table D-4). Likewise, little degradation is seen by CE-SDS (Table D-5). At most 2 to 4% degradation is seen, but the variability in the method makes it difficult to determine if these are real changes. There does appear to be higher impurity levels (Other) for Formulations 1 and 2 and 10 through 14. Block E Formulation Studies This block of formulations was designed to evaluate the stability of formulations at different pH levels. If a buffer is not specified, acetate buffer (10 mM) was employed (Table E). A secondary objective was to evaluate Gly and Arg at higher concentrations and in combination as alternative stabilizers to mannitol and NaCl. TABLE E BLOCK E STUDY DESIGN Form PS No. API pH citrate phosphate sorbitol Gly Arg mannitol NaCl 80 1 Adalimumab 5.2 8 18 0 0 0 65 100 0.1 biosimilar 2 Adalimumab 3.5 8 18 0 0 0 65 100 0.1 biosimilar 3 Adalimumab 5.2 0 0 0 0 0 65 100 0.1 biosimilar 4 Adalimumab 3.5 0 0 0 0 0 65 100 0.1 biosimilar 5 Adalimumab 3.5 0 0 65 0 0 0 100 0.1 biosimilar 6 Adalimumab 3.5 0 0 0 0 130 0 0 0.1 biosimilar 7 Adalimumab 3.5 0 0 0 0 130 0 0 0 biosimilar 8 Adalimumab 3.5 0 0 0 240 0 0 0 0 biosimilar 9 Adalimumab 5.2 0 0 0 240 0 0 0 0 biosimilar 10 Adalimumab 3.5 0 0 0 100 100 0 0 0 biosimilar 11 Adalimumab 5.2 0 0 0 100 100 0 0 0 biosimilar 12 Adalimumab 3.5 0 0 0 150 50 0 0 0 biosimilar TABLE E-1 Measured pH for Block E formulations at t0 and t1 (one week, 40° C.) Form PS No. pH citrate phosphate sorbitol Gly Arg mannitol NaCl 80 t0 t1 t2 1 5.2 8 18 0 0 0 65 100 0.1 5.15 5.11 5.21 2 3.5 8 18 0 0 0 65 100 0.1 3.36 3.49 3.50 3 5.2 0 0 0 0 0 65 100 0.1 5.13 5.24 5.24 4 3.5 0 0 0 0 0 65 100 0.1 3.31 3.43 3.45 5 3.5 0 0 65 0 0 0 100 0.1 3.30 3.48 3.42 6 3.5 0 0 0 0 130 0 0 0.1 3.24 3.52 3.42 7 3.5 0 0 0 0 130 0 0 0 3.27 3.59 3.48 8 3.5 0 0 0 240 0 0 0 0 3.27 3.33 3.39 9 5.2 0 0 0 240 0 0 0 0 5.05 5.25 5.20 10 3.5 0 0 0 100 100 0 0 0 3.30 3.45 3.41 11 5.2 0 0 0 100 100 0 0 0 5.20 5.38 5.39 12 3.5 0 0 0 150 50 0 0 0 3.24 3.38 3.37 TABLE E-2 Monomer content by SEC for formulations in Block E at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. pH citrate phosphate sorbitol Gly Arg mannitol NaCl 80 t0 t1 t2 1 5.2 8 18 0 0 0 65 100 0.1 99.23 98.20 98.85 2 3.5 8 18 0 0 0 65 100 0.1 98.82 44.15 86.37 3 5.2 0 0 0 0 0 65 100 0.1 99.30 98.37 99.02 4 3.5 0 0 0 0 0 65 100 0.1 95.85 33.51 76.21 5 3.5 0 0 65 0 0 0 100 0.1 97.37 26.21 77.80 6 3.5 0 0 0 0 130 0 0 0.1 97.79 35.67 65.83 7 3.5 0 0 0 0 130 0 0 0 99.00 55.51 90.60 8 3.5 0 0 0 240 0 0 0 0 99.24 75.60 98.24 9 5.2 0 0 0 240 0 0 0 0 99.08 98.63 99.18 10 3.5 0 0 0 100 100 0 0 0 99.28 51.03 91.66 11 5.2 0 0 0 100 100 0 0 0 99.32 98.54 99.09 12 3.5 0 0 0 150 50 0 0 0 99.29 45.86 93.06 TABLE E-3 Percent purity by RP HPLC for formulations in Block E at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. pH citrate phosphate sorbitol Gly Arg mannitol NaCl 80 t0 t1 t2 1 5.2 8 18 0 0 0 65 100 0.1 98.58 96.88 96.91 2 3.5 8 18 0 0 0 65 100 0.1 98.51 90.29 95.99 3 5.2 0 0 0 0 0 65 100 0.1 98.50 96.90 96.83 4 3.5 0 0 0 0 0 65 100 0.1 98.56 91.18 95.55 5 3.5 0 0 65 0 0 0 100 0.1 98.45 90.96 95.71 6 3.5 0 0 0 0 130 0 0 0.1 98.71 93.28 95.38 7 3.5 0 0 0 0 130 0 0 0 98.40 90.65 96.54 8 3.5 0 0 0 240 0 0 0 0 98.03 93.94 96.82 9 5.2 0 0 0 240 0 0 0 0 98.23 97.19 97.12 10 3.5 0 0 0 100 100 0 0 0 98.13 91.10 96.67 11 5.2 0 0 0 100 100 0 0 0 98.13 97.17 97.12 12 3.5 0 0 0 150 50 0 0 0 98.07 93.40 96.48 TABLE E-4 Percentage of bands for light chain (LC), heavy chain (HC), non- glycosylated HC, and other species for formulations in Block E at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 29.97 68.80 0.59 0.64 t1 28.49 70.07 0.60 0.81 t2 28.21 70.29 0.59 0.90 2 t0 28.50 68.67 0.52 2.31 t1 29.69 50.92 0.30 19.09 t2 28.76 69.64 0.60 1.00 3 t0 24.30 74.01 0.60 1.09 t1 28.27 69.63 0.60 1.51 t2 28.17 69.89 0.54 1.40 4 t0 29.45 68.73 0.56 1.26 t1 29.52 51.33 0.30 18.86 t2 27.92 65.73 0.52 5.83 5 t0 35.59 63.85 0.56 0.00 t1 32.47 48.72 0.30 18.52 t2 34.98 60.88 0.46 3.68 6 t0 34.33 63.39 0.51 1.77 t1 t2 35.32 61.31 0.45 2.92 7 t0 30.13 68.87 0.60 0.40 t1 28.13 54.79 0.59 16.49 t2 34.39 63.32 0.53 1.76 8 t0 33.27 64.97 0.55 1.21 t1 33.20 52.62 0.33 13.85 t2 33.25 65.26 0.58 0.92 9 t0 32.28 66.34 0.57 0.81 t1 31.81 65.76 0.57 1.86 t2 31.23 66.81 0.57 1.39 10 t0 35.66 63.36 0.43 0.56 t1 24.96 58.61 0.33 16.10 t2 33.44 66.03 0.53 0.00 11 t0 29.75 69.08 0.60 0.57 t1 27.67 70.83 0.61 0.89 t2 28.81 69.86 0.59 0.73 12 t0 30.23 49.07 0.26 20.44 t1 28.14 70.11 0.58 1.18 t2 29.75 69.08 0.60 0.57 TABLE E-5 Percentage of main bands seen in the cIEF profile of formulations in Block E at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C. Form No. pH t0 t1 t2 1 8.56 8.37 12.52 12.65 8.23 51.77 50.04 8.14 8.03 21.54 12.40 7.93 14.17 16.26 2 1.88 1.49 8.37 10.07 17.66 14.15 8.21 37.52 32.26 33.88 8.13 19.03 9.96 8.01 16.57 28.70 7.93 4.12 7.45 4 8.54 1.04 2.67 8.38 10.50 9.32 8.21 68.34 31.91 8.13 28.52 8.02 16.55 10.05 7.88 3.57 8.67 5 6 7 8 9 8.60 1.40 2.60 3.26 8.43 10.04 12.33 12.03 8.26 62.39 63.19 63.89 8.14 8.03 15.00 16.95 16.57 7.88 7.08 4.93 4.25 Results of Block E Studies The pH stability was modest, with increases in pH occurring at t1 for many of the formulations, especially those buffered with acetate at low pH (Table E-1 above). Two of the samples (Formulations 6 and 12) gelled at t1. There were sizable losses in monomer content for the pH3.5 samples (Table E-3), whereas the pH 5.2 samples displayed stability comparable to what was seen in the preceding Blocks. It was also clear that the degradation was much more pronounced at 40 C than at 25, despite being stored for twice the length of time. In fact, Formulation 8 lost less than 1% monomer at t2 (Table E-2). The Gly and Arg formulations all displayed good stability, provided the pH was held 5.2. The data in this block of studies confirm our discovery that glycine or arginine, or a mixture thereof are good stabilizers in an adalimumab formulation. The RP HPLC data shows large decreases in purity, although not nearly as great as for monomer loss by SEC (Table E-3). This suggests that chemical instability is less than physical instability. As with the SEC results, the loss of stability is more pronounced at t1 than at t2. The CE-SDS results show large increases in new peaks, with the Other category increasing to 15-20% for low pH samples at t1 (Table E-4). The most stable formulation by CE-SDS appears to be Formulation 11, which contains both Gly and Arg as the tonicity modifiers/stabilizers. We encountered difficulties running the cIEF for many of the Block E samples. However, given the clearly inferior stability at pH 3.5, it is unlikely that cIEF would provide any new information on those stability profiles. For example, Formulation 4 (pH 3.5) shows a splitting of the main peak at t1. Block F Formulation Studies The Block F studies were intended to investigate the stability for His-containing formulation using either mannitol, Gly or Arg as the sole tonicity modifier (Table F below). It also served as an opportunity to evaluate additives such as EDTA and methionine (Met), which can be effective at slowing oxidation. In addition, one high citrate concentration and one high phosphate concentration formulation were examined. TABLE F BLOCK F STUDY DESIGN Form PS No. API pH citrate phosphate His Gly Arg mannitol NaCl 80 EDTA Met 1 Adalimumab 5.2 8 18 0 0 0 65 100 0.1 0 0 biosimilar 2 Adalimumab 5.2 8 18 0 0 0 65 100 0.1 0.5 0 biosimilar 3 Adalimumab 5.2 0 0 10 0 150 0 0 0 0.1 0 biosimilar 4 Adalimumab 5.2 0 0 10 0 150 0 0 0 0.5 0 biosimilar 5 Adalimumab 5.2 0 0 10 0 0 240 0 0 0 0 biosimilar 6 Adalimumab 5.2 0 0 10 0 0 240 0 0 0 10 biosimilar 7 Adalimumab 5.2 0 0 10 0 0 240 0 0 0 50 biosimilar 8 Adalimumab 5.2 30 0 0 240 0 0 0 0 0 0 biosimilar 9 Adalimumab 5.2 0 30 0 240 0 0 0 0 0 0 biosimilar 10 Adalimumab 5.2 0 0 30 240 0 0 0 0 0 0 biosimilar 11 Adalimumab 5.2 0 0 20 0 25 120 0 0.1 0 0 biosimilar 12 Adalimumab 5.2 0 0 20 0 25 120 0 0.1 0 0 biosimilar TABLE F-1 Measured pH for Block F formulations at t0 and t1 (one week, 40° C.) Form PS No. citrate phosphate His Gly Arg mannitol NaCl 80 EDTA Met t0 t1 t2 1 8 18 0 0 0 65 100 0.1 0 0 4.67 4.88 4.77 2 8 18 0 0 0 65 100 0.1 0.5 0 5.05 5.15 5.20 3 0 0 10 0 150 0 0 0 0.1 0 5.11 5.22 5.27 4 0 0 10 0 150 0 0 0 0.5 0 4.95 5.06 5.15 5 0 0 10 0 0 240 0 0 0 0 5.12 5.25 5.29 6 0 0 10 0 0 240 0 0 0 10 4.45 4.74 4.67 7 0 0 10 0 0 240 0 0 0 50 5.03 5.24 5.24 8 30 0 0 240 0 0 0 0 0 0 5.09 5.18 5.22 9 0 30 0 240 0 0 0 0 0 0 5.13 5.25 5.32 10 0 0 30 240 0 0 0 0 0 0 5.08 5.24 5.24 11 0 0 20 0 25 120 0 0.1 0 0 5.01 5.17 5.18 12 0 0 20 0 25 120 0 0.1 0 0 5.06 5.20 5.19 TABLE F-2 Monomer content by SEC for formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. citrate phosphate His Gly Arg mannitol NaCl 80 EDTA Met t0 t1 t2 1 8 18 0 0 0 65 100 0.1 0 0 97.69 94.75 96.06 2 8 18 0 0 0 65 100 0.1 0.5 0 99.25 98.14 98.92 3 0 0 10 0 150 0 0 0 0.1 0 99.30 98.54 99.16 4 0 0 10 0 150 0 0 0 0.5 0 99.28 98.31 99.14 5 0 0 10 0 0 240 0 0 0 0 99.17 98.64 99.14 6 0 0 10 0 0 240 0 0 0 10 99.07 98.50 99.07 7 0 0 10 0 0 240 0 0 0 50 99.29 98.92 99.24 8 30 0 0 240 0 0 0 0 0 0 99.28 98.40 99.04 9 0 30 0 240 0 0 0 0 0 0 99.30 98.50 99.08 10 0 0 30 240 0 0 0 0 0 0 99.31 98.60 99.23 11 0 0 20 0 25 120 0 0.1 0 0 99.27 98.64 99.16 12 0 0 20 0 25 120 0 0.1 0 0 99.29 98.51 99.17 TABLE F-3 Percent purity by RP HPLC for formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. citrate phosphate His Gly Arg mannitol NaCl 80 EDTA Met t0 t1 t2 1 8 18 0 0 0 65 100 0.1 0 0 97.47 96.89 97.98 2 8 18 0 0 0 65 100 0.1 0.5 0 97.33 97.02 97.99 3 0 0 10 0 150 0 0 0 0.1 0 97.64 97.14 98.04 4 0 0 10 0 150 0 0 0 0.5 0 97.59 97.00 97.97 5 0 0 10 0 0 240 0 0 0 0 97.11 97.30 98.03 6 0 0 10 0 0 240 0 0 0 10 97.61 97.27 98.03 7 0 0 10 0 0 240 0 0 0 50 97.55 97.37 98.08 8 30 0 0 240 0 0 0 0 0 0 97.48 97.51 98.05 9 0 30 0 240 0 0 0 0 0 0 97.64 97.58 98.03 10 0 0 30 240 0 0 0 0 0 0 97.68 97.41 98.06 11 0 0 20 0 25 120 0 0.1 0 0 97.67 97.18 98.03 12 0 0 20 0 25 120 0 0.1 0 0 97.68 97.33 98.02 TABLE F-4 Percentage of bands for light chain (LC), heavy chain (HC), non- glycosylated HC, and other species for formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 27.36 71.86 0.60 0.17 t1 t2 25.34 73.18 0.63 0.86 2 t0 27.80 71.07 0.60 0.53 t1 28.29 71.08 0.63 0.00 t2 27.53 70.97 0.64 0.86 3 t0 27.78 70.62 0.65 0.95 t1 28.26 70.85 0.66 0.23 t2 28.26 70.50 0.63 0.61 4 t0 28.20 70.24 0.60 0.96 t1 29.17 69.30 0.74 0.80 t2 29.17 70.27 0.56 0.00 5 t0 27.50 70.74 0.59 1.17 t1 29.56 65.79 0.41 4.24 t2 28.24 69.90 0.58 1.28 6 t0 29.10 68.84 0.54 1.52 t1 28.58 69.18 0.54 1.70 t2 27.47 70.39 0.54 1.60 7 t0 27.87 70.28 0.55 1.30 t1 t2 8 t0 34.72 64.87 0.41 0.00 t1 34.94 64.53 0.53 0.00 t2 33.21 65.76 0.50 0.52 9 t0 31.96 68.04 0 0 t1 48.51 51.49 0 0 t2 33.15 65.82 0.57 0.46 10 t0 27.81 71.27 0.51 0.40 t1 29.59 68.46 0.53 1.43 t2 31.25 67.89 0.50 0.36 11 t0 27.33 70.80 0.61 1.26 t1 26.54 71.00 0.64 1.82 t2 29.46 69.85 0.69 0.00 12 t0 24.18 71.21 0 4.61 t1 t2 28.95 68.98 0.59 1.46 TABLE F-5 Percentage of main bands seen in the cIEF profile of formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C. Form No. pH t0 t1 t2 1 8.65 2.11 8.31 13.07 11.43 34.17 8.24 64.66 67.99 28.67 8.14 2.29 8.08 16.13 17.73 15.98 7.95 6.14 4.80 2 8.60 1.56 1.93 1.12 8.48 12.95 11.26 11.12 8.24 58.99 55.85 60.37 8.13 20.98 22.43 18.77 7.93 3.56 6.41 6.09 8.60 1.56 1.93 1.12 3 8.56 1.56 1.69 8.34 10.88 12.85 10.83 8.18 66.93 55.35 62.00 8.02 17.28 19.04 20.13 7.89 4.91 11.21 5.35 4 8.58 1.86 1.68 8.45 13.79 10.61 12.84 8.27 65.06 51.89 61.94 8.06 19.29 18.85 25.22 7.96 6.28 4.91 5 8.60 1.35 1.78 1.45 8.45 12.35 13.63 8.59 8.27 60.12 55.07 64.28 8.07 20.50 20.35 19.73 7.94 5.69 9.17 5.95 6 8.55 1.30 1.30 1.08 8.43 13.29 13.26 13.23 8.24 54.83 56.88 61.67 8.08 20.76 19.79 17.19 7.96 9.82 8.76 6.84 7 8.57 1.28 1.41 2.40 8.44 12.08 12.63 13.05 8.27 61.50 55.33 60.70 8.08 17.55 19.48 17.43 7.94 5.93 8.92 4.25 8 8.55 1.32 0.90 8.43 11.51 12.47 10.09 8.24 62.99 54.09 63.81 8.05 15.43 22.71 20.91 7.90 8.75 9.83 5.19 9 8.59 1.35 1.63 8.45 11.59 13.67 11.40 8.28 63.60 52.70 63.11 8.06 17.98 24.08 18.57 7.94 2.28 7.05 5.29 10 8.57 1.56 2.50 2.08 8.45 13.22 11.93 12.90 8.28 61.86 55.12 61.87 8.08 17.87 20.99 18.74 7.97 5.50 4.71 4.41 11 8.59 1.43 1.19 8.45 12.25 11.42 9.85 8.28 58.83 59.88 64.13 8.08 18.18 22.06 17.46 7.97 9.61 5.45 6.97 12 8.56 1.64 1.39 0.94 8.39 15.30 13.07 15.71 8.21 63.76 59.71 62.92 8.02 16.72 20.51 16.60 7.97 2.58 4.21 3.85 Results of Block F In this block of formulations, the pH values were all slightly lower than the target value of pH 5.2 (Table F-1). In addition, the pH does change by about 0.1 units for most of the formulations when measured at t1. These differences were considered when constructing mathematical models of the data, as discussed below. The addition of EDTA does appear to improve stability for the worst formulation (Formulation 1). Whether it increases stability in general was less clear, based on the SEC data (Table F-2). The formulations containing high concentrations of Arg or Gly all performed quite well upon storage (Table F-2). The initial purities by RP HPLC were universally lower than expected for these formulations (Table F-3). Upon storage at t1 and t2, there are some slight differences, with Gly- and Arg-based formulations showing the greatest stability. Based upon the RP HPLC data, EDTA does not appear to be a significant stabilizer (Table F-3). Likewise, the effect of Met appears to be minimal on stability as measured by RP HPLC or SEC, with the exception of the monomer content for the highest Met concentration (Table F-2, Formulation 7). Analysis by CE-SDS indicates that very little degradation occurs upon storage (usually less than 1% increase in ‘Other’) (Table F-4). However, there are some formulations that begin with higher ‘Other’ contents (Formulations 4 through 7, for example). These are all formulations using a high concentration of mannitol (240 mM). The same seems to be true for formulations containing 120 mM mannitol. As for analysis by cIEF, there is little change in the relative intensities of the main peak, at least in a systematic fashion that would allow one to discern stability trends (Table F-5). In general, the changes are smaller at t2 than at t1. Block G Formulation Studies The Block G formulation studies examined a variety of formulations with combinations of Gly and Arg as the primary stabilizers (Table XXXIV). In addition, two other surfactants (Pluronic F-68 and polysorbate 20, PS 20) were evaluated in addition to PS 80. Finally, a range of PS 80 concentrations was evaluated. TABLE G BLOCK G STUDY DESIGN Form No. API citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 1 Adalimumab 8 18 0 0 0 0 65 100 0 0 0.1 biosimilar 2 Adalimumab 8 18 0 0 0 0 65 100 0 0.1 0 biosimilar 3 Adalimumab 8 18 0 0 0 0 65 100 0.1 0 0 biosimilar 4 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.1 biosimilar 5 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.05 biosimilar 6 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.01 biosimilar 7 Adalimumab 0 0 0 10 120 120 0 0 0 0.05 0 biosimilar 8 Adalimumab 0 0 0 10 120 120 0 0 0.1 0 0 biosimilar 9 Adalimumab 0 0 10 0 120 120 0 0 0 0 0.05 biosimilar 10 Adalimumab 0 0 20 0 150 100 0 0 0 0.05 0 biosimilar 11 Adalimumab 0 0 0 20 150 100 0 0 0 0 0.01 biosimilar 12 Adalimumab 0 0 0 20 120 120 0 0 0 0.01 0 biosimilar TABLE G-1 Measured pH for Block G formulations at t0, t1 (one week, 40° C.), and t2 (two weeks, 40° C.) Form No. citrate phosphate succinate His Gly Arg mannitol NaCl F68 PS20 PS80 t0 t1 t2 1 8 18 0 0 0 0 65 100 0 0 0.1 5.19 5.38 5.25 2 8 18 0 0 0 0 65 100 0 0.1 0 5.23 5.28 5.24 3 8 18 0 0 0 0 65 100 0.1 0 0 5.22 5.26 5.20 4 0 0 0 10 120 120 0 0 0 0 0.1 5.20 5.33 5.29 5 0 0 0 10 120 120 0 0 0 0 0.05 5.23 5.34 5.29 6 0 0 0 10 120 120 0 0 0 0 0.01 5.19 5.40 5.27 7 0 0 0 10 120 120 0 0 0 0.05 0 5.23 5.39 5.42 8 0 0 0 10 120 120 0 0 0.1 0 0 5.19 5.38 5.41 9 0 0 10 0 120 120 0 0 0 0 0.05 5.19 5.27 5.24 10 0 0 20 0 150 100 0 0 0 0.05 0 5.23 5.28 5.24 11 0 0 0 20 150 100 0 0 0 0 0.01 5.23 5.33 5.27 12 0 0 0 20 120 120 0 0 0 0.01 0 5.22 5.29 5.29 TABLE G-2 Monomer content by SEC for formulations in Block G at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. citrate phosphate succinate His Gly Arg mannitol NaCl F68 PS20 PS80 t0 t1 t2 1 8 18 0 0 0 0 65 100 0 0 0.1 99.17 97.45 98.09 2 8 18 0 0 0 0 65 100 0 0.1 0 99.11 97.78 98.09 3 8 18 0 0 0 0 65 100 0.1 0 0 98.99 97.74 97.92 4 0 0 0 10 120 120 0 0 0 0 0.1 99.12 98.67 98.68 5 0 0 0 10 120 120 0 0 0 0 0.05 99.05 98.57 98.53 6 0 0 0 10 120 120 0 0 0 0 0.01 99.05 98.66 98.70 7 0 0 0 10 120 120 0 0 0 0.05 0 99.04 98.63 98.50 8 0 0 0 10 120 120 0 0 0.1 0 0 99.11 98.64 98.55 9 0 0 10 0 120 120 0 0 0 0 0.05 99.12 98.56 98.98 10 0 0 20 0 150 100 0 0 0 0.05 0 99.10 98.49 98.88 11 0 0 0 20 150 100 0 0 0 0 0.01 99.07 98.76 98.45 12 0 0 0 20 120 120 0 0 0 0.01 0 99.11 98.48 TABLE G-3 Percent purity by RP HPLC for formulations in Block G at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C. Form No. citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 t0 t1 t2 1 8 18 0 0 0 0 65 100 0 0 0.1 99.74 99.66 98.93 2 8 18 0 0 0 0 65 100 0 0.1 0 99.59 99.66 98.97 3 8 18 0 0 0 0 65 100 0.1 0 0 99.58 99.60 99.22 4 0 0 0 10 120 120 0 0 0 0 0.1 99.62 99.62 98.99 5 0 0 0 10 120 120 0 0 0 0 0.05 99.70 99.61 99.01 6 0 0 0 10 120 120 0 0 0 0 0.01 99.60 99.66 99.00 7 0 0 0 10 120 120 0 0 0 0.05 0 99.71 99.65 98.99 8 0 0 0 10 120 120 0 0 0.1 0 0 99.70 99.61 99.03 9 0 0 10 0 120 120 0 0 0 0 0.05 99.71 99.60 99.03 10 0 0 20 0 150 100 0 0 0 0.05 0 99.72 99.60 99.02 11 0 0 0 20 150 100 0 0 0 0 0.01 99.72 99.61 99.05 12 0 0 0 20 120 120 0 0 0 0.01 0 99.61 99.04 TABLE G-4 Percentage of bands for light chain (LC), heavy chain (HC), non- glycosylated HC, and other species for formulations in Block G at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 28.55 70.77 0.50 0.17 t1 29.71 69.42 0.57 0.30 t2 30.32 68.80 0.53 0.35 2 t0 37.14 62.38 0.49 0.00 t1 30.31 69.38 0.28 0.03 t2 31.60 67.87 0.53 0.00 3 t0 28.95 70.40 0.65 0.00 t1 28.17 70.26 0.58 0.99 t2 27.32 71.52 0.56 0.59 4 t0 29.56 69.02 0.65 0.77 t1 32.19 66.09 0.53 1.19 t2 31.58 66.03 0.57 1.81 5 t0 36.54 62.48 0.56 0.42 t1 28.77 69.28 0.62 1.33 t2 23.76 74.49 0.60 1.16 6 t0 29.60 68.61 0.58 1.21 t1 30.37 67.42 0.59 1.61 t2 32.27 66.08 0.59 1.06 7 t0 31.90 65.50 0.63 1.97 t1 31.26 66.66 0.56 1.51 t2 31.37 66.64 0.67 1.31 8 t0 31.04 67.38 0.54 1.04 t1 30.34 67.99 0.62 1.05 t2 30.21 67.63 0.68 1.48 9 t0 33.12 65.34 0.61 0.94 t1 34.01 63.97 0.56 1.46 t2 34.47 63.77 0.57 1.19 10 t0 36.78 61.61 0.54 1.07 t1 39.25 58.66 0.53 1.56 t2 32.83 65.42 0.55 1.21 11 t0 36.37 61.97 0.54 1.11 t1 t2 34.97 63.14 0.54 1.36 12 t0 34.26 64.16 0.52 1.05 t1 t2 34.90 63.35 0.56 1.19 TABLE G-5 Percentage of main bands seen in the cIEF profile of formulations in Block G at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C. Form No. pH t0 t1 t2 1 8.53 1.24 1.21 8.36 14.30 12.69 13.67 8.24 64.03 53.50 60.30 8.14 8.01 15.77 9.32 19.12 7.86 3.73 3.35 4.48 2 8.52 1.06 1.37 0.88 8.35 13.10 13.30 12.53 8.16 66.28 59.68 57.99 7.97 17.14 19.60 21.55 7.83 2.42 4.78 4.92 3 8.51 0.65 0.65 1.03 8.34 13.31 14.00 15.31 8.16 65.13 59.04 60.70 8.14 7.98 17.26 18.90 17.56 7.82 2.89 5.68 4.16 4 8.36 1.87 2.43 1.00 8.19 7.74 10.89 11.69 7.99 61.91 54.27 59.10 7.82 20.94 22.72 19.81 7.66 6.35 7.98 6.92 5 8.44 1.79 0.95 071 8.26 13.33 12.85 10.43 8.06 61.67 59.94 60.12 7.88 17.49 21.08 20.82 7.69 4.02 4.50 6.50 6 8.36 1.71 4.76 8.21 12.37 12.93 10.95 8.04 62.53 54.16 56.48 7.87 19.24 26.08 17.97 7.64 4.15 2.07 6.50 7 8.54 0.77 1.19 0.79 8.34 7.15 12.32 13.15 8.17 54.73 42.64 60.58 8.02 22.18 29.90 17.28 7.83 7.12 11.47 4.77 7.69 1.41 2.48 2.11 8 8.55 1.04 2.11 8.39 7.28 10.69 14.82 8.23 64.01 57.42 55.68 8.05 20.81 23.86 23.76 7.96 6.79 5.37 5.74 9 8.54 8.48 10.99 7.91 8.31 53.85 61.43 8.17 31.58 23.83 7.99 8.82 7.85 3.58 3.27 10 8.50 0.95 2.16 8.36 9.10 10.65 15.79 8.18 59.02 55.35 58.56 8.02 23.76 24.79 25.66 7.87 5.63 7.05 11 8.58 2.08 1.68 8.40 9.74 10.05 9.67 8.21 62.70 56.96 57.36 8.05 21.39 24.14 25.18 7.99 5.24 6.77 6.11 12 8.54 1.67 8.37 15.99 8.22 63.18 8.02 15.41 7.82 3.75 TABLE G-6 Block G study design for F/T and agitation studies Form No. API citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 1 Adalimumab 8 18 0 0 0 0 65 100 0 0 0.1 biolsimilar 2 Adalimumab 8 18 0 0 0 0 65 100 0 0.1 0 biolsimilar 3 Adalimumab 8 18 0 0 0 0 65 100 0.1 0 0 biolsimilar 4 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.1 biolsimilar 5 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.05 biolsimilar 6 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.01 biolsimilar 7 Adalimumab 0 0 0 10 120 120 0 0 0 0.05 0 biolsimilar 8 Adalimumab 0 0 0 10 120 120 0 0 0.1 0 0 biolsimilar 9 Adalimumab 0 0 10 0 120 120 0 0 0 0 0.05 biolsimilar 10 Adalimumab 0 0 20 0 150 100 0 0 0 0.05 0 biolsimilar 11 Adalimumab 0 0 0 20 150 100 0 0 0 0 0.01 biolsimilar 12 Adalimumab 0 0 0 20 120 120 0 0 0 0.01 0 biolsimilar TABLE G-7 Monomer content by SEC for select formulations in Block G that were untreated (Q, quiescent), underwent 5 F/T cycles or subjected to agitation for 24 hours Form No. citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 Q F/T agit 1 8 18 0 0 0 0 65 100 0 0 0.1 99.15 99.03 99.14 4 0 0 0 10 120 120 0 0 0 0 0.1 99.21 99.11 99.18 8 0 0 0 10 120 120 0 0 0.1 0 0 99.18 99.14 99.17 11 0 0 0 20 150 100 0 0 0 0 0.01 99.16 99.09 99.13 12 0 0 0 20 120 120 0 0 0 0.01 0 99.10 TABLE G-8 Percent purity by RP HPLC for select formulations in Block G that were untreated (Q, quiescent), underwent 5 F/T cycles or subjected to agitation for 24 hours Form No. citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 Q F/T agit 1 8 18 0 0 0 0 65 100 0 0 0.1 99.60 99.72 99.76 4 0 0 0 10 120 120 0 0 0 0 0.1 99.56 99.70 99.59 8 0 0 0 10 120 120 0 0 0.1 0 0 99.58 99.57 99.73 11 0 0 0 20 150 100 0 0 0 0 0.01 99.72 99.59 99.65 12 0 0 0 20 120 120 0 0 0 0.01 0 99.75 99.56 Results of Block G All of the pH values were close to the target values (Table G-1), with relatively small changes occurring upon storage. There appears to be some preference in terms of polysorbates over F-68 in terms of stability, as measured by SEC (Table G-2). However, the differences are relatively small. It does appear that succinate formulations (Formulations 9 and 10) fared reasonably well as far as monomer content retained. The RP HPLC data are all very close, making any determination of stability differences virtually impossible (Table G-3). These data will only be interpretable when examined in the larger context of all of the blocks of screening studies. The CE-SDS results suggest that PS 20 is the best stabilizer at 0.1% concentration for the Humira® formulation (Formulations 1 through 3) (Table G-4). Otherwise, the differences appear to be too small and variable to make any general conclusions. As seen before, the results for cIEF data are variable enough to make interpretation difficult (Table G-5). It does appear that the changes are smaller in the Gly/Arg formulations than for formulations using other stabilizers, like mannitol. Still, overall, the stability by cIEF looks to be quite good for many of the formulations in this study. Block G (F/T and Agitation) Studies. For a liquid formulation, it is important to evaluate the sensitivity to interfacial stress. Two kinds of stress studies were selected. The first is agitation at 150 rpm on an orbital shaker for 24 hours at 2-8° C. The second is five successive cycles of freezing and thawing (F/T), where this cycle should generate increasing amounts of damage protein, if the protein is sensitive to interfacial damage. Four formulations from Block G were selected for assessment, and they are highlighted in blue bold text Table G-6. Upon repeated F/T cycling, there is a very small decrease in monomer content for all of the formulations tested (Table G-7). Thus, it seems like there is little interfacial sensitivity form this stress and that the presence of PS 80 is not critical for protection. As for agitated samples, the losses are even smaller. The trends in the RP HPLC data are essentially the same (Table G-8). There are little, if any, losses in purity upon exposure to interfacial stress. Block H Formulation Studies The Block H formulations focused on three aspects of the adalimumab formulation: (1) higher protein concentrations, (2) formulations with no buffers present (other than the protein), and (3) the use of various buffer combinations beside citrate-phosphate (See Table H). TABLE H BLOCK H STUDY DESIGN Form No. API protein citrate phosphate succinate HIS ACETATE Gly Arg mannitol NaCl PS80 1 *** 100 8 18 0 0 0 0 0 65 100 0.1 2 *** 100 0 0 0 10 0 120 120 0 0 0.1 3 *** 50 0 0 0 0 0 0 0 65 100 0.1 4 *** 50 0 0 0 0 0 120 120 0 0 0.1 5 *** 50 0 0 0 0 0 120 120 0 0 0 6 *** 50 0 0 0 10 10 0 0 65 100 0.1 7 *** 50 0 0 10 10 0 0 0 65 100 0.1 8 *** 50 0 10 0 10 0 0 0 65 100 0.1 9 *** 50 0 0 10 0 10 0 0 65 100 0.1 10 *** 50 10 0 10 0 0 0 0 65 100 0.1 11 *** 50 10 0 0 10 0 0 0 65 100 0.1 12 *** 50 0 0 10 10 0 120 100 0 0 0.1 *** denotes proprietary adalimumab biosimilar TABLE H-1 Measured pH for Block H formulations at t0, t1 (one week, 40° C.), and t2 (two weeks, 40° C.) Form No. protein Citrate Phosphate Succinate Histidine acetate Gly Arg Mannitol NaCl PS80 t0 t1 t2 1 100 8 18 0 0 0 0 0 65 100 0.1 5.19 5.30 5.29 2 100 0 0 0 10 0 120 120 0 0 0.1 5.20 5.19 5.15 3 50 0 0 0 0 0 0 0 65 100 0.1 5.21 5.23 5.21 4 50 0 0 0 0 0 120 120 0 0 0.1 5.21 5.41 5.46 5 50 0 0 0 0 0 120 120 0 0 0 5.21 5.30 5.39 6 50 0 0 0 10 10 0 0 65 100 0.1 5.20 5.28 5.28 7 50 0 0 10 10 0 0 0 65 100 0.1 5.21 5.24 5.24 8 50 0 10 0 10 0 0 0 65 100 0.1 5.20 5.17 5.16 9 50 0 0 10 0 10 0 0 65 100 0.1 5.21 5.24 5.29 10 50 10 0 10 0 0 0 0 65 100 0.1 5.20 5.24 5.26 11 50 10 0 0 10 0 0 0 65 100 0.1 5.21 5.24 5.26 12 50 0 0 10 10 0 120 100 0 0 0.1 5.21 5.26 5.29 TABLE H-2 Monomer content by SEC for formulations in Block H at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. protein Citrate Phosphate Succinate Histidine acetate Gly Arg mannitol NaCl PS80 t0 t1 t2 1 100 8 18 0 0 0 0 0 65 100 0.1 99.25 98.36 98.42 2 100 0 0 0 10 0 120 120 0 0 0.1 99.19 98.88 98.47 3 50 0 0 0 0 0 0 0 65 100 0.1 99.06 98.81 98.74 4 50 0 0 0 0 0 120 120 0 0 0.1 99.19 99.06 98.99 5 50 0 0 0 0 0 120 120 0 0 0 99.26 99.03 98.96 6 50 0 0 0 10 10 0 0 65 100 0.1 99.26 98.92 98.86 7 50 0 0 10 10 0 0 0 65 100 0.1 99.14 98.98 98.93 8 50 0 10 0 10 0 0 0 65 100 0.1 99.11 98.93 98.66 9 50 0 0 10 0 10 0 0 65 100 0.1 99.16 98.79 98.63 10 50 10 0 10 0 0 0 0 65 100 0.1 99.10 98.79 98.49 11 50 10 0 0 10 0 0 0 65 100 0.1 99.21 98.93 98.18 12 50 0 0 10 10 0 120 100 0 0 0.1 99.30 99.22 98.65 TABLE H-3 Percent purity by RP HPLC for formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. protein citrate phosphate succinate histidine acetate Gly Arg mannitol NaCl PS80 t0 t1 t2 1 100 8 18 0 0 0 0 0 65 100 0.1 99.36 99.64 99.64 2 100 0 0 0 10 0 120 120 0 0 0.1 99.37 99.68 99.74 3 50 0 0 0 0 0 0 0 65 100 0.1 99.45 99.47 99.70 4 50 0 0 0 0 0 120 120 0 0 0.1 99.50 99.69 99.59 5 50 0 0 0 0 0 120 120 0 0 0 99.47 99.71 99.56 6 50 0 0 0 10 10 0 0 65 100 0.1 99.48 99.56 99.72 7 50 0 0 10 10 0 0 0 65 100 0.1 99.43 99.45 99.72 8 50 0 10 0 10 0 0 0 65 100 0.1 99.43 99.51 99.72 9 50 0 0 10 0 10 0 0 65 100 0.1 99.47 99.55 99.72 10 50 10 0 10 0 0 0 0 65 100 0.1 99.48 99.53 99.67 11 50 10 0 0 10 0 0 0 65 100 0.1 99.45 99.69 99.60 12 50 0 0 10 10 0 120 100 0 0 0.1 99.44 99.54 99.72 TABLE H-4 Percentage of bands for light chain (LC), heavy chain (HC), non- glycosylated HC, and other species for formulations in Block H at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 32.87 65.48 0.54 1.11 t1 28.08 70.09 0.58 1.25 t2 52.57 47.43 0.00 0.00 2 t0 36.20 62.40 0.55 0.86 t1 29.64 68.68 0.57 1.11 t2 43.09 55.23 0.57 1.10 3 t0 34.70 63.55 0.57 1.18 t1 28.24 69.72 0.61 1.57 t2 34.25 63.97 0.67 1.11 4 t0 41.04 57.61 0.51 0.84 t1 27.58 70.65 0.62 1.15 t2 34.14 64.01 0.60 1.26 5 t0 37.64 60.77 0.50 1.09 t1 28.07 70.02 0.61 1.30 t2 37.67 60.76 0.55 1.02 6 t0 31.64 66.46 0.55 1.34 t1 27.67 70.19 0.50 1.64 t2 34.07 63.49 0.62 1.81 7 t0 30.38 69.10 0.53 0.00 t1 27.14 70.55 0.62 1.69 t2 46.41 51.21 0.00 2.38 8 t0 28.46 71.19 0.35 0.00 t1 30.05 68.71 0.55 0.69 t2 34.14 63.97 0.63 1.25 9 t0 27.74 70.63 0.60 1.03 t1 27.48 70.48 0.61 1.43 t2 36.56 61.59 0.49 1.36 10 t0 t1 27.69 70.46 0.60 1.24 t2 11 t0 27.64 70.83 0.57 1.13 t1 31.85 66.08 0.61 1.46 t2 38.58 59.26 0.52 1.64 12 t0 29.48 68.55 0.58 1.40 t1 29.53 68.68 0.58 1.40 t2 30.64 68.20 0.70 0.46 TABLE H-5 Percentage of main bands seen in the cIEF profile of formulations in Block H at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. pH t0 t1 t2 1 8.55 1.20 1.17 1.21 8.39 9.57 5.57 8.23 8.23 46.84 38.18 39.78 7.99 13.67 12.64 11.62 7.81 6.93 4.61 3.70 2 8.43 1.17 1.06 1.38 8.26 8.97 8.15 8.38 8.09 45.46 40.27 39.95 7.87 13.37 16.45 6.77 7.72 5.47 5.39 9.55 7.56 1.64 1.52 3.33 3 8.36 0.80 0.74 0.61 8.16 6.02 6.03 7.30 7.98 35.60 35.58 37.24 7.83 11.75 14.10 13.15 7.64 2.17 4.78 2.00 7.51 1.23 1.81 4 8.40 0.82 0.74 0.30 8.22 7.87 7.38 6.29 8.04 42.46 34.42 35.89 7.89 14.44 13.71 11.34 7.71 3.18 3.31 2.69 7.56 0.98 0.95 5 8.42 0.82 1.02 8.25 7.22 5.09 8.07 34.68 28.99 7.91 2.67 3.63 7.86 10.63 7.83 7.72 2.52 2.05 6 8.42 1.17 1.28 1.22 8.23 9.88 8.56 7.90 8.09 45.26 40.45 40.80 7.94 13.23 16.50 13.28 7 8.59 1.79 1.45 1.90 8.45 11.74 11.32 11.51 8.28 59.90 61.63 56.22 8.05 20.34 19.49 22.98 7.92 6.24 6.11 7.39 8 8.58 1.59 2.94 1.38 8.44 11.86 12.83 12.12 8.26 61.08 60.20 63.05 8.05 20.21 24.03 23.45 7.88 5.25 6.55 9 8.61 1.22 1.42 1.21 8.48 12.47 12.36 11.00 8.33 56.64 54.59 55.34 8.10 23.37 23.81 25.31 7.94 6.30 7.83 Results of Block H The pH stability of these formulations was acceptable (<0.1 units), except for Formulations 4 and 5. These are the buffer-free formulations using Gly and Arg as the stabilizers (Table H-1). There was also a slight rise in pH for Formulation 1 (the Humira® formulation at 100 mg/ml protein concentration). Stability of Block H formulations was monitored using SEC and RP HPLC. There is little loss in monomer content, with Formulation 1 appearing to be the least stable by SEC (Table H-2). At 100 mg/ml of adalimumab biosimilar API the histidine-buffered formulation containing Gly and Arg appears to be quite stable. In general, the best buffer combination appears to be His-succinate (Formulations 7 and 12). Buffer-free formulations with Gly and Arg show acceptable stability as well (Table H-2). The RP HPLC data indicate that the buffer-free formulations (4 and 5) may not do quite as well as shown by SEC (Table H-3), with measurable decreases in purity, but are believed to be satisfactory for obtaining a formulation having long term stability. The CE-SDS data detect the least change in Formulation 12, which is a His-succinate formulation (Table H-4). The largest change at t1 occurs with Formulation 7, which is also a His-succinate formulation, but using mannitol and NaCl as the tonicity modifiers. PLS Modeling PLS Method The data for the adalimumab formulations in Blocks A through H were analyzed together using a chemometric method termed partial least squares (PLS). Detailed descriptions of PLS modeling have been published. See, for example, Katz, M. H. Multivariate Analysis: A Practice Guide for Clinicians. Cambridge University Press, New York, pp. 158-162 (1999); Stahle, L., Wold, K., Multivariate data analysis and experimental design in biomedical research. Prog. Med. Chem. 1988, 25: 291-338; Wold S. PLS-regression: a basic tool of chemometrics. Chemom. Intell. Lab. Syst. 2001, 58: 109-130; and Martens, H.; Martens, M. Multivariate Analysis of Quality: An Introduction, Wiley and Sons, Chichester, UK (2001). For any large matrix of values, where there are a reasonable number of samples (together forming the so-called X-matrix), mathematical models can be constructed that explain the largest amount of variance in the dependent variable(s) of interest (the Y-matrix). The best single description of the relationship between the variation in the X-matrix and the endpoint (the Y matrix) is called the first principal component, PC1. The next important (in terms of describing the variance in the Y-matrix) component is called the second principal component, PC2, and so on. Quite often, only one or two PCs are required to explain most of the variance in the Y-matrix. Each of these PCs contains some contribution from each of the variables in the X-matrix. If a variable within the X-matrix contributes heavily to the construction of a given PC, then it is ranked as being significant. In fact, regression coefficients can be calculated for each variable in the X-matrix for a given model, where a model is the composite of a certain number of PCs in order to provide an adequate description of the Y-matrix. In summary, PLS takes information from the X-matrix, calculates the desired number of PCs, and constructs a suitable model. The model that includes all of the samples is termed a calibration model [1,2]. The overall coefficient of determination (r2) indicates the quality of the model. All PLS calculations were conducted using Unscrambler® software (CAMO, Corvallis, Oreg.). A PLS analysis done with a single variable in the Y-matrix is termed PLS1 analysis. Building a model that fits multiple variables in the Y-matrix is called PLS2 analysis. A full cross validation was performed on all calibration models using standard techniques. Briefly, one sample is removed at a time, the data set is recalibrated, and a new model is constructed. This process is repeated until all of the calibration samples are removed once and quantified as a validation model. Therefore, the first set, containing all samples is referred to as the calibration set and the one after cross-validation as the validation set. The jack-knife algorithm (See, Martens et al) was used to determine statistical significance for any factor used in constructing the PLS models described above. PLS Modeling of Adalimumab Formulations (Blocks B, C and D) See FIGS. 3 Through 12 Note: The PLS surface graphs depicted in FIGS. 3 through 12 are based on the data obtained from Blocks B, C and D. The following is a discussion of the findings reflected in the PLS surface plots shown in FIGS. 3 through 12. PLS Model 1—FIG. 3. FIG. 3 contains a depiction of the monomer content at t1 (model 1) as a function of citrate and phosphate concentrations. The pH has been fixed at 5.2. The model indicated that phosphate and citrate by themselves were weak destabilizers (not to statistical significance), along with tartrate and maleate. By comparison, succinate, which is structurally similar to citrate, tartrate and maleate, was a weak stabilizer. The only buffer found to be a significant stabilizer was histidine. None of these findings could have been predicted based on the literature or examination of the chemical structure of each buffer. The model also indicated that when citrate and phosphate buffer are used together, the formulation is least stable. If one only uses a single buffer, especially phosphate, stability improves. This is surprising, as phosphate has little or no buffer capacity at pH 5.2, while citrate buffer does. None of this behavior could have been predicted based on what was known in the art. PLS Model 2—FIG. 4. FIG. 4 contains a depiction of the monomer content at t2 (model 2). Likewise, a model was constructed using the monomer content by SEC at t2 as the endpoint. This model also demonstrated that the stability is lowest when citrate and phosphate are used together. The lowest stability was shown when citrate is above 10 mM and phosphate is between 5 and 15 mM. Stability improves when the citrate concentration is lowered and/or phosphate concentration is lowered or raised. These findings suggest that a single buffer composition is preferred. The same trend in buffer stabilization is seen as with PLS Model 1, with citrate and phosphate being weak stabilizers (not statistically significant), while histidine is a strong stabilizer (statistically significant). PLS Model 1—FIG. 5. FIG. 5 is a PLS model 1 showing the effect of histidine and glycine on the stability of formulations. It contains a depiction of the monomer content at t1 (model 1). This model indicated that the combination of histidine and glycine yielded very good stability results. Both histidine (His) and glycine (Gly) were determined to be stabilizers. The lowest stability on the response surface (shown in blue) is when there is the lowest concentration of His and Gly. The effect of His on stability is greater, with 20 mM His providing comparable stabilization to 120 mM Gly (note the opposite corners of the graph). The model indicates that there will be an additive benefit to stability by using both excipients, with the highest stability occurring when the His concentration is 20 mM and the Gly concentration is 120 mM. PLS Model 1—FIG. 6. FIG. 6 is a PLS model 1 showing the effect of arginine and sorbitol on the stability of formulations. It contains a depiction of the monomer content at t1 (model 1). This model indicated that arginine was a good stabilizer, while sorbitol was a poor stabilizer. Likewise, arginine (Arg) provides a degree of stabilization that is similar to that found for Gly. The poorest stability as indicated by this model is when the Arg concentration is low and the sorbitol concentration is low (the blue area of the graph). As the concentrations of each excipient are increased, the monomer content at t1 is increased. The effect of sorbitol is roughly linear with concentration, while the effect of Arg appears to be increasing more rapidly once the concentration exceeds 60 mM. Even though sorbitol is predicted to increase the stability of adalimumab in terms of retained monomer content, its ability to increase stability is less than that found for Gly and Arg (on a molar basis). PLS Model 1—FIG. 7. FIG. 7 is a PLS model 1 showing the effect of pH and histidine on the stability of formulations. It contains a depiction of the monomer content at t1 (model 1). This model indicated that histidine appears to be the best buffer, while pH should preferably be at 5 or higher for best stability. PLS Model 2—FIG. 8. FIG. 8 is a PLS model 2 showing the effect of pH and histidine on the stability of formulations. It contains a depiction of the monomer content at t2 (model 2). This model indicated that histidine appears to be the best buffer, while pH should preferably be at 5 or higher for best stability. The results indicate that the optimal pH is near 5.2. Of all of the buffers that were examined, histidine provides the greatest degree of stabilization. This response surface illustrates two important points. First, the stability appears to be maximal near pH 5.2, falling off at a higher and lower pH. Second, histidine is shown to provide a significant increase in stability. When histidine is used at 20 mM, it provides a marked increase in stability over lower buffer concentrations. In fact, the effect appears to be non-linear, with more stabilization occurring from 10 to 20 mM than from 0 to 10 mM. Further, the loss in stability is more abrupt at higher pH than at lower pH. PLS Model 2—FIG. 9. FIG. 9 is a PLS model 2 showing the effect of trehalose and PS80 on the stability of formulations. It contains a depiction of the monomer content at t2. This model indicated that trehalose appears to be a weak stabilizer, while PS80 improves thermal stability. The response surface shown in FIG. 9 indicates that PS 80 is a potent stabilizer for protecting adalimumab against thermal stress, with a concentration of 0.1% providing maximal stability. The concentration of PS 80 has not been varied other than at 0 and 0.1%. By comparison, this model shows that the stabilization effect of trehalose is quite small, certainly less than what was seen with sorbitol. PLS Model 2—FIG. 10. FIG. 10 is a PLS model 2 showing the effect of mannitol and PS80 on the stability of formulations. It contains a depiction of the monomer content at t2 (model 2). This model indicated that mannitol appears to be a destabilizer, while PS80 improves thermal stability. The PLS model using monomer content by SEC at t2 allows one to examine the relative effects of any of the factors included in the model. As the mannitol concentration increases, the overall stability decreases. By comparison, the impact of PS80 on the stability is rather small. PLS Model 1—FIG. 11. FIG. 11 is a PLS model 1 showing the effect of mannitol and NaCl on the stability of formulations. It contains a depiction of the monomer content at t1 (model 1). This model indicated that mannitol and NaCl both appear to be destabilizers. The stability, as indicated by the monomer content at t1, is lowest when the mannitol concentration is anywhere below 150 mM. Likewise, addition of NaCl also diminishes the stability of adalimumab. PLS Model 1—FIG. 12. FIG. 12 is a PLS model 1 showing the effect of EDTA and methionine on the stability of formulations. It contains a depiction of the monomer content at t1. In the case of EDTA, the stability decreases slightly as the concentration of this additive increases. In contrast, addition, of Met appears to improve stability. PLS Modeling of Adalimumab Formulations for Blocks B through G See FIGS. 13 Through 28 The First PLS Model (“PLS Model A) The first PLS model (PLS Model A) used difference in monomer content at t1 as the endpoint. The model employed three PCs and had a correlation coefficient for the calibration set of 0.83 and a r-value of 0.67 for the validation set. It was a quadratic model including pH-buffer and buffer-buffer interaction terms. TABLE J PLS “MODEL A” COEFFICIENTS Factor r-value pH t0 0.041 protein −0.025 citrate +0.123 phos +0.267 succinate −0.089 histidine −0.174 acetate −0.053 glycine −0.190 arginine −0.128 sorbitol −0.003 trehalose +0.020 mannitol −0.104 NaCl +0.250 F68 +0.018 PS 20 +0.021 PS 80 −0.152 EDTA +0.112 Met −0.062 Note: Overall correlation coefficients for each linear factor includes in the first PLS model (PLS Model A) using the difference in monomer content by SEC at t1 as the endpoint. Factors deemed to be statistically significant are highlighted in bold text. The model quality is acceptable, considering the correlation coefficients of the calibration and validation sets. The overall correlation coefficients for the various factors included in the model are summarized in Table J. Note that the quadratic and interaction terms are not listed here. As the endpoint is the difference in monomer content, one wishes to minimize this value. Thus, stabilizers exhibit negative correlation coefficients, while destabilizers have positive r-values. Of the stabilizers, His, Gly, Arg, and PS 80 are the most potent, although mannitol and succinate also have a stabilizing effect (Table J). Meanwhile, there are some significant destabilizers, such as NaCl, citrate, and phosphate. Keep in mind that these models are a composite of all of the stability data gathered across the various blocks of formulations, A through H, and individual formulations could vary from the model. While the table of correlation coefficients is helpful to gauge the effects of various factors, they do not capture the non-linear and interaction effects, so it is helpful to view response surfaces to examine the effects of various parameters in greater detail, as shown in the response surfaces that are reproduced in FIGS. 13 through 28. Discussion of PLS Model A—FIGS. 13 and 14. The Krause '583 patent describes the citrate-phosphate buffer system as being integral to product stability. Our studies show this not to be the case. The poorest stability would occur when these two buffers were used in combination and the effect would get worse as the buffer concentrations increase, according to this model (FIG. 13[1]). The response surface indicates that the phosphate and citrate are equally destabilizing, contrary to some earlier observations, but the quantitative nature of these surfaces must be considered with some care as they include data from all of the formulations from Blocks B through H. The effect of pH and His is shown in FIG. 14. It shows that His is destabilizing at low pH, where it is clearly outside of the buffer capacity of His. Again, this result is a function of all pH observations in this study, not just those involving His (although this could be done). According to this response surface, the optimal pH may be nearer to 5.4 than 5.2, although the surface is relatively flat through this region, indicating a shallow response surface from pH 5 to 5.4 (FIG. 14). Discussion of PLS Model A—FIG. 15 The response surface for Gly and Arg is shown in FIG. 15. The studies repeatedly show that these two amino acids can be potent stabilizers of adalimumab. Note that the minimum difference in monomer content (i.e., the blue part of the surface) is reached at 100 mM Arg, but at 200 mM Gly, suggesting that Arg may be the better stabilizer for adalimumab at pH 5.2. Discussion of PLS Model A—FIG. 16 The final response surface shown for PLS Model A is for the effect of NaCl and PS 80 (FIG. 16). It shows that the stability of adalimumab decreases upon addition of NaCl, especially above 100 mM. Meanwhile, PS 20 provides significant stability when used above 0.04%. The Second PLS Model (PLS Model B) The second PLS model (PLS Model B) used the monomer content at t1 and at t2 as the endpoints. The model employed four PCs and had a correlation coefficient for the calibration set of 0.82 and a r-value of 0.67 for the validation set. It was a quadratic model including pH-buffer and buffer-buffer interaction terms. In terms of model quality, this is comparable to the first PLS Model A described above. TABLE K (L) PLS “MODEL B” CORRELATION COEFFICIENTS Factor r-value pH −0.086 protein +0.030 citrate −0.079 phos −0.157 succinate +0.060 histidine +0.185 acetate +0.063 glycine +0.126 arginine +0.150 sorbitol +0.025 trehalose +0.006 mannitol +0.014 NaCl −0.215 F68 −0.044 PS 20 −0.028 PS 80 +0.227 EDTA −0.097 Met +0.096 The endpoints for PLS Model B are the total monomer contents at both t1 and t2. Therefore, one will wish to maximize these values. This means that stabilizers with have positive correlation coefficients and destabilizers will display negative r-values (Table K). As with the previous model, citrate, phosphate, and NaCl are significant destabilizers. On the other hand, His, Gly Arg, and PS 20 are potent stabilizers. In this model, trehalose, sorbitol and mannitol have very little effect. The primary differences are that pH is now a significant factor and that EDTA is a significant destabilizer, while Met appears to be a stabilizer as well. Discussion of PLS Model B—FIG. 17 This model suggests that addition of citrate has little effect on stability if phosphate is absent (view the back edge of the response surface of FIG. 5). On the other hand, added phosphate does decrease monomer content (view the right hand edge) and the combination is even more destabilizing (FIG. 5). Thus, the citrate-phosphate buffer combination is not effective at stabilizing adalimumab, contrary to what is taught by the '583 patent. The destabilizing effect of phosphate is about three-fold greater than for citrate according to this model. Discussion of PLS Model B—FIG. 18 The use of His at low pH has little or detrimental effects (FIG. 18[6\\). However, when employed at pH 5.2 or above, the His provides a significant increase in stability (as measured by monomer content by SEC). Discussion of PLS Model B—FIG. 19 The response surface for Gly and Arg is shown in FIG. 19. Including both stabilizers at high concentrations would be beneficial for stability, but impractical for tonicity reasons. It does appear that Arg is the more potent stabilizer in this model compared to Gly, where a 75 mM concentration of Arg has the same effect as ˜120 mM Gly. The model indicates either one alone would work well, or that a combination would be effective as well. Discussion of PLS Model B—FIG. 20 The PLS model B shows a modest effect of mannitol on stability, whereas PS 80 is an effective stabilizer above concentrations near 0.05% (FIG. 20). Thus, one could conclude from this data that a stable formulation could be comprised of 240 mM mannitol and 0.1% PS 80 at pH 5.2. Discussion of PLS Model B—FIG. 21 Throughout the project, it appears that NaCl is a destabilizer of adalimumab, especially when the concentration reach 100 mM or above, as shown in this response surface (FIG. 21). While only a few formulations were tested that included EDTA, it appears that this excipient is destabilizing, unless the concentration were ˜0.1%. We also note that the effect of Met was favorable with respect to stability, but it did not prove to be a significant effect, probably because relatively few examples were evaluated. Discussion of PLS Model B—FIG. 22 The final response surface from the PLS Model B to be considered is the effect of succinate and His (FIG. 22). The model did include all relevant buffer-buffer interactions. This surface shows that succinate has little or even deleterious effects on its own (see the front edge of the plot). However, in conjunction with His it proves to increase the overall stability (e.g., note that back edge of the surface). Therefore, a His-succinate buffer system appear to be the most favorable of all of the buffer combinations tested to date. The Third PLS Model (PLS Model C) The third PLS model C used the difference in percent purity by RP HPLC at t1 as the endpoint. The model employed two PCs and had a correlation coefficient for the calibration set of 0.86 and a r-value of 0.67 for the validation set. It was a quadratic model including pH-buffer and buffer-buffer interaction terms. In terms of model quality, this is very similar to the previous model. TABLE L PLS “MODEL C” CORRELATION COEFFICIENTS Factor r-value pH −0.115 protein −0.139 citrate +0.014 phosphate +0.084 succinate −0.051 histidine −0.075 acetate +0.159 glycine −0.096 arginine −0.045 sorbitol +0.029 trehalose +0.020 mannitol −0.060 NaCl +0.068 F68 −0.047 PS 20 −0.067 PS 80 −0.028 EDTA +0.099 Met −0.015 PLS Model C demonstrates that RP HPLC is stability-indicating, even though the sensitivity may be less than for SEC. The model finds that both phosphate and citrate are destabilizing, with the effect of phosphate being statistically significant (Table LI). Likewise, acetate is a strong destabilizer as is EDTA. Both Gly and Arg are shown to be stabilizers, but the effects are not deemed to be statistically significant. Only His was found to be a significant stabilizer (along with protein concentration). Discussion of PLS Model C—FIG. 23 The response surface for citrate and phosphate at pH 5.2 is shown in FIG. 23[11]. Both buffers are destabilizing (follow the front and left-hand edges of the plot). Above concentrations of ˜10 mM, the combination becomes quite destabilizing. Overall, phosphate is predicted to be more destabilizing according to this model (FIG. 11). Discussion of PLS Model C—FIG. 24 As seen in previous models, the stability of adalimumab decreases as the pH is reduced to less than 5.0 (FIG. 12). In this model the stabilizing effect of His is seen across all pH values, but is most pronounced when the pH is lower. Discussion of PLS Model C—FIG. 25 The effects of Gly and Arg are seen in FIG. 25. Both excipients decrease loss of purity as the concentration increases and they are predicted to be roughly equipotent, as judged by the slopes along the edges of the response surface. Otherwise, it appears that it takes less Arg (75 mM) to achieve optimal loss of purity (the blue region of the graph) than for Gly (˜200 mM). Discussion of PLS Model C—FIG. 26 The effect of mannitol and PS 80 is seen in the response surface in FIG. 26[14]. It is clear that chemical stability is greatly improved by adding PS 80, especially at concentrations above 0.04%. Meanwhile, mannitol is also stabilizing, but even 240 mM mannitol has less effect than a small about of the surfactant. Discussion of PLS Model C—FIG. 27 While mannitol is believed to be a stabilizer in the Humira® formulation, NaCl is clearly a destabilizer, both in this model (See FIG. 27[15]), and in previous PLS models. The effect is substantial when the NaCl concentration exceeds 75 mM or so. Discussion of PLS Model C—FIG. 28 The final response surface from PLS Model C is seen in FIG. 28[16] describing the effects of pH and protein concentration. As seen before, the stability is best when the pH is above 4.8 or 5.0. As for the protein effect, this model predicts that the stability, based on RP HPLC, is better at higher protein concentrations. A similar trend, albeit a fairly weak one, was seen for the SEC data (monomer content at t1 and t2). Therefore, it may be possible to achieve similar stability profiles at concentrations at 100 mg/ml as one could obtain at 50 mg/ml. Summary of Findings for Blocks A Through H The formulation studies in Blocks A through H evaluated adalimumab formulations stored at elevated temperature and held for either one week at 40° C. or for two weeks at 25° C. The stability was monitored using SEC, RP HPLC, cIEF and CE-SDS. The optimal pH appears to be 5.2±0.2. Of all of the buffer compositions tested, the citrate-phosphate combination is inferior to nearly any other buffer system evaluated, hence an important aspect of the present invention is the avoidance of this combined buffer system altogether. The best single buffer appears to be His, while a His-succinate buffer also offers very good stability. Even buffer-free systems, which rely on the ability of the protein to buffer the formulation, appear to have acceptable stability profiles under accelerated stress conditions. Of all of the stabilizers/tonicity modifiers evaluated, both Arg and Gly elicit very good stabilization of adalimumab. They both work better than mannitol. Mannitol does appear to be a stabilizer, however we have discovered that if used it should be at the highest possible concentrations, but in any event exceeding about 150 mM, ad most preferably at or exceeding about 200 mM. By comparison, NaCl is clearly a destabilizer, especially when the concentrations exceed 75-100 mM; hence, NaCl, if present should be controlled to levels below about 75 mM. Other polyols, such as sorbitol and trehalose, appear to work about as well as mannitol and therefore may be substituted for mannitol if desired. Surprisingly, polysorbate 80 (PS 80) provides significant protection against thermal stress. While the mechanism of stabilization is not known, it appears that other surfactants tested (PS 20 and F-68), do not appear to be nearly as effective as PS 80. Hence the selection of PS80 versus PS 20 is a preferred feature of the present invention. Formulations according to the present invention preferably contain at least 0.04% (w/v) PS 80. Based on the findings in the formulation studies of Blocks A through H, the following are particularly preferred adalimumab formulations according to the present invention. TABLE M SELECTED FORMULATIONS NaCl PS 80 Form No pH His (mM) succinate (mM) Gly (mM) Arg (mM) mannitol (mM) (mM) (wt %) A 5.2 30 0 240 0 0 0 0.1 B 5.2 30 0 240 0 0 0 0.02 C 5.2 30 0 0 0 240 0 0.1 D 5.2 30 15 0 0 220 0 0.1 E 5.2 30 0 90 0 150 0 0.1 F 5.2 30 0 240 0 0 0 0 G 5.2 20 0 0 0 240 0 0 H 5.4 30 0 240 0 0 0 0.02 I 5.2 30 0 120 80 0 0 0.1 J 5.2 30 15 90 80 0 0 0.1 K 5.2 30 0 0 0 240 0 0.1 L 5.2 30 0 0 50 160 0 0.1 M 5.2 30 0 90 100 0 0 0.1 N 5.2 20 0 120 90 0 0 0.1 O 5.4 30 0 120 80 0 0 0.1 P 5.2 30 0 120 0 0 50 0.01 Q 5.2 30 0 0 0 240 0 0.02 Additional Components of the Provided Pharmaceutical Compositions The formulations of the invention may also include other buffers (unless they are specifically excluded in the description of the specific embodiments of the invention), tonicity modifiers, excipients, pharmaceutically acceptable carriers and other commonly used inactive ingredients of the pharmaceutical compositions. A tonicity modifier is a molecule that contributes to the osmolality of a solution. The osmolality of a pharmaceutical composition is preferably adjusted to maximize the active ingredient's stability and/or to minimize discomfort to the patient upon administration. It is generally preferred that a pharmaceutical composition be isotonic with serum, i.e., having the same or similar osmolality, which is achieved by addition of a tonicity modifier. In a preferred embodiment, the osmolality of the provided formulations is from about 180 to about 420 mOsM. However, it is to be understood that the osmolality can be either higher or lower as specific conditions require. Examples of tonicity modifiers suitable for modifying osmolality include, but are not limited to amino acids (not including arginine) (e.g., cysteine, histidine and glycine), salts (e.g., sodium chloride or potassium chloride) and/or sugars/polyols (e.g., sucrose, sorbitol, maltose, and lactose). In a preferred embodiment, the concentration of the tonicity modifier in the formulation is preferably between about 1 mM to about 1 M, more preferably about 10 mM to about 200 mM. Tonicity modifiers are well known in the art and are manufactured by known methods and available from commercial suppliers. Suitable tonicity modifiers may be present in the compositions of the invention unless they are specifically excluded in the description of the specific embodiments of the invention. Excipients, also referred to as chemical additives, co-solutes, or co-solvents, that stabilize the polypeptide while in solution (also in dried or frozen forms) can also be added to a pharmaceutical composition. Excipients are well known in the art and are manufactured by known methods and available from commercial suppliers. Examples of suitable excipients include but are not limited to sugars/polyols such as: sucrose, lactose, glycerol, xylitol, sorbitol, mannitol, maltose, inositol, trehalose, glucose; polymers such as: serum albumin (bovine serum albumin (BSA), human SA or recombinant HA), dextran, PVA, hydroxypropyl methylcellulose (HPMC), polyethyleneimine, gelatin, polyvinylpyrrolidone (PVP), hydroxyethylcellulose (HEC); non-aqueous solvents such as: polyhydric alcohols, (e.g., PEG, ethylene glycol and glycerol) dimethysulfoxide (DMSO) and dimethylformamide (DMF); amino acids such as: proline, L-serine, sodium glutamic acid, alanine, glycine, lysine hydrochloride, sarcosine and gamma-aminobutyric acid; surfactants such as: Tween®-80 (polysorbate 80), Tween®-20 (polysorbate 20), SDS, polysorbates, poloxamers; and miscellaneous excipients such as: potassium phosphate, sodium acetate, ammonium sulfate, magnesium sulfate, sodium sulfate, trimethylamine N-oxide, betaine, CHAPS, monolaurate, 2-O-beta-mannoglycerate or any combination of the above. Suitable excipients may be present in the compositions of the invention unless they are specifically excluded in the description of the specific embodiments of the invention. The concentration of one or more excipients in a formulation of the invention is/are preferably between about 0.001 to 5 weight percent, more preferably about 0.1 to 2 weight percent. Methods of Treatment In another embodiment, the invention provides a method of treating a mammal comprising administering a therapeutically effective amount of the pharmaceutical compositions of the invention to a mammal, wherein the mammal has a disease or disorder that can be beneficially treated with adalimumab. In a preferred embodiment, the mammal is a human. Diseases or disorders that can be treated with the provided compositions include but are not limited to rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Wegener's disease (granulomatosis), Crohn's disease (or inflammatory bowel disease), chronic obstructive pulmonary disease (COPD), Hepatitis C, endometriosis, asthma, cachexia, psoriasis, and atopic dermatitis. Additional diseases or disorders that can be treated with the compositions of the present invention include those described in U.S. Pat. Nos. 6,090,382 and 8,216,583 the relevant portions of which are incorporated herein by reference. The provided pharmaceutical compositions may be administered to a subject in need of treatment by injection systemically, such as by intravenous injection; or by injection or application to the relevant site, such as by direct injection, or direct application to the site when the site is exposed in surgery; or by topical application. In one embodiment, the invention provides a method of treatment and/or prevention of rheumatoid arthritis comprises administering to a mammal in need thereof a therapeutically effective amount of one of the provided adalimumab compositions. The therapeutically effective amount of the adalimumab in the provided compositions will depend on the condition to be treated, the severity of the condition, prior therapy, and the patient's clinical history and response to the therapeutic agent. The proper dose can be adjusted according to the judgment of the attending physician such that it can be administered to the patient one time or over a series of administrations. In one embodiment, the effective adalimumab amount per adult dose is from about 1-500 mg/m2, or from about 1-200 mg/m2, or from about 1-40 mg/m2 or about 5-25 mg/m2. Alternatively, a flat dose may be administered, whose amount may range from 2-500 mg/dose, 2-100 mg/dose or from about 10-80 mg/dose. If the dose is to be administered more than one time per week, an exemplary dose range is the same as the foregoing described dose ranges or lower and preferably administered two or more times per week at a per dose range of 25-100 mg/dose. In another embodiment, an acceptable dose for administration by injection contains 80-100 mg/dose, or alternatively, containing 80 mg per dose. The dose can be administered weekly, biweekly, or separated by several weeks (for example 2 to 8). In one embodiment, adalimumab is administered at 40 mg by a single subcutaneous (SC) injection. In some instances, an improvement in a patient's condition will be obtained by administering a dose of up to about 100 mg of the pharmaceutical composition one to three times per week over a period of at least three weeks. Treatment for longer periods may be necessary to induce the desired degree of improvement. For incurable chronic conditions the regimen may be continued indefinitely. For pediatric patients (ages 4-17), a suitable regimen may involve administering a dose of 0.4 mg/kg to 5 mg/kg of adalimumab, one or more times per week. In another embodiment, the pharmaceutical formulations of the invention may be prepared in a bulk formulation, and as such, the components of the pharmaceutical composition are adjusted to be higher than would be required for administration and diluted appropriately prior to administration. The pharmaceutical compositions can be administered as a sole therapeutic or in combination with additional therapies as needed. Thus, in one embodiment, the provided methods of treatment and/or prevention are used in combination with administering a therapeutically effective amount of another active agent. The other active agent may be administered before, during, or after administering the pharmaceutical compositions of the present invention. Another active agent may be administered either as a part of the provided compositions, or alternatively, as a separate formulation. Administration of the provided pharmaceutical compositions can be achieved in various ways, including parenteral, oral, buccal, nasal, rectal, intraperitoneal, intradermal, transdermal, subcutaneous, intravenous, intra-arterial, intracardiac, intraventricular, intracranial, intratracheal, intrathecal administration, intramuscular injection, intravitreous injection, and topical application. The pharmaceutical compositions of this invention are particularly useful for parenteral administration, i.e., subcutaneously, intramuscularly, intravenously, intraperitoneal, intracerebrospinal, intra-articular, intrasynovial, and/or intrathecal. Parenteral administration can be by bolus injection or continuous infusion. Pharmaceutical compositions for injection may be presented in unit dosage form, e.g., in ampoules or in multi-dose containers, with an added preservative. In addition, a number of recent drug delivery approaches have been developed and the pharmaceutical compositions of the present invention are suitable for administration using these new methods, e.g., Inject-Ease®, Genject®, injector pens such as GenPen®, and needleless devices such as MediJector® and BioJector®. The present pharmaceutical composition can also be adapted for yet to be discovered administration methods. See also Langer, 1990, Science, 249:1527-1533. The provided pharmaceutical compositions can also be formulated as a depot preparation. Such long acting formulations may be administered by implantation (for example subcutaneously or intramuscularly) or by intramuscular injection. Thus, for example, the formulations may be modified with suitable polymeric or hydrophobic materials (for example as an emulsion in an acceptable oil) or ion exchange resins, or as sparingly soluble derivatives, for example, as a sparingly soluble salt. The pharmaceutical compositions may, if desired, be presented in a vial, pack or dispenser device which may contain one or more unit dosage forms containing the active ingredient. In one embodiment the dispenser device can comprise a syringe having a single dose of the liquid formulation ready for injection. The syringe can be accompanied by instructions for administration. In another embodiment, the present invention is directed to a kit or container, which contains an aqueous pharmaceutical composition of the invention. The concentration of the polypeptide in the aqueous pharmaceutical composition can vary over a wide range, but is generally within the range of from about 0.05 to about 20,000 micrograms per milliliter (μg/ml) of aqueous formulation. The kit can also be accompanied by instructions for use. In addition to the formulations referenced in the formulation studies of Blocks A through H, the following additional examples are provided as further embodiments of the invention, as are the representative embodiments which are included in Appendices A through C which are to be understood as part of this specification. Example 1 Stabilized Adalimumab Formulation (Simile Buffer) Containing Polyol; without Surfactant A stable aqueous pharmaceutical composition containing adalimumab, using a single buffer, and substantially free of a surfactant may be prepared as follows: Each solid formulation component may be weighed to the amount required for a given volume of formulation buffer. These components may then be combined into a beaker or vessel capable of carrying and measuring the given volume of formulation buffer. A volume of deionized water equal to approximately ¾ of the target given formulation buffer may be added to the beaker, and the components may be solubilized through use of a magnetic stir bar. The pH of the buffer may be adjusted to the target formulation pH using 1 molar sodium hydroxide and/or 1 molar hydrogen chloride. The final formulation buffer volume may then be raised to the target volume through the addition of deionized water. The solution may then be mixed with a magnetic stir bar after final water addition. Adalimumab solution may then be placed in dialysis material housing (such as Thermo Scientific Slide-A-Lyzer MINI Dialysis Unit 10,000 MWCO), which may then be placed in contact with the desired formulation buffer for 12 hours at 4° C. Formulation buffer volume to protein solution volume ratio should be no less than 1000:1. The dialysis housing and protein solution it contains may then be placed in a second, equal volume of formulation buffer for an additional 12 hours at 4° C. Resulting adalimumab solution may then be removed from the dialysis material housing, and the concentration of adalimumab may then be determined using ultraviolet spectroscopy. Adalimumab concentration may then be adjusted to the desired level using centrifugation (such as Amicon Ultra 10,000 MWCO Centrifugal Concentrators) and/or dilution with formulation buffer. A sample composition of the invention is represented in Table 1 below: TABLE 1 Ingredient concentration Adalimumab (active ingredient) 50 mg/ml Mannitol (inactive ingredient) 4% Citrate (pH 5.2) (single buffer) 15 mM The composition disclosed in Table 1 does not contain a combination of citrate and phosphate buffer. It also does not require the presence of a surfactant. Example 2 Stabilized Adalimumab Formulation (Single Buffer) without Polyol or Surfactant Ingredient concentration Adalimumab (active ingredient) 50 mg/ml Citrate (pH 5.2) 15 mM Glycine (inactive ingredient) 100 mM Example 3 Stabilized Adalimumab Formulation (Single Buffer) Containing Polyol without Surfactant Ingredient concentration Adalimumab (active ingredient) 50 mg/ml Mannitol (inactive ingredient) 4% Citrate (pH 5.2) 15 mM The compositions of examples 2 and 3 have long term stability and do not contain a combination of citrate and phosphate buffer, and do not require the presence of a surfactant. Example 4 Stabilized Adalimumab Formulation (Simile Buffer) Containing Surfactant; without Polyol 4A Ingredient concentration Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Histidine Buffer (pH 5.2) (sole buffer) 20 mM Glycine (stabilizer) 50 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) 4B Ingredient concentration Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Histidine Buffer (pH 5.2) (sole buffer) 20 mM Glycine (stabilizer) 120 mM Arginine (stabilizer) 100 mM Polysorbate 80 0.1 (wt %) (w/v) 4C Ingredient concentration Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Histidine Buffer (pH 5.2) (sole buffer) 10 mM Glycine (stabilizer) 50 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) 4D Ingredient concentration Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Succinate Buffer (pH 5.2) (sole buffer) 20 mM Glycine (stabilizer) 50 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) 4E Ingredient concentration Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Succinate Buffer (pH 5.2) (sole buffer) 20 mM Glycine (stabilizer) 120 mM Arginine (stabilizer) 100 mM Polysorbate 80 0.1 (wt %) (w/v) 4F Ingredient concentration Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Succinate Buffer (pH 5.2) (sole buffer) 10 mM Glycine (stabilizer) 50 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) The compositions disclosed in Examples 4(a) through 4(f) above will afford stability without need for polyol and without need for a combined buffer system. Insofar as the present invention has discovered that the citrate/phosphate buffer combination required in U.S. Pat. No. 8,216,583 is not required for stabilization of adalimumab formulations according to the present invention, persons skilled in the art may appreciate, in practicing examples 4(a) through 4(f), that additional buffers may be employed in combination with the histidine and succinate buffers disclosed herein (e.g, acetate, citrate, maleate, tartrate, and phosphate buffers); provided the formulation does not use a buffer combination of citrate and phosphate. Example 5 Stabilized Adalimumab Formulation (Simile Buffer) Containing Surfactant; and Polyol 5A Ingredient Concentration Adalimumab (active ingredient) 50 mg/ml Sorbitol 65 mM Histidine Buffer (pH 5.2) (sole buffer) 20 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) 5B Ingredient Concentration Adalimumab (active ingredient) 50 mg/ml Sorbitol 65 mM Succinate Buffer (pH 5.2) (sole buffer) 20 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) The foregoing description of the exemplary embodiments of the invention in the block studies A through H, in the examples above, and in the Appendices A through C, are presented only for the purposes of illustration and description and is not intended to be exhaustive or to limit the invention to the precise forms disclosed. Many modifications and variations are possible in light of the above teaching. Other embodiments of the invention will be apparent to those skilled in the art from consideration of the specification and practice of the invention disclosed herein. It is intended that the specification and examples be considered as exemplary only, with a true scope and spirit of the invention being indicated by the following claims. Appendix A Further Representative Embodiments Disclosed in Priority Application U.S. Ser. No. 61/698,138 A. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 5 to about 6, and wherein said buffer does not comprise both of citrate and phosphate. B. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a surfactant, wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a buffer. C. The composition of any of embodiments A-B, wherein said adalimumab is at a concentration from about 20 to about 150 mg/ml. D. The composition of any of embodiments A-C, wherein said adalimumab is at a concentration from about 20 to about 100 mg/ml. E. The composition of any of embodiments A-D, wherein said adalimumab is at a concentration from about 30 to about 50 mg/ml. F. The composition of any of embodiments A-E, wherein said buffer is at a concentration from about 5 mM to about 50 mM. G. The composition of any of embodiments A-F, wherein said buffer is at a concentration from about 5 mM to about 20 mM. H. The composition of any of embodiments A-G, wherein said buffer is at a concentration from about 10 mM to about 20 mM. I. The composition of any of embodiments A-G, wherein said surfactant is a polysorbate. J. The composition of embodiment I, wherein said polysorbate is polysorbate 80. K. The composition of any of embodiments A-J, wherein said polyol is a sugar alcohol. L. The composition of embodiment K, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. M. The composition of embodiment L, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. N. The composition of any of embodiments L-M, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. O. The composition of any of embodiments L-N, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. P. The composition of any of embodiments A-O further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. Q. The composition of embodiment P, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. R. The composition of embodiment P, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. S. The composition of embodiment P, wherein said metal ion is selected from zinc, magnesium and calcium. T. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, mannitol at a concentration from about 1 to 10% weight by volume, polysorbate 80 at a concentration from about 1 to 50 μM, and citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of phosphate. U. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a surfactant. V. The composition of embodiment U, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. W. The composition of any of embodiments U-V, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. X. The composition of any of embodiments U-V, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. Y. The composition of any of embodiments U-Y, wherein said buffer is at a concentration from about 5 mM and about 50 mM. Z. The composition of any of embodiments U-Y, wherein said buffer is at a concentration from about 5 mM and about 20 mM. AA. The composition of any of embodiments U-Z, wherein said buffer is at a concentration from about 10 mM and about 20 mM. BB. The composition of any of embodiments U-AA, wherein said polyol is a sugar alcohol. CC. The composition of embodiment BB, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. DD. The composition of embodiment CC, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. EE. The composition of any of embodiments CC-DD, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. FF. The composition of any of embodiments CC-EE, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. GG. The composition of any of embodiments CC-FF further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. HH. The composition of embodiment GG, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. II. The composition of embodiment GG, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. JJ. The composition of embodiment GG, wherein said metal ion is selected from zinc, magnesium and calcium. KK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, mannitol at a concentration from about 1 to 10% weight by volume, and citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a surfactant. LL. A stable aqueous pharmaceutical composition comprising adalimumab, a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion, and wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a polyol. MM. The composition of embodiment LL, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. NN. The composition of any of embodiments LL-MM, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. OO. The composition of any of embodiments LL-NN, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. PP. The composition of any of embodiments LL-00, wherein said buffer is at a concentration from about 5 mM and about 50 mM. QQ. The composition of any of embodiments LL-PP, wherein said buffer is at a concentration from about 5 mM and about 20 mM. RR. The composition of any of embodiments LL-QQ, wherein said buffer is at a concentration from about 10 mM and about 20 mM. SS. The composition of embodiment LL, wherein said stabilizer is selected from the group consisting of an amino acid, a salt, EDTA and a metal ion. TT. The composition of embodiment SS, wherein said amino acid is selected from the group consisting of glycine, alanine and arginine. UU. The composition of embodiment SS wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. VV. The composition of embodiment TT, wherein said glycine is at a concentration from about 20 to about 200 mM. WW. The composition of embodiment W, wherein said glycine is at a concentration from about 50 to about 200 mM. XX. The composition of embodiment SS, wherein said arginine is at a concentration from about 1 to about 250 mM. YY. The composition of embodiment XX, wherein said arginine is at a concentration from about 20 to about 200 mM. ZZ. The composition of embodiment YY, wherein said arginine is at a concentration from about 20 to about 100 mM. AAA. The composition of embodiment UU, wherein said sodium chloride is at a concentration from about 5 to about 150 mM. BBB. The composition of embodiment AAA, wherein said sodium chloride is at a concentration from about 20 to about 140 mM. CCC. The composition of embodiment BBB, wherein said sodium chloride is at a concentration from about 75 to about 125 mM. DDD. The composition of embodiment UU, wherein said sodium sulfate is at a concentration from about 5 to about 150 mM. EEE. The composition of embodiment UU, wherein said sodium chloride is at a concentration from about 20 to about 120 mM. FFF. The composition of embodiment EEE, wherein said sodium chloride is at a concentration from about 60 to about 100 mM. GGG. The composition of any of embodiments LL-FF further comprising a surfactant. HHH. The composition of embodiment GGG, wherein said surfactant is a polysorbate. III. The composition of embodiment HHH, wherein said polysorbate is polysorbate 80. JJJ. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, glycine at a concentration from about 20 to about 200 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. KKK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, arginine at a concentration from about 1 to about 250 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH from about 5 to about 5.5, and wherein said composition is substantially free of a polyol. LLL. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. MMM. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, polysorbate 80 at a concentration from about 1 to 50 μM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. NNN. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion, and a buffer selected from the group consisting of citrate, phosphate, succinate, tartrate and maleate, wherein said composition has a pH from about 5 to about 6. OOO. The composition of embodiment NNN, wherein the buffer does not comprise a combination of citrate and phosphate. PPP. The composition of embodiment NNN, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. QQQ. The composition of any of embodiments NNN-PPP, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. RRR. The composition of any of embodiments NNN-QQQ, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. SSS. The composition of any of embodiments NNN-RRR, wherein said buffer is at a concentration from about 5 mM and about 50 mM. TTT. The composition of any of embodiments NNN-SSS, wherein said buffer is at a concentration from about 5 mM and about 20 mM. UUU. The composition of any of embodiments NNN-TTT, wherein said buffer is at a concentration from about 10 mM and about 20 mM. VVV. The composition of any of embodiments NNN-UUU, wherein said surfactant is a polysorbate. WWW. The composition of embodiment VVV, wherein said polysorbate is polysorbate 80. XXX. The composition of any of embodiments NNN-WWW, wherein said polyol is a sugar alcohol. YYY. The composition of embodiment XXX, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. ZZZ. The composition of embodiment XXX, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. AAAA. The composition of any of embodiments XXX-ZZZ, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. BBBB. The composition of any of embodiments YYY-AAAA, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. CCCC. The composition of any of embodiments NNN-BBBB, wherein said stabilizer is EDTA. DDDD. The composition of embodiment CCCC, wherein said EDTA is at a concentration from about 0.01% to about 0.5%. EEEE. The composition of embodiment DDDD, wherein said EDTA is at a concentration from about 0.05% to about 0.25%. FFFF. The composition of embodiment EEEE, wherein said EDTA is at a concentration from about 0.08% to about 0.2%. GGGG. The composition of any of embodiments NNN-BBBB, wherein said stabilizer is methionine. HHHH. The composition of embodiment GGGG, wherein said methionine is at a concentration from about 1 to about 10 mg/ml. IIII. The composition of embodiment GGGG, wherein said methionine is at a concentration from about 1 to about 5 mg/ml. JJJJ. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol at a concentration from about 1 to 10% weight by volume, EDTA at a concentration from about 0.01% to about 0.5%, citrate at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. KKKK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol at a concentration from about 1 to 10% weight by volume, methionine at a concentration from about 1 to about 10 mg/ml, citrate at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. LLLL. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, tartrate and maleate, wherein said composition has a pH of about 3.5. MMMM. The composition of embodiment LLLL, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. NNNN. The composition of any of embodiments LLLL-MMMM, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. OOOO. The composition of any of embodiments LLLL-NNNN, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. PPPP. The composition of any of embodiments LLLL-0000, wherein said buffer is at a concentration from about 5 mM and about 50 mM. QQQQ. The composition of any of embodiments LLLL-PPPP, wherein said buffer is at a concentration from about 5 mM and about 20 mM. RRRR. The composition of any of embodiments LLLL-QQQQ, wherein said buffer is at a concentration from about 10 mM and about 20 mM. SSSS. The composition of any of embodiments LLLL-RRRR, wherein said polyol is a sugar alcohol. TTTT. The composition of embodiment SSSS, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. UUUU. The composition of embodiment TTTT, wherein said mannitol is at a concentration from about 1 to about 10% weight by volume of the total composition. VVVV. The composition of any of embodiments TTTT-UUUU, wherein said mannitol is at a concentration from about 2 to about 6% weight by volume of the total composition. WWWW. The composition of any of embodiments TTTT-VVVV, wherein said mannitol is at a concentration from about 3 to about 5% weight by volume of the total composition. XXXX. The composition of any of embodiments LLLL-WWWW further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. YYYY. The composition of embodiment XXXX, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. ZZZZ. The composition of embodiment XXXX, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. AAAAA. The composition of embodiment XXXX, wherein said metal ion is selected from zinc, magnesium and calcium. BBBBB. The composition of any of embodiments TTTT-AAAAA further comprising a surfactant. CCCCC. The composition of embodiment BBBBB, wherein said surfactant is a polysorbate. DDDDD. The composition of embodiment CCCCC, wherein said polysorbate is polysorbate 80. Appendix B Further Representative Embodiments Disclosed in Priority Application U.S. Ser. No. 61/770,421 A. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 5 to about 6, and wherein said buffer does not comprise both of citrate and phosphate. B. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a surfactant, wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a buffer. C. The composition of any of embodiments A-B, wherein said adalimumab is at a concentration from about 20 to about 150 mg/ml. D. The composition of any of embodiments A-C, wherein said adalimumab is at a concentration from about 20 to about 100 mg/ml. E. The composition of any of embodiments A-D, wherein said adalimumab is at a concentration from about 30 to about 50 mg/ml. F. The composition of any of embodiments A-E, wherein said buffer is at a concentration from about 5 mM to about 50 mM. G. The composition of any of embodiments A-F, wherein said buffer is at a concentration from about 5 mM to about 20 mM. H. The composition of any of embodiments A-G, wherein said buffer is at a concentration from about 10 mM to about 20 mM. I. The composition of any of embodiments A-H, wherein said surfactant is a polysorbate. J. The composition of embodiment I, wherein said polysorbate is polysorbate 80. K. The composition of any of embodiments A-J, wherein said polyol is a sugar alcohol. L. The composition of embodiment K, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. M. The composition of embodiment L, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. N. The composition of any of embodiments L-M, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. O. The composition of any of embodiments L-N, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. P. The composition of any of embodiments A-O further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. Q. The composition of embodiment P, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. R. The composition of embodiment P, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. S. The composition of embodiment P, wherein said metal ion is selected from zinc, magnesium and calcium. T. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, mannitol at a concentration from about 1 to 10% weight by volume, polysorbate 80 at a concentration from about 1 to 50 μM, and citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of phosphate. U A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a surfactant. V. The composition of embodiment U, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. W. The composition of any of embodiments U-V, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. X. The composition of any of embodiments U-W, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. Y. The composition of any of embodiments U-X, wherein said buffer is at a concentration from about 5 mM and about 50 mM. Z. The composition of any of embodiments U-Y, wherein said buffer is at a concentration from about 5 mM and about 20 mM. AA. The composition of any of embodiments U-Z, wherein said buffer is at a concentration from about 10 mM and about 20 mM. BB. The composition of any of embodiments U-AA, wherein said polyol is a sugar alcohol. CC. The composition of embodiment BB, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. DD. The composition of embodiment CC, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. EE. The composition of any of embodiments CC-DD, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. FF. The composition of any of embodiments CC-EE, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. GG. The composition of any of embodiments U-FF further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. HH. The composition of embodiment GG, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. II. The composition of embodiment GG, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. JJ. The composition of embodiment GG, wherein said metal ion is selected from zinc, magnesium and calcium. KK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, mannitol at a concentration from about 1 to 10% weight by volume, and citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a surfactant. LL. A stable aqueous pharmaceutical composition comprising adalimumab, a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion, and wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a polyol. MM. The composition of embodiment LL, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. NN. The composition of any of embodiments LL-MM, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. OO. The composition of any of embodiments LL-NN, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. PP. The composition of any of embodiments LL-00, wherein said buffer is at a concentration from about 5 mM and about 50 mM. QQ. The composition of any of embodiments LL-PP, wherein said buffer is at a concentration from about 5 mM and about 20 mM. RR. The composition of any of embodiments LL-QQ, wherein said buffer is at a concentration from about 10 mM and about 20 mM. SS. The composition of embodiment LL, wherein said stabilizer is selected from the group consisting of an amino acid, a salt, EDTA and a metal ion. TT. The composition of embodiment TT, wherein said amino acid is selected from the group consisting of glycine, alanine and arginine. UU. The composition of embodiment TT, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. VV. The composition of embodiment TT, wherein said glycine is at a concentration from about 20 to about 200 mM. WW. The composition of embodiment W, wherein said glycine is at a concentration from about 50 to about 200 mM. XX. The composition of embodiment TT, wherein said arginine is at a concentration from about 1 to about 250 mM. YY. The composition of embodiment XX, wherein said arginine is at a concentration from about 20 to about 200 mM. ZZ. The composition of embodiment YY, wherein said arginine is at a concentration from about 20 to about 100 mM. AAA. The composition of embodiment UU, wherein said sodium chloride is at a concentration from about 5 to about 150 mM. BBB. The composition of embodiment AAA, wherein said sodium chloride is at a concentration from about 20 to about 140 mM. CCC. The composition of embodiment AAA, wherein said sodium chloride is at a concentration from about 75 to about 125 mM. DDD. The composition of embodiment UU, wherein said sodium sulfate is at a concentration from about 5 to about 150 mM. EEE. The composition of embodiment UU, wherein said sodium chloride is at a concentration from about 20 to about 120 mM. FFF. The composition of embodiment EEE, wherein said sodium chloride is at a concentration from about 60 to about 100 mM. GGG. The composition of any of embodiments LL-FF further comprising a surfactant. HHH. The composition of embodiment GGG, wherein said surfactant is a polysorbate. III. The composition of embodiment HHH, wherein said polysorbate is polysorbate 80. JJJ. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, glycine at a concentration from about 20 to about 200 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. KKK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, arginine at a concentration from about 1 to about 250 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH from about 5 to about 5.5, and wherein said composition is substantially free of a polyol. LLL. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. MMM. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, polysorbate 80 at a concentration from about 1 to 50 μM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. NNN. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion, and a buffer selected from the group consisting of citrate, phosphate, succinate, tartrate and maleate, wherein said composition has a pH from about 5 to about 6. OOO. The composition of embodiment NNN, wherein the buffer does not comprise a combination of citrate and phosphate. PPP. The composition of embodiment NNN, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. QQQ. The composition of any of embodiments NNN-PPP, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. RRR. The composition of any of embodiments NNN-QQQ, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. SSS. The composition of any of embodiments NNN-RRR, wherein said buffer is at a concentration from about 5 mM and about 50 mM. TTT. The composition of any of embodiments NNN-SSS, wherein said buffer is at a concentration from about 5 mM and about 20 mM. UUU. The composition of any of embodiments NNN-TTT, wherein said buffer is at a concentration from about 10 mM and about 20 mM. VVV. The composition of any of embodiments NNN-UUU, wherein said surfactant is a polysorbate. WWW. The composition of embodiment VVV, wherein said polysorbate is polysorbate 80. XXX. The composition of any of embodiments NNN-WWW, wherein said polyol is a sugar alcohol. YYY. The composition of embodiment XXX, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. ZZZ. The composition of embodiment YYY, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. AAAA. The composition of any of embodiments YYY-ZZZ, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. BBBB. The composition of any of embodiments YYY-AAAA, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. CCCC. The composition of any of embodiments NNN-BBBB, wherein said stabilizer is EDTA. DDDD. The composition of embodiment CCCC, wherein said EDTA is at a concentration from about 0.01% to about 0.5%. EEEE. The composition of embodiment DDDD, wherein said EDTA is at a concentration from about 0.05% to about 0.25%. FFFF. The composition of embodiment EEEE, wherein said EDTA is at a concentration from about 0.08% to about 0.2%. GGGG. The composition of any of embodiments NNN-BBBB, wherein said stabilizer is methionine. HHHH. The composition of embodiment GGGG, wherein said methionine is at a concentration from about 1 to about 10 mg/ml. IIII. The composition of embodiment GGGG, wherein said methionine is at a concentration from about 1 to about 5 mg/ml. JJJJ. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol at a concentration from about 1 to 10% weight by volume, EDTA at a concentration from about 0.01% to about 0.5%, citrate at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. KKKK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol at a concentration from about 1 to 10% weight by volume, methionine at a concentration from about 1 to about 10 mg/ml, citrate at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. LLLL. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, tartrate and maleate, wherein said composition has a pH of about 3.5. MMMM. The composition of embodiment LLLL, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. NNNN. The composition of any of embodiments LLLL-MMMM, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. OOOO. The composition of any of embodiments LLLL-NNNN, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. PPPP. The composition of any of embodiments LLLL-0000, wherein said buffer is at a concentration from about 5 mM and about 50 mM. QQQQ. The composition of any of embodiments LLLL-PPPP, wherein said buffer is at a concentration from about 5 mM and about 20 mM. RRRR. The composition of any of embodiments LLLL-QQQQ, wherein said buffer is at a concentration from about 10 mM and about 20 mM. SSSS. The composition of any of embodiments LLLL-RRRR, wherein said polyol is a sugar alcohol. TTTT. The composition of embodiment SSSS, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. UUUU. The composition of embodiment TTTT, wherein said mannitol is at a concentration from about 1 to about 10% weight by volume of the total composition. VVVV. The composition of any of embodiments TTTT-UUUU, wherein said mannitol is at a concentration from about 2 to about 6% weight by volume of the total composition. WWWW. The composition of any of embodiments TTTT-VVVV, wherein said mannitol is at a concentration from about 3 to about 5% weight by volume of the total composition. XXXX. The composition of any of embodiments LLLL-WWWW further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. YYYY. The composition of embodiment XXXX, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. ZZZZ. The composition of embodiment XXXX, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. AAAAA. The composition of embodiment XXXX, wherein said metal ion is selected from zinc, magnesium and calcium. BBBBB. The composition of any of embodiments LLLL-AAAAA further comprising a surfactant. CCCCC. The composition of embodiment BBBBB, wherein said surfactant is a polysorbate. DDDDD. The composition of embodiment CCCCC, wherein said polysorbate is polysorbate 80. EEEEE. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM; polyol selected from sorbitol, mannitol or trehalose at a concentration from about 1 to about 10% weight by volume, and at least one amino acid stabilizer selected from the group consisting of (a) arginine at a concentration from about 1 to about 250 mg/ml and (b) glycine at a concentration of about 20 to 200 mg/ml, and histidine buffer or succinate buffer at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. FFFFF. The composition of embodiment EEEEE wherein the polyol is sorbitol, and the composition is free or substantially free of any citrate/phosphate buffer combination, and the formulation comprises arginine or glycine, but not both. GGGGG. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, arginine at a concentration from about 1 to about 250 mg/ml, glycine at a concentration of about 20 to 200 mg/ml, and histidine buffer or succinate buffer at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5 and said composition is free or substantially free of polyol. HHHHH. The composition of embodiment GGGGG wherein the composition is free or substantially free of any citrate/phosphate buffer combination. Appendix C Further Representative Embodiments Disclosed in Priority Application U.S. Ser. No. 61/769,581 A. A stable aqueous pharmaceutical composition comprising adalimumab and a single buffer. B. The composition of embodiment A, wherein said single buffer is selected from the group consisting of succinate, histidine, citrate, phosphate, tartrate and maleate. C. The composition of any of the preceding embodiments, wherein said composition has a pH of about 5 to about 6. D. The composition of any of the preceding embodiments, wherein said adalimumab contained in said pharmaceutical compositions does not lose more than 20% of its activity relative to activity of the composition at the beginning of storage. E. The composition of any of the preceding embodiments, further comprising a surfactant. F. The composition of embodiment E, wherein said surfactant is a polysorbate. G. The composition of embodiment F wherein said polysorbate is polysorbate 80. H. The composition of any of the preceding embodiments, further comprising a polyol. I. The composition of embodiment H, wherein said polyol is a sugar alcohol. J. The composition of embodiment I, wherein said sugar alcohol is sorbitol. K. The composition of any of the preceding embodiments, further comprising a sugar. L. The composition of embodiment K, wherein said sugar is selected from the group consisting of sucrose and trehalose. M. The composition of any of the preceding embodiments, wherein said adalimumab is at a concentration from about 20 to about 150 mg/ml. N. The composition of any of the preceding embodiments, wherein said buffer is at a concentration from about 5 mM to about 50 mM. O. The composition of any of embodiments A-N further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. P. The composition of embodiment O, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. Q. The composition of embodiment 0, wherein said metal ion is selected from zinc, magnesium and calcium. R. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 0.01% w/v to 0.5% w/v by weight of the total formulation, and succinate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. S. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 0.01% w/v to 0.5% w/v by weight of the total formulation, and histidine at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. T. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 0.01% w/v to 0.5% w/v by weight of the total formulation, and tartrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. U. A method of treating a mammal comprising administering to said mammal a therapeutically effective amount of the composition of any of preceding embodiments, wherein said mammal has a disease or disorder that can be beneficially treated with adalimumab. V. The method of embodiment U, wherein said disease or disorder is selected from the group consisting of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Wegener's disease (granulomatosis), Crohn's disease (or inflammatory bowel disease), chronic obstructive pulmonary disease (COPD), Hepatitis C, endometriosis, asthma, cachexia, psoriasis, and atopic dermatitis."},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE INVENTION <EOH>Tumor necrosis factor alpha (TNFα) is a naturally occurring mammalian cytokine produced by various cell types, including monocytes and macrophages in response to endotoxin or other stimuli. TNFα is a major mediator of inflammatory, immunological, and pathophysiological reactions (Grell, M., et al. (1995) Cell, 83: 793-802). Soluble TNFα is formed by the cleavage of a precursor transmembrane protein (Kriegler, et al. (1988) Cell 53: 45-53), and the secreted 17 kDa polypeptides assemble to soluble homotrimer complexes (Smith, et al. (1987), J. Biol. Chem. 262: 6951-6954; for reviews of TNF, see Butler, et al. (1986), Nature 320:584; Old (1986), Science 230: 630). These complexes then bind to receptors found on a variety of cells. Binding produces an array of pro-inflammatory effects, including (i) release of other pro-inflammatory cytokines such as interleukin (IL)-6, IL-8, and IL-1, (ii) release of matrix metalloproteinases and (iii) up-regulation of the expression of endothelial adhesion molecules, further amplifying the inflammatory and immune cascade by attracting leukocytes into extravascular tissues. There are many disorders associated with elevated levels of TNFα. For example, TNFα has been shown to be up-regulated in a number of human diseases, including chronic diseases such as rheumatoid arthritis (RA), inflammatory bowel disorders, including Crohn's disease and ulcerative colitis, sepsis, congestive heart failure, asthma bronchiale and multiple sclerosis. TNFα is also referred to as a pro-inflammatory cytokine. Physiologically, TNFα is also associated with protection from particular infections (Cerami. et al. (1988), Immunol. Today 9:28). TNFα is released by macrophages that have been activated by lipopolysaccharides of Gram-negative bacteria. As such, TNFα appears to be an endogenous mediator of central importance involved in the development and pathogenesis of endotoxic shock associated with bacterial sepsis. Adalimumab (Humira®, AbbVie, Inc.) is a recombinant human IgG1 monoclonal antibody specific for human TNF. This antibody is also known as D2E7. Adalimumab consists of 1330 amino acids and has a molecular weight of approximately 148 kilodaltons. Adalimumab has been described and claimed in U.S. Pat. No. 6,090,382, the disclosure of which is hereby incorporated by reference in its entirety. Adalimumab is usually produced by recombinant DNA technology in a mammalian cell expression system, such as, for example, Chinese Hamster Ovary cells. Adalimumab binds specifically to TNFα and neutralizes the biological function of TNF by blocking its interaction with the p55 and p75 cell surface TNF receptors. Various formulations of adalimumab are known in the art. See, for example, U.S. Pat. Nos. 8,216,583 and 8,420,081. There is still need for stable liquid formulations of adalimumab that allow its long term storage without substantial loss in efficacy."},"summary":{"kind":"string","value":"<SOH> SUMMARY OF THE INVENTION <EOH>The invention provides stable aqueous formulations comprising adalimumab that allow its long term storage. In a first embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab; a stabilizer comprising at least one member selected from the group consisting of a polyol and a surfactant; and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said buffer does not comprise a combination of citrate and phosphate, and preferably does not comprise any citrate buffer. In this embodiment, the stabilizer preferably comprises both polyol and surfactant. In a second embodiment, utilizing a single buffer system, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer system comprising a single buffering agent, said single buffering agent being selected from citrate, phosphate, succinate, histidine, tartrate or maleate, but not including combinations of the foregoing; wherein the formulation has a pH of about 4 to 8, and preferably about 5 to about 6. Histidine and succinate are particularly preferred for use as single buffering agents. As used herein the term buffer, buffer system, or buffering agent, and like terminology, is intended to denoted buffer components that introduce buffer capacity in the formulation in addition to any buffering capacity offered by the protein itself, hence the term “buffer”, etc, is not intended to include the protein itself as a self buffering entity. In a third embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a stabilizer comprising at least one member selected from a polyol and a surfactant, wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said composition is substantially free of a buffer. In a fourth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said composition is free or substantially free of a surfactant. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate; and (iii) the polyol is selected from the group consisting of mannitol, sorbitol and trehalose. In a fifth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to 8 and preferably about 5 to about 6, and wherein said composition is substantially free of polyol. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate, including combinations thereof. In each of the five embodiments discussed above, the composition may optionally further comprise a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid stabilizer may be selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. The salt stabilizer may be selected from the group consisting of sodium chloride and sodium sulfate. The metal ion stabilizer may be selected from the group consisting of zinc, magnesium and calcium. Preferably, adalimumab formulations containing the stabilizers mentioned above also do not contain buffer systems in which phosphate buffer and citrate buffer are present in combination, and, most preferably contains buffer systems free or substantially free of citrate buffer. In particularly preferred embodiments, (i) the optional additional stabilizer present in this embodiment is not sodium chloride, or comprises sodium chloride present in amounts not to exceed about 100 mM, and comprises at least one of arginine and glycine, including combinations of the two amino acids; (ii) the buffer, when present, contains no citrate, or at least no citrate and phosphate combination, but is instead at least one of histidine and succinate, including combinations thereof; and (iii) the stabilizer when it includes a polyol is preferably mannitol in amounts exceeding about 150 mM. In further embodiments the invention is directed to an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of a buffer combination that comprises both a citrate buffer and a phosphate buffer; and (ii) the composition exhibits long term stability. Another embodiment of the invention concerns an aqueous, buffered pharmaceutical composition exhibiting long term stability, said composition comprising: (i) adalimumab; (ii) a buffer selected from the group consisting of histidine buffer, succinate buffer, and combinations thereof; (iii) a polysorbate or poloxamer surfactant, or combinations thereof; and (iv) one or both of the following: (a) a stabilizer selected from the group consisting of glycine, alanine, glutamate, arginine, methionine, EDTA, sodium chloride, sodium sulfate, metal ions, and combinations thereof; and (b) a polyol selected from sorbitol, mannitol, and trehalose, or combinations thereof. Optionally, the formulation may also include a sugar, such as sucrose. In a further embodiment the invention is an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of a polyol; and (ii) the composition exhibits long term stability. In still a further embodiment the invention is directed to an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of surfactant; and (ii) the composition exhibits long term stability. Another embodiment of the inventions concerns an aqueous pharmaceutical composition comprising adalimumab wherein: (i) the composition is free or substantially free of buffer; and (ii) the composition exhibits long term stability. In another embodiment, the adalimumab formulation of the present invention comprises, consists of, or consists essentially of, adalimumab, histidine buffer as the sole buffer in the formulation, glycine (or arginine, or combinations thereof) as the sole stabilizer among the non-surfactant stabilizers referenced earlier, and polysorbate 80. In this formulation, the amount of adalimumab is 20 to 150 mg/ml, the amount of histidine buffer is up to about 50 mM; the amount of glycine is up to about 300 mM; and the amount of polysorbate 80 is in the range of about 0.01 to about 0.2 wt %. Optionally, this formulation may include up to about 100 mM NaCl. The present invention also contemplates modification of this formulation to combine the histidine buffer with one or more of citrate, acetate, phosphate, maleate, tartrate buffers. In yet another embodiment, the adalimumab formulation of the present invention comprises, consists of, or consists essentially of, adalimumab, histidine buffer as the sole buffer, mannitol (or sorbitol or trehelose), and polysorbate 80, and further being free or substantially free of the non-surfactant stabilizers (e.g. glycine, arginine, etc.) referenced above. In this formulation, the amount of adalimumab is 20 to 150 mg/ml; the amount of histidine buffer is up to about 50 mM; the amount of polyol is up to about 300 mM; and the amount of polysorbate 80 is in the range of about 0.01 to about 0.2 wt %. Optionally, this formulation may include up to about 100 mM NaCl. The present invention also contemplates modification of this formulation to combine the histidine buffer with one or more of citrate, acetate, phosphate, maleate, tartrate buffers. In a method aspect, the invention is directed to a method for enhancing long term stability in an aqueous, buffered adalimumab formulation, comprising one or more of the steps of: (a) incorporating histidine buffer, succinate buffer, or a combination thereof, in the formulation based on empirical data indicating that such buffers contribute to the stability of the formulation to a greater extent than other buffers or buffer combinations; or (b) incorporating glycine, arginine or a combination thereof as stabilizers in the formulation, based upon empirical data indicating that such stabilizer contribute to the stability of the formulation to a greater extent than other stabilizers; or (c) substantially excluding the presence of buffer or buffer combinations comprising citrate buffer (especially buffer combinations comprising both citrate and phosphate) based upon empirical data indicating that such buffer or buffer combinations perform poorly in terms of stabilizing the formulation in comparison to other buffers. The method may further comprise the selection of PS 80 as a surfactant based on empirical data indicating that PS 80 imparts better thermal stability to the adalimumab formulation than other surfactants, including PS 20. The method is useful to obtain a formulation of adalimumab that exhibits long term stability comparable to or better than commercially available adalimumab formulations marketed under the trademark Humira®. In a further method aspect, the invention is directed to a method for treating an inflammatory condition in a subject which comprises administering to such subject any of the adalimumab formulation embodiments as described herein. In the foregoing embodiments, where the above referenced stabilizers may be included in the formulations, it is further discovered that satisfactory stabilization can be attained when such stabilizers are used in place of both polyol and surfactant and hence stabilized formulations of the present invention can be free or substantially free of both polyol and surfactant. Accordingly, in a sixth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, optionally a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, EDTA, and a metal ion, and wherein said composition has a pH of about 4 to about 8, and preferably 5 to about 6, and wherein said composition is either substantially free of both polyol and surfactant. When buffer is present in this embodiment, it is especially preferred that (i) the buffer not include the combination of citrate and phosphate; (ii) the buffer is selected from the group consisting of histidine and succinate; and (iii) the stabilizer does not comprise sodium chloride, but instead is at least one member selected from the group consisting of arginine and glycine. Important aspects of the present invention in certain embodiments include (i) that sorbitol and trehalose are discovered to be significantly better stabilizers of adalimumab formulations than mannitol, unless mannitol is used at concentrations in excess of about 200-300 mM in which case the three are generally equivalent; (ii) arginine and glycine (and combinations) are discovered to be significantly better stabilizers of adalimumab formulations than sodium chloride; and; (iii) when buffers are used in the formulation, it is discovered that the combination of citrate and phosphate is surprisingly significantly poorer in stabilizing adalimumab than other buffers such as succinate, histidine, phosphate and tartrate. The relatively poor performance of the buffer combination of citrate and phosphate is rather unexpected considering the apparent importance attributed to the use of a citrate/phosphate combined buffer in U.S. Pat. No. 8,216,583. To the contrary, we have now found that a phosphate/citrate buffer combination is not an optimal choice for obtaining a stabilized adalimumab formulation, and in fact, an element of our invention is the discovery that this combination should be avoided altogether in favor of other buffer systems. Preferably, a polyol is a sugar alcohol; and even more preferably, the sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. However, as between mannitol and sorbitol, the invention has discovered, as noted above, a distinct stabilization advantage in using sorbitol or trehalose instead of mannitol, unless mannitol is used at concentrations in excess of about 200 mM, in which case mannitol, sorbitol and trehalose are generally equivalent. At concentrations below about 200 mM, mannitol has been found to be a poorer stabilizer than sorbitol or trehalose in an adalimumab formulation. Preferably, a surfactant is a polysorbate or poloxamer; and even more preferably PS 80, PS 40, PS20, Pluronic F-68 and combinations. We have discovered a distinct and surprising thermal stabilization advantage in selecting PS 80 instead of PS-20. These and other aspects will become apparent from the following description of the various embodiments, although variations and modifications therein may be affected without departing from the spirit and scope of the novel concepts of the disclosure. It is to be understood that both the foregoing general description and the following detailed description are exemplary and explanatory only and are not restrictive of the invention, as claimed. Further representative embodiments are set forth in the numerous formulation studies reported in the detailed description, as well as the various embodiments listed in Appendices A, B and C attached hereto and made a part hereof."},"cpc_label":{"kind":"string","value":"A61K3939591"},"filing_date":{"kind":"string","value":"20171005"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180215"},"examiner_id":{"kind":"string","value":"72243.0"},"ipc_label":{"kind":"string","value":"A61K39395"},"npe_litigated_count":{"kind":"number","value":1,"string":"1"},"examiner_full_name":{"kind":"string","value":"KIM, YUNSOO"},"invention_title":{"kind":"string","value":"Stable Aqueous Formulations of Adalimumab"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"A61K"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32897,"cells":{"application_number":{"kind":"number","value":15726215,"string":"15,726,215"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"Stable Aqueous Formulations of Adalimumab"},"abstract":{"kind":"string","value":"The invention provides aqueous pharmaceutical adalimumab compositions suitable for long-term storage of adalimumab, methods of manufacture of these compositions, methods of administration, and kits containing same."},"claims":{"kind":"string","value":"1. A stable aqueous pharmaceutical composition comprising: i) adalimumab; ii) a single buffer; iii) a surfactant; and iv) a sugar, wherein the composition is free of polyol and has a pH of about 5 to about 6. 2. The composition of claim 1, wherein the composition is free of citrate buffer. 3. The composition of claim 2, wherein the single buffer is acetate. 4. The composition of claim 1, wherein the surfactant is polysorbate 80. 5. The composition of claim 1, wherein the sugar is sucrose. 6. The composition of claim 5, wherein the single buffer is acetate and the surfactant is polysorbate 80. 7. The composition of claim 6, wherein the composition is free of sodium chloride. 8. The composition of claim 1, wherein the composition has osmolality of about 180 to 420 mOsM; the composition is suitable for administration to a subject as a single dose; and the dose contains about 40 mg of adalimumab. 9. The composition of claim 8, wherein the single buffer is acetate, the surfactant is polysorbate 80, and the sugar is sucrose."},"description":{"kind":"string","value":"FIELD OF THE INVENTION The present invention relates to aqueous pharmaceutical compositions suitable for long-term storage of adalimumab (including antibody proteins considered or intended as “biosimilar” or “bio-better” variants of commercially available adalimumab), methods of manufacture of the compositions, methods of their administration, and kits containing the same. BACKGROUND OF THE INVENTION Tumor necrosis factor alpha (TNFα) is a naturally occurring mammalian cytokine produced by various cell types, including monocytes and macrophages in response to endotoxin or other stimuli. TNFα is a major mediator of inflammatory, immunological, and pathophysiological reactions (Grell, M., et al. (1995) Cell, 83: 793-802). Soluble TNFα is formed by the cleavage of a precursor transmembrane protein (Kriegler, et al. (1988) Cell 53: 45-53), and the secreted 17 kDa polypeptides assemble to soluble homotrimer complexes (Smith, et al. (1987), J. Biol. Chem. 262: 6951-6954; for reviews of TNF, see Butler, et al. (1986), Nature 320:584; Old (1986), Science 230: 630). These complexes then bind to receptors found on a variety of cells. Binding produces an array of pro-inflammatory effects, including (i) release of other pro-inflammatory cytokines such as interleukin (IL)-6, IL-8, and IL-1, (ii) release of matrix metalloproteinases and (iii) up-regulation of the expression of endothelial adhesion molecules, further amplifying the inflammatory and immune cascade by attracting leukocytes into extravascular tissues. There are many disorders associated with elevated levels of TNFα. For example, TNFα has been shown to be up-regulated in a number of human diseases, including chronic diseases such as rheumatoid arthritis (RA), inflammatory bowel disorders, including Crohn's disease and ulcerative colitis, sepsis, congestive heart failure, asthma bronchiale and multiple sclerosis. TNFα is also referred to as a pro-inflammatory cytokine. Physiologically, TNFα is also associated with protection from particular infections (Cerami. et al. (1988), Immunol. Today 9:28). TNFα is released by macrophages that have been activated by lipopolysaccharides of Gram-negative bacteria. As such, TNFα appears to be an endogenous mediator of central importance involved in the development and pathogenesis of endotoxic shock associated with bacterial sepsis. Adalimumab (Humira®, AbbVie, Inc.) is a recombinant human IgG1 monoclonal antibody specific for human TNF. This antibody is also known as D2E7. Adalimumab consists of 1330 amino acids and has a molecular weight of approximately 148 kilodaltons. Adalimumab has been described and claimed in U.S. Pat. No. 6,090,382, the disclosure of which is hereby incorporated by reference in its entirety. Adalimumab is usually produced by recombinant DNA technology in a mammalian cell expression system, such as, for example, Chinese Hamster Ovary cells. Adalimumab binds specifically to TNFα and neutralizes the biological function of TNF by blocking its interaction with the p55 and p75 cell surface TNF receptors. Various formulations of adalimumab are known in the art. See, for example, U.S. Pat. Nos. 8,216,583 and 8,420,081. There is still need for stable liquid formulations of adalimumab that allow its long term storage without substantial loss in efficacy. SUMMARY OF THE INVENTION The invention provides stable aqueous formulations comprising adalimumab that allow its long term storage. In a first embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab; a stabilizer comprising at least one member selected from the group consisting of a polyol and a surfactant; and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said buffer does not comprise a combination of citrate and phosphate, and preferably does not comprise any citrate buffer. In this embodiment, the stabilizer preferably comprises both polyol and surfactant. In a second embodiment, utilizing a single buffer system, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer system comprising a single buffering agent, said single buffering agent being selected from citrate, phosphate, succinate, histidine, tartrate or maleate, but not including combinations of the foregoing; wherein the formulation has a pH of about 4 to 8, and preferably about 5 to about 6. Histidine and succinate are particularly preferred for use as single buffering agents. As used herein the term buffer, buffer system, or buffering agent, and like terminology, is intended to denoted buffer components that introduce buffer capacity in the formulation in addition to any buffering capacity offered by the protein itself, hence the term “buffer”, etc, is not intended to include the protein itself as a self buffering entity. In a third embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a stabilizer comprising at least one member selected from a polyol and a surfactant, wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said composition is substantially free of a buffer. In a fourth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said composition is free or substantially free of a surfactant. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate; and (iii) the polyol is selected from the group consisting of mannitol, sorbitol and trehalose. In a fifth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to 8 and preferably about 5 to about 6, and wherein said composition is substantially free of polyol. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate, including combinations thereof. In each of the five embodiments discussed above, the composition may optionally further comprise a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid stabilizer may be selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. The salt stabilizer may be selected from the group consisting of sodium chloride and sodium sulfate. The metal ion stabilizer may be selected from the group consisting of zinc, magnesium and calcium. Preferably, adalimumab formulations containing the stabilizers mentioned above also do not contain buffer systems in which phosphate buffer and citrate buffer are present in combination, and, most preferably contains buffer systems free or substantially free of citrate buffer. In particularly preferred embodiments, (i) the optional additional stabilizer present in this embodiment is not sodium chloride, or comprises sodium chloride present in amounts not to exceed about 100 mM, and comprises at least one of arginine and glycine, including combinations of the two amino acids; (ii) the buffer, when present, contains no citrate, or at least no citrate and phosphate combination, but is instead at least one of histidine and succinate, including combinations thereof; and (iii) the stabilizer when it includes a polyol is preferably mannitol in amounts exceeding about 150 mM. In further embodiments the invention is directed to an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of a buffer combination that comprises both a citrate buffer and a phosphate buffer; and (ii) the composition exhibits long term stability. Another embodiment of the invention concerns an aqueous, buffered pharmaceutical composition exhibiting long term stability, said composition comprising: (i) adalimumab; (ii) a buffer selected from the group consisting of histidine buffer, succinate buffer, and combinations thereof; (iii) a polysorbate or poloxamer surfactant, or combinations thereof; and (iv) one or both of the following: (a) a stabilizer selected from the group consisting of glycine, alanine, glutamate, arginine, methionine, EDTA, sodium chloride, sodium sulfate, metal ions, and combinations thereof; and (b) a polyol selected from sorbitol, mannitol, and trehalose, or combinations thereof. Optionally, the formulation may also include a sugar, such as sucrose. In a further embodiment the invention is an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of a polyol; and (ii) the composition exhibits long term stability. In still a further embodiment the invention is directed to an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of surfactant; and (ii) the composition exhibits long term stability. Another embodiment of the inventions concerns an aqueous pharmaceutical composition comprising adalimumab wherein: (i) the composition is free or substantially free of buffer; and (ii) the composition exhibits long term stability. In another embodiment, the adalimumab formulation of the present invention comprises, consists of, or consists essentially of, adalimumab, histidine buffer as the sole buffer in the formulation, glycine (or arginine, or combinations thereof) as the sole stabilizer among the non-surfactant stabilizers referenced earlier, and polysorbate 80. In this formulation, the amount of adalimumab is 20 to 150 mg/ml; the amount of histidine buffer is up to about 50 mM; the amount of glycine is up to about 300 mM; and the amount of polysorbate 80 is in the range of about 0.01 to about 0.2 wt %. Optionally, this formulation may include up to about 100 mM NaCl. The present invention also contemplates modification of this formulation to combine the histidine buffer with one or more of citrate, acetate, phosphate, maleate, tartrate buffers. In yet another embodiment, the adalimumab formulation of the present invention comprises, consists of, or consists essentially of, adalimumab, histidine buffer as the sole buffer, mannitol (or sorbitol or trehelose), and polysorbate 80, and further being free or substantially free of the non-surfactant stabilizers (e.g. glycine, arginine, etc.) referenced above. In this formulation, the amount of adalimumab is 20 to 150 mg/ml; the amount of histidine buffer is up to about 50 mM; the amount of polyol is up to about 300 mM; and the amount of polysorbate 80 is in the range of about 0.01 to about 0.2 wt %. Optionally, this formulation may include up to about 100 mM NaCl. The present invention also contemplates modification of this formulation to combine the histidine buffer with one or more of citrate, acetate, phosphate, maleate, tartrate buffers. In a method aspect, the invention is directed to a method for enhancing long term stability in an aqueous, buffered adalimumab formulation, comprising one or more of the steps of: (a) incorporating histidine buffer, succinate buffer, or a combination thereof, in the formulation based on empirical data indicating that such buffers contribute to the stability of the formulation to a greater extent than other buffers or buffer combinations; or (b) incorporating glycine, arginine or a combination thereof as stabilizers in the formulation, based upon empirical data indicating that such stabilizer contribute to the stability of the formulation to a greater extent than other stabilizers; or (c) substantially excluding the presence of buffer or buffer combinations comprising citrate buffer (especially buffer combinations comprising both citrate and phosphate) based upon empirical data indicating that such buffer or buffer combinations perform poorly in terms of stabilizing the formulation in comparison to other buffers. The method may further comprise the selection of PS 80 as a surfactant based on empirical data indicating that PS 80 imparts better thermal stability to the adalimumab formulation than other surfactants, including PS 20. The method is useful to obtain a formulation of adalimumab that exhibits long term stability comparable to or better than commercially available adalimumab formulations marketed under the trademark Humira®. In a further method aspect, the invention is directed to a method for treating an inflammatory condition in a subject which comprises administering to such subject any of the adalimumab formulation embodiments as described herein. In the foregoing embodiments, where the above referenced stabilizers may be included in the formulations, it is further discovered that satisfactory stabilization can be attained when such stabilizers are used in place of both polyol and surfactant and hence stabilized formulations of the present invention can be free or substantially free of both polyol and surfactant. Accordingly, in a sixth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, optionally a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, EDTA, and a metal ion, and wherein said composition has a pH of about 4 to about 8, and preferably 5 to about 6, and wherein said composition is either substantially free of both polyol and surfactant. When buffer is present in this embodiment, it is especially preferred that (i) the buffer not include the combination of citrate and phosphate; (ii) the buffer is selected from the group consisting of histidine and succinate; and (iii) the stabilizer does not comprise sodium chloride, but instead is at least one member selected from the group consisting of arginine and glycine. Important aspects of the present invention in certain embodiments include (i) that sorbitol and trehalose are discovered to be significantly better stabilizers of adalimumab formulations than mannitol, unless mannitol is used at concentrations in excess of about 200-300 mM in which case the three are generally equivalent; (ii) arginine and glycine (and combinations) are discovered to be significantly better stabilizers of adalimumab formulations than sodium chloride; and; (iii) when buffers are used in the formulation, it is discovered that the combination of citrate and phosphate is surprisingly significantly poorer in stabilizing adalimumab than other buffers such as succinate, histidine, phosphate and tartrate. The relatively poor performance of the buffer combination of citrate and phosphate is rather unexpected considering the apparent importance attributed to the use of a citrate/phosphate combined buffer in U.S. Pat. No. 8,216,583. To the contrary, we have now found that a phosphate/citrate buffer combination is not an optimal choice for obtaining a stabilized adalimumab formulation, and in fact, an element of our invention is the discovery that this combination should be avoided altogether in favor of other buffer systems. Preferably, a polyol is a sugar alcohol; and even more preferably, the sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. However, as between mannitol and sorbitol, the invention has discovered, as noted above, a distinct stabilization advantage in using sorbitol or trehalose instead of mannitol, unless mannitol is used at concentrations in excess of about 200 mM, in which case mannitol, sorbitol and trehalose are generally equivalent. At concentrations below about 200 mM, mannitol has been found to be a poorer stabilizer than sorbitol or trehalose in an adalimumab formulation. Preferably, a surfactant is a polysorbate or poloxamer; and even more preferably PS 80, PS 40, PS20, Pluronic F-68 and combinations. We have discovered a distinct and surprising thermal stabilization advantage in selecting PS 80 instead of PS-20. These and other aspects will become apparent from the following description of the various embodiments, although variations and modifications therein may be affected without departing from the spirit and scope of the novel concepts of the disclosure. It is to be understood that both the foregoing general description and the following detailed description are exemplary and explanatory only and are not restrictive of the invention, as claimed. Further representative embodiments are set forth in the numerous formulation studies reported in the detailed description, as well as the various embodiments listed in Appendices A, B and C attached hereto and made a part hereof. BRIEF DESCRIPTION OF THE DRAWINGS The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee. FIG. 1 is a bar chart of stability of various adalimumab formulations as determined by size exclusion chromatography (SEC). FIG. 2 is a bar chart of stability of various adalimumab formulations as determined by reversed phase (RP) high performance liquid chromatography (HPLC). FIG. 3 is a graph of a partial least squares (PLS) model 1 demonstrating effect of citrate/phosphate on stability. FIG. 4 is a graph of a PLS model 2 demonstrating effect of citrate/phosphate on stability. FIG. 5 is a graph of a PLS model 1 demonstrating effect of histidine/glycine on stability. FIG. 6 is a graph of a PLS model 1 demonstrating effect of arginine/sorbitol on stability. FIG. 7 is a graph of a PLS model 1 demonstrating effect of pH/histidine on stability. FIG. 8 is a graph of a PLS model 2 demonstrating effect of pH/histidine on stability. FIG. 9 is a graph of a PLS model 2 demonstrating effect of trehalose/PS80 on stability. FIG. 10 is a graph of a PLS model 2 demonstrating effect of mannitol/PS80 on stability. FIG. 11 is a graph of a PLS model 1 demonstrating effect of mannitol/NaCl on stability. FIG. 12 is a graph of a PLS model 1 demonstrating effect of EDTA/methionine on stability. FIG. 13 is a graph of a PLS model A demonstrating effect of citrate and phosphate on stability. FIG. 14 is a graph of a PLS model A demonstrating effect of pH and histidine buffer on stability. FIG. 15 is a graph of a PLS model A demonstrating effect of glycine and arginine on stability. FIG. 16 is a graph of a PLS model A demonstrating effect of NaCl and polysorbate 80 (PS 80) on stability. FIG. 17 is a graph of a PLS model B demonstrating effect of citrate and phosphate on stability. FIG. 18 is a graph of a PLS model B demonstrating effect of pH and histidine buffer on stability. FIG. 19 is a graph of a PLS model B demonstrating effect arginine and glycine on stability. FIG. 20 is a graph of a PLS model B demonstrating effect of PS80 and mannitol on stability. FIG. 21 is a graph of a PLS model B demonstrating effect of EDTA and NaCl on stability. FIG. 22 is a graph of a PLS model B demonstrating effect of succinate buffer and histidine buffer on stability. FIG. 23 is a graph of a PLS model C demonstrating effect of citrate and phosphate on stability. FIG. 24 is a graph of a PLS model C demonstrating effect of pH and histidine buffer on stability. FIG. 25 is a graph of a PLS model C demonstrating effect of arginine and glycine on stability. FIG. 26 is a graph of a PLS model C demonstrating effect of mannitol and PS 80 on stability. FIG. 27 is a graph of a PLS model C demonstrating effect of PS 80 and NaCl on stability. FIG. 28 is a graph of a PLS model C demonstrating effect of pH and protein concentration on stability. DETAILED DESCRIPTION OF THE INVENTION Various embodiments of the invention are now described in detail. As used in the description and throughout the claims, the meaning of “a”, “an”, and “the” includes plural reference unless the context clearly dictates otherwise. Also, as used in the description and throughout the claims, the meaning of “in” includes “in” and “on” unless the context clearly dictates otherwise. Additionally, some terms used in this specification are more specifically defined below. Definitions The terms used in this specification generally have their ordinary meanings in the art, within the context of the invention, and in the specific context where each term is used. Certain terms that are used to describe the invention are discussed below, or elsewhere in the specification, to provide additional guidance to the practitioner regarding the description of the invention. Synonyms for certain terms are provided. A recital of one or more synonyms does not exclude the use of other synonyms. The use of examples anywhere in this specification including examples of any terms discussed herein is illustrative only, and in no way limits the scope and meaning of the invention or of any exemplified term. The invention is not limited to the various embodiments given in this specification. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains. In the case of conflict, the present document, including definitions will control. “Around,” “about” or “approximately” shall generally mean within 20 percent, within 10 percent, within 5, 4, 3, 2 or 1 percent of a given value or range. Numerical quantities given are approximate, meaning that the term “around,” “about” or “approximately” can be inferred if not expressly stated. The term “adalimumab” is synonymous with the active pharmaceutical ingredient in Humira® as well as protein considered or intended as biosimilar or bio-better variants thereof. Adalimumab is a recombinant human IgG1 monoclonal antibody specific for human TNF. Adalimumab is also known as D2E7. Adalimumab has two light chains, each with a molecular weight of approximately 24 kilodaltons (kDa) and two IgG1 heavy chains each with a molecular weight of approximately 49 kDa. Each light chain consists of 214 amino acid residues and each heavy chain consists of 451 amino acid residues. Thus, adalimumab consists of 1330 amino acids and has a total molecular weight of approximately 148 kDa. The term adalimumab is also intended to encompass so-called bio-similar or bio-better variants of the adalimumab protein used in commercially available Humira®. For example, a variant of commercial Humira® may be acceptable to the FDA when it has essentially the same pharmacological effects as commercially available Humira®, even though it may exhibit certain physical properties, such as glycosylation profile, that may be similar if not identical to Humira®. For the purposes of the present application, the term “adalimumab” also encompasses adalimumab with minor modifications in the amino acid structure (including deletions, additions, and/or substitutions of amino acids) or in the glycosylation properties, which do not significantly affect the function of the polypeptide. The term “adalimumab” encompasses all forms and formulations of Humira®, including but not limited to concentrated formulations, injectable ready-to-use formulations; formulations reconstituted with water, alcohol, and/or other ingredients, and others. The term “human TNFα” (which may be abbreviated as hTNFα, or simply hTNF), as used herein, is intended to refer to a human cytokine that exists as a 17 kD secreted form and a 26 kD membrane associated form, the biologically active form of which is composed of a trimer of noncovalently bound 17 kD molecules. The structure of hTNFα is described further in, for example, Pennica, D., et al. (1984) Nature 312:724-729; Davis, J. M., et al. (1987) Biochemistry 26:1322-1326; and Jones, E. Y., et al. (1989) Nature 338:225-228. The term human TNFα is intended to include recombinant human TNFα (rhTNFα), which can be prepared by standard recombinant expression methods or purchased commercially (R & D Systems, Catalog No. 210-TA, Minneapolis, Minn.). The term “antibody”, as used herein, refers to immunoglobulin molecules comprised of four polypeptide chains, two heavy (H) chains and two light (L) chains inter-connected by disulfide bonds. Each heavy chain is comprised of a heavy chain variable region (abbreviated herein as HCVR or VH) and a heavy chain constant region. The heavy chain constant region is comprised of three domains, CH1, CH2 and CH3. Each light chain is comprised of a light chain variable region (abbreviated herein as LCVR or VL) and a light chain constant region. The light chain constant region is comprised of one domain, CL. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FR). Each VH and VL is composed of three CDRs and four FRs, arranged from amino-terminus to carboxy-terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. In one embodiment of the invention, the formulation contains an antibody with CDR1, CDR2, and CDR3 sequences like those described in U.S. Pat. Nos. 6,090,382; 6,258,562, and 8,216,583. An antibody or antigen-binding portion thereof may be part of a larger immunoadhesion molecule, formed by covalent or noncovalent association of the antibody or antibody portion with one or more other proteins or peptides. Examples of such immunoadhesion molecules include use of the streptavidin core region to make a tetrameric scFv molecule (Kipriyanov, S. M., et al. (1995) Human Antibodies and Hybridomas 6:93-101) and use of a cysteine residue, a marker peptide and a C-terminal polyhistidine tag to make bivalent and biotinylated scFv molecules (Kipriyanov, S. M., et al. (1994) Mol. Immunol. 31:1047-1058). Antibody portions, such as Fab and F(ab′)2 fragments, can be prepared from whole antibodies using conventional techniques, such as papain or pepsin digestion, respectively, of whole antibodies. Moreover, antibodies, antibody portions and immunoadhesion molecules can be obtained using standard recombinant DNA techniques, as described herein. The term “isolated antibody”, as used herein, refers to an antibody that is substantially free of other antibodies having different antigenic specificities (e.g., an isolated antibody that specifically binds hTNFα is substantially free of antibodies that specifically bind antigens other than hTNFα). An isolated antibody that specifically binds hTNFα may, however, have cross-reactivity to other antigens, such as TNFα molecules from other species. Moreover, an isolated antibody may be substantially free of other cellular material and/or chemicals. The term “glycine” refers to an amino acid whose codons are GGT, GGC, GGA, and GGG. The term “arginine” refers to an α-amino acid whose codons are CCU, CCC, CCA, and CCG. The term “alanine” refers to an amino acid whose codons are GCT, GCC, GCA, and GCG. The term “methionine” refers to an amino acid whose codon is ATG. The term “glutamate” refers to an amino acid whose codons are GAA and GAG. The term “sugar” refers to monosaccharides, disachharides, and polysaccharides. Examples of sugars include, but are not limited to, sucrose, glucose, dextrose, and others. The term “polyol” refers to an alcohol containing multiple hydroxyl groups. Examples of polyols include, but are not limited to, mannitol, sorbitol, and others. The term “metal ion” refers to a metal atom with a net positive or negative electric charge. For the purposes of the present application, the term “metal ion” also includes sources of metal ions, including but not limited to metal salts. The term “long-term storage” or “long term stability” is understood to mean that the pharmaceutical composition can be stored for three months or more, for six months or more, and preferably for one year or more, most preferably a minimum stable shelf life of at least two years. Generally speaking, the terms “long term storage” and “long term stability” further include stable storage durations that are at least comparable to or better that the stable shelf typically required for currently available commercial formulations of adalimumab, without losses in stability that would render the formulation unsuitable for its intended pharmaceutical application. Long-term storage is also understood to mean that the pharmaceutical composition is stored either as a liquid at 2-8° C., or is frozen, e.g., at −20° C., or colder. It is also contemplated that the composition can be frozen and thawed more than once. The term “stable” with respect to long-term storage is understood to mean that adalimumab contained in the pharmaceutical compositions does not lose more than 20%, or more preferably 15%, or even more preferably 10%, and most preferably 5% of its activity relative to activity of the composition at the beginning of storage. The term “substantially free” means that either no substance is present or only minimal, trace amounts of the substance are present which do not have any substantial impact on the properties of the composition. If reference is made to no amount of a substance, it should be understood as “no detectable amount”. The term “mammal” includes, but is not limited to, a human. The term “pharmaceutically acceptable carrier” refers to a non-toxic solid, semisolid or liquid filler, diluent, encapsulating material, formulation auxiliary, or excipient of any conventional type. A pharmaceutically acceptable carrier is non-toxic to recipients at the dosages and concentrations employed and is compatible with other ingredients of the formulation. The term “composition” refers to a mixture that usually contains a carrier, such as a pharmaceutically acceptable carrier or excipient that is conventional in the art and which is suitable for administration into a subject for therapeutic, diagnostic, or prophylactic purposes. It may include a cell culture in which the polypeptide or polynucleotide is present in the cells or in the culture medium. For example, compositions for oral administration can form solutions, suspensions, tablets, pills, capsules, sustained release formulations, oral rinses or powders. The terms “pharmaceutical composition” and “formulation” are used interchangeably. The term “treatment” refers to any administration or application of remedies for disease in a mammal and includes inhibiting the disease, arresting its development, relieving the disease, for example, by causing regression, or restoring or repairing a lost, missing, or defective function; or stimulating an inefficient process. The term includes obtaining a desired pharmacologic and/or physiologic effect, covering any treatment of a pathological condition or disorder in a mammal. The effect may be prophylactic in terms of completely or partially preventing a disorder or symptom thereof and/or may be therapeutic in terms of a partial or complete cure for a disorder and/or adverse affect attributable to the disorder. It includes (1) preventing the disorder from occurring or recurring in a subject who may be predisposed to the disorder but is not yet symptomatic, (2) inhibiting the disorder, such as arresting its development, (3) stopping or terminating the disorder or at least its associated symptoms, so that the host no longer suffers from the disorder or its symptoms, such as causing regression of the disorder or its symptoms, for example, by restoring or repairing a lost, missing or defective function, or stimulating an inefficient process, or (4) relieving, alleviating or ameliorating the disorder, or symptoms associated therewith, where ameliorating is used in a broad sense to refer to at least a reduction in the magnitude of a parameter, such as inflammation, pain and/or tumor size. The term “disease” refers to any condition, infection, disorder or syndrome that requires medical intervention or for which medical intervention is desirable. Such medical intervention can include treatment, diagnosis and/or prevention. The term “therapeutically effective amount” refers to an amount which, when administered to a living subject, achieves a desired effect on the living subject. For example, an effective amount of the polypeptide of the invention for administration to the living subject is an amount that prevents and/or treats an integrin αvβ3-mediated disease. The exact amount will depend on the purpose of the treatment, and will be ascertainable by one skilled in the art using known techniques. As is known in the art, adjustments for systemic versus localized delivery, age, body weight, general health, sex, diet, time of administration, drug interaction and the severity of the condition may be necessary, and will be ascertainable with routine experimentation by those skilled in the art. EMBODIMENTS OF THE INVENTION When pharmaceutical compositions containing adalimumab (Humira®), including aqueous and lyophilized formulations of adalimumab are stored on a long-term basis, the activity of adalimumab can be lost or decreased due to aggregation and/or degradation. Thus, the present invention provides aqueous formulations of adalimumab that allow stable long-term storage of adalimumab, so that adalimumab is stable over the course of storage either in liquid or frozen states. The provided formulations do not require any extra steps such as rehydrating. Numerous embodiments of the present invention are explained in a greater detail below. Adalimumab All of the compositions of the present invention comprise adalimumab. As explained in the Background section of this application, adalimumab is a recombinant human IgG1 monoclonal antibody specific for human tumor necrosis factor (TNF). This antibody is also known as D2E7. Adalimumab consists of 1330 amino acids and has a molecular weight of approximately 148 kilodaltons. Adalimumab has been described and claimed in U.S. Pat. No. 6,090,382. The term “adalimumab” is also intended to mean so-called “bio-similar” and “bio-better” versions of the active adalimumab protein present in commercially available Humira®. Adalimumab suitable for storage in the present pharmaceutical composition can be produced by standard methods known in the art. For example, U.S. Pat. Nos. 6,090,382 and 8,216,583 describe various methods that a skilled artisan could use to prepare adalimumab protein for use in the formulations of the present invention. These methods are incorporated by reference herein. For example, adalimumab can be prepared by recombinant expression of immunoglobulin light and heavy chain genes in a host cell. Purification of the expressed adalimumab can be performed by any standard method. When adalimumab is produced intracellularly, the particulate debris is removed, for example, by centrifugation or ultrafiltration. When adalimumab is secreted into the medium, supernatants from such expression systems can be first concentrated using standard polypeptide concentration filters. Protease inhibitors can also be added to inhibit proteolysis and antibiotics can be included to prevent the growth of microorganisms. Adalimumab can be purified using, for example, hydroxyapatite chromatography, gel electrophoresis, dialysis, and affinity chromatography, and any combination of known or yet to be discovered purification techniques, including but not limited to Protein A chromatography, fractionation on an ion-exchange column, ethanol precipitation, reverse phase HPLC, chromatography on silica, chromatography on heparin SEPHAROSET®, an anion or cation exchange resin chromatography (such as a polyaspartic acid column), chromatofocusing, SDS-PAGE, and ammonium sulfate precipitation. I Formulations of Adalimumab with a Polyol and/or Surfactant, but without a Citrate/Phosphate Buffer In a first embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab; a stabilizer comprising at least one member selected from the group consisting of a polyol and a surfactant; and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said buffer does not comprise a combination of citrate and phosphate. In this embodiment, the stabilizer preferably comprises both polyol and surfactant. The pharmaceutical composition can comprise one, or any combination of two or more buffers, as long as it does not comprise both citrate and phosphate. The surfactant may be any pharmaceutically acceptable surfactant, preferably polysorbates (e.g., polysorbate 80) or poloxamers (e.g., Pluronic F-68). II Formulations of Adalimumab Using a Single Buffer System In a second embodiment, utilizing a single buffer system, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer system comprising a single buffering agent, said single buffering agent being selected from citrate, phosphate, succinate, histidine, tartrate or maleate, but not including combinations of the foregoing; wherein the formulation has a pH of about 4 to 8, and preferably about 5 to about 6. Histidine and succinate are particularly preferred for use as single buffering agents. It was surprisingly discovered that adalimumab compositions which comprise only one buffer (as opposed to two or more buffers) are more stable than adalimumab compositions comprising both a citrate buffer and a phosphate buffer. In the single buffer embodiment, adalimumab can be present at a concentration from about 20 to about 150 mg/ml, more preferably from about 20 to about 100 mg/ml, and even more preferably from about 30 to about 50 mg/ml. The buffer is present at a concentration from about 5 mM to about 50 mM. The pH of the compositions is between about 5 and about 6. The single buffer compositions of the invention may further comprise a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine, most preferably glycine, arginine and methionine. The salt is selected from the group consisting of sodium chloride and sodium sulfate. The metal ion is selected from the group consisting of zinc, magnesium and calcium. The compositions of the invention may further comprise a surfactant. The surfactant is a polysorbate surfactant or a poloxamer surfactant. Polysorbate surfactants include polysorbate 80, polysorbate 40 and polysorbate 20. A preferred polysorbate surfactant is polysorbate 80. Poloxamer surfactants include poloxamer 188 (also available commercially as Pluronic F-68). Most preferably, the surfactant is polysorbate 80. The single buffer composition may further comprise a polyol. Preferably, the polyol is a sugar alcohol; and even more preferably, the sugar alcohol is mannitol, sorbitol or trehalose. The single buffer adalimumab composition may also comprise a sugar, preferably sucrose, glucose or dextrose. In one embodiment of a single buffer adalimumab formulation, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to 50 μM, and succinate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. In another embodiment of a single buffer adalimumab formulation, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to 50 μM, and histidine at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. In a further embodiment of a single buffer adalimumab formulation, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to 50 μM, and either tartrate, maleate or acetate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. III Formulations of Adalimumab which Exclude Buffer In a third embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a stabilizer comprising at least one member selected from a polyol and a surfactant, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said composition is substantially free of a buffer. The term “free of buffer” should be understood to allow inclusion of the inherent buffering effect of the protein itself. In a buffer free formulation, the stabilizers referenced above may also be present (e.g. glycine, arginine and combinations thereof). IV Formulations of Adalimumab which Exclude Surfactant In a fourth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said composition is free or substantially free of a surfactant. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate; and (iii) the polyol is not mannitol at concentrations less than about 150 mM, but instead is selected from the group consisting of mannitol at concentrations exceeding about 150 mM, sorbitol and trehalose. V Formulations of Adalimumab which Exclude Polyol In a fifth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said composition is substantially free of polyol. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate. Additional Stabilizers Useful in Embodiments I Through V. Optionally, in each of the five embodiments summarized above, the composition may further comprise a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid stabilizer may be selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. The salt stabilizer may be selected from the group consisting of sodium chloride and sodium sulfate. The metal ion stabilizer may be selected from the group consisting of zinc, magnesium and calcium. Preferably, adalimumab formulations containing the stabilizers mentioned above also do not contain buffer systems in which phosphate buffer and citrate buffer are present in combination. Most preferably (i) the optional additional stabilizer present in this embodiment is not sodium chloride, and comprises at least one or both of arginine and glycine; (ii) the buffer, when present, contains no citrate and phosphate combination but is instead at least one of histidine and succinate; and (iii) the stabilizer when it includes a polyol is not mannitol unless in amounts greater than about 150 mM, and may also include trehalose and sorbitol. Preferably the amount of mannitol is greater than about 150 mM, and most preferably greater than about 200 mM. VI Formulations of Adalimumab Replacing Both Surfactant and Polyol with Other Stabilizers It has been further discovered that satisfactory stabilization can be attained when the stabilizers mentioned above are used in place of both polyol and surfactant, accordingly, in a sixth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, optionally a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, EDTA, and a metal ion, and wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said composition is free or substantially free of a polyol and surfactant. When buffer is present in this embodiment, it is especially preferred that (i) the buffer not include the combination of citrate and phosphate; (ii) the buffer is selected from the group consisting of histidine and succinate; and (iii) the stabilizer does not comprise sodium chloride, but instead is at least one member selected from the group consisting of arginine and glycine. It is also preferred that the buffer is free or substantially free of citrate buffer, as we have discovered that it is generally poorer in terms of stability contribution than other buffers, such as histidine and succinate. In each of the embodiments above at least one of the following advantageous conditions can be optionally present (unless stated as being required): (i) the buffer preferably does not contain a combination of citrate and phosphate, or is free or substantially free of citrate buffer (ii) the buffer preferably is at least one member selected from the group consisting of histidine and succinate; and (iii) the stabilizer preferably does not include sodium chloride, or if present is controlled to levels less than about 100 mM; (iv) the stabilizer is at least one member selected from the group consisting of arginine and glycine, including combinations thereof; and (v) the polyol is preferably not mannitol (unless mannitol is present in amounts greater than about 150 mM and preferably greater than about 200 mM) but may include sorbitol and trehalose. When using polyols for stabilization, mannitol is discovered herein to be destabilizing in comparison to sorbitol and trehalose unless the mannitol is present in amounts generally above about 150 to 200 mM. When using other stabilizers, it is discovered herein that sodium chloride is destabilizing compared to arginine or glycine, but we observe some stabilization when the levels of sodium chloride are controlled to less than about 100 mM and preferably less than about 75 mM. Preferably, adalimumab is present in the composition of the present invention at a concentration from about 20 to about 150 mg/ml, more preferably from about 20 to about 100 mg/ml, and even more preferably from about 30 to about 50 mg/ml. Buffer, if present, is present at a concentration from about 5 mM to about 50 mM. Surfactant, if present, is preferably a polysorbate (PS). In an even more preferred embodiment, the polysorbate is polysorbate 80 (PS 80). Poloxamer surfactants are also suitable (e.g., Pluronic® F-68). The polyol, if present, is a sugar alcohol. In an even more preferred embodiment, the sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose, and most preferably sorbitol and trehalose. Preferably, the polyol is at a concentration from about 1 to about 10%, more preferably, from about 2 to about 6%, and even more preferably from about 3 to 5%, wherein said values are weight by volume (w/v) of the total composition. A stabilizer, when present, can be selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid can be selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. The salt may be selected from the group consisting of sodium chloride and sodium sulfate. The metal ion may be selected from the group consisting of zinc, magnesium and calcium. Glycine and arginine are particularly preferred stabilizers. Zinc, magnesium and calcium, when present for stabilization, may be at a concentration from about 1 mM to about 100 mM, and more preferably from about 1 to about 10 mM. Glycine, or arginine, or combinations thereof, if present for stabilization, is at a total concentration of up to about 300 mM, and preferably about 150 to 300 mM. Methionine, if present for stabilization, is present at a concentration from about 1 to about 10 mg/ml, more preferably from about 1 mg/ml to about 5 mg/ml. Sodium chloride, if present for stabilization, is at a concentration from about 5 to about 150 mM, more preferably, from about 20 to about 140 mM, and even more preferably less than about 100 mM. Sodium sulfate, if present if present for stabilization, is at a concentration from about 5 to about 150 mM, more preferably, from about 20 to about 120 mM, and even more preferably from about 60 to about 100 mM. EDTA, if present for stabilization, is present at a concentration from about 0.01% to about 0.05%, more preferably from about 0.05% to about 0.25%, and even more preferably from about 0.08% to about 0.2%. Preferably, the pH of the composition is from about 5 to about 5.5; and even more preferably is about 5.2 to 5.4. In an example of Embodiment I and II, above, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sorbitol or trehalose at a concentration from about 1 to 10% weight by volume, polysorbate 80 at a concentration from about 1 to 50 μM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM to about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and provided said composition is free or substantially free of citrate/phosphate buffer combination. Further, we rank citrate as the poorest of buffers, and preferably avoid it although it is still within the scope of the invention to formulate stable formulations of adalimumab that include citrate buffer, if not the combination thereof with phosphate. In an example of Embodiment IV, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sorbitol or trehalose at a concentration from about 1 to 10% weight by volume, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM to about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a surfactant and, optionally, and preferably, free or substantially free of citrate/phosphate buffer combination. In an example of Embodiment VI, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, glycine at a concentration from about 20 to about 200 mM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM to about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is free or substantially free polyol; surfactant (e.g. PS8) is preferably, but optionally present; and the composition is, optionally, and preferably, free or substantially free of citrate/phosphate buffer combination. In a further example of Embodiment VI, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, arginine or glycine at a concentration from about 1 to about 250 mM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of polyol. Surfactant (e.g. PS80) is preferably but optionally present, and the composition is, optionally, and preferably, free or substantially free of citrate/phosphate buffer combination. In a further example of Embodiment VI, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is free or substantially free of a polyol. Surfactant (e.g. PS80) is preferably but optionally present; and the composition is, optionally, and preferably, free or substantially free of citrate/phosphate buffer combination. In an example of Embodiment V, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, polysorbate 80 at a concentration from about 1 to 50 μM, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate buffer, at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is free or substantially free of a polyol and, optionally, and preferably, free or substantially free of citrate/phosphate buffer. In an example of Embodiments I and II, with additional stabilization, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, sorbitol or trehalose at a concentration from about 1 to about 10% weight by volume, EDTA at a concentration from about 0.01% to about 0.5%, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate, as a sole buffer, at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, and wherein the composition is free, or substantially free of citrate/phosphate buffer combination. In a further example of Embodiments I and II, with additional stabilization, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, sorbitol or trehalose at a concentration from about 1 to about 10% weight by volume, methionine at a concentration from about 1 to about 10 mg/ml, %, and at least one of succinate, histidine, phosphate, tartrate, maleate or citrate at a concentration from about 5 mM and about 50 mM wherein said composition has a pH of about 5 to about 5.5, wherein the composition is free or substantially free of any citrate/phosphate buffer combination. In a further example of Embodiments I and II, with additional amino acid stabilization, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol, sorbitol or trehalose (preferably sorbitol) at a concentration from about 1 to about 10% weight by volume, and amino acid that is preferably one and not both of (a) arginine at a concentration from about 1 to about 250 mg/ml, and (b) glycine at a concentration of about 20 to 200 mg/ml, and histidine buffer or succinate buffer at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5; and wherein the composition is free or substantially free of any citrate/phosphate buffer combination. In a further example of Embodiment IV, with additional amino acid stabilization, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, arginine at a concentration from about 1 to about 250 mg/ml, glycine at a concentration of about 20 to 200 mg/ml, and histidine buffer or succinate buffer at a concentration from about 5 mM to about 50 mM, and wherein said composition has a pH of about 5 to about 5.5 and is free or substantially free of polyol; and, optionally, wherein the composition is preferably free of any citrate/phosphate buffer combination. Numerous embodiments of the adalimumab formulations of the present invention were prepared in eight separate blocks of experiments, referred to herein as “Block A” through “Block H.” Each block had 12 to 16 different formulations that were exposed to accelerated storage conditions, 1 week at 40′C and 2 weeks at 25′C. For each time point the chemical and physical stability of the adalimumab protein was measured by SEC, RP, UV, pH, CE-IEF and CE-SDS. Materials and Methods 1. Equipment Used in the Formulation Studies Equipment Manufacture Model Serial Number Balance Sartorius CPA124S 23350022 pH meter Denver Model 250 E25006B100 Instrument UV Cary Bio 100 EL07103025 HPLC Dionex 3 Ultimate 3000 UPLC 8047439 HPLC Dionex 2 Ultimate 3000, 8036991 UPLC Beckman Beckman P/ACE 455436 CE Agilent CE Agilent 3DCE 1600A 3546G00736 Rocker Labnet Orbit P4 8091840 Plate 2. Chemicals and Materials Used in the Formulation Studies Chemical/Materials Producer Purity Lot Number: Citrate Mallinckrodt ACS H28475 Phosphate Fisher FCC 103372 Fisher ACS 113670 Succinate Spectrum Reagent ZM0462 Histidine Spectrum USP XV0239 Spectrum USP ZG0216 Tartrate Spectrum FCC 1BC0152 Maleate TCI >99% 206-738-1 Mannitol BDH USP 57910 Glycine Spectrum FCC YM3312 Spectrum FCC 1BJ0243 Fisher Tissue 070082 Grade Arginine Spectrum USP 2AK0238 Spectrum USP 1CB0771 Sodium Chloride Mallinckrodt ACS J52619 Macron USP 26434 Polysorbate 80 Sigma-Aldrich Low 028K5309 Peroxide Sorbitol Spectrum NF 1AH0521 Trehalose Spectrum N/A 1AE0739 Acetate Mallinckrodt FCC H31613 EDTA Sigma 98.5% 057K00071 Methionine Spectrum USP ZF0377 F-68 Sigma Cell Culture 057K00331 Polysorbate 20 Spectrum NF 1AE0882 Sodium dodecyl sulfate Fluka ACS 1344034 Tris base Fisher ACS S61374 2-mercaptoethanol Fisher Electrophoresis 107667 Part Material/Reagents Number Supplier Slide-A-Lyzers 7K cutoff 66373 Thermo Mini Dialysis Units 69550 Thermo Millex ®-GV 0.22 μM, Filter SLGV004SL Millipore 1 mL Vials 4500050375 SCHOTT cIEF Gel Polymer Solution 477497 Beckman Coulter pI Marker Kit A58481 Beckman Coulter Pharmalyte 3-10 ampholyte 17-0456-01 GE Healthcare Fused silica capillary (50 μm TSP050375 Polymicro i.d.) SDS-MW gel buffer A10663 Beckman 10 kD internal standard A26487 Beckman 3. HPLC Columns Used in the Formulation Studies Column Company Part # Lot Poroshell 300SB- Agilent 660750-906 USZW003083 C8, 2.1 × 75 mm, 5um Poroshell 300SB- Agilent 660750-906 USZW003073 C8, 2.1 × 75 mm, 5um ACQUITY UPLC BEH200 Waters 186005225 138123331 SEC, 1.7 um Column, 4.6 × 150 mm ACQUITY UPLC BEH200 Waters 186005225 01471130951 SEC, 1.7 um Column, 4.6 × 150 mm Processing of Humira®. Block A experiments used adalimumab present in commercially available Humira®. Humira® material was dialyzed as follows: 100 μL of Humira® was placed into Mini Dialysis units with a 3.5 MWCO and dialyzed in 1 L of formulation buffer for 24 hours at 4 to 8° C. A few samples did experience a small increase in volume due to the dialysis, but never to extent that the concentration of the polysorbate 80 dropped below the CMC (critical micelle concentration). The protein concentration for each formulation was measured by UV absorbance spectroscopy, using an calculated experimental molar absorptivity based on reported concentration of Humira®, 50 mg/mL. For a number of the formulations the protein concentration was adjusted by using a spin concentrator. The sample was placed in the spin concentrator and rotated at 14,000 RPM for 30 to 60 secs. The protein concentration was then checked with UV. After the targeted protein concentration around 50 mg/mL was reached the samples were filtered through a 0.22 μM sterile filter into sterile vials in a biosafety hood. The samples were then placed on stability at 40° C. for one and two weeks. Processing of a Proprietary Adalimumab Protein. The formulation studies described herein used a proprietary adalimumab biosimilar protein which did not contain polysorbate 80. The material was dialyzed using 7,000 MWCO Slide-A-Lyzers in different formulation buffers for 24 hours at a temperature range between 4 to 8° C. After dialysis the protein concentration was measured by UV and sample pH was measured. The target concentration of samples was 50±2.5 mg/mL, which was adjusted if the sample concentration fell out of the above range. Some of the samples did experience an increase in sample volume do to dilution, requiring the concentration of the protein to increase. For these samples the protein concentration was increased by using spin concentrators, usually at 14,000 rpm for 30 to 60 secs. The pH of a number of samples were adjusted using 1M NaOH or 1M HCl to reach the target pH of 5.2. After the targeted protein concentration and pH of the samples were determined to be within experimental parameters, the samples were filtered through a 0.22 μM sterile filter into sterile vials in a biosafety hood. The samples were then placed on stability at 40° C. for one week and 25° C. for two weeks. Freeze-Thaw Conditions: The freeze thaw samples were prepared on the day of analysis to match with t=0. The samples were frozen at −80° C. between 3 to 7 minutes. The frozen sample was then thawed at room temperature until all the ice had thawed. The freeze and thaw cycle was repeated 5 times for each sample. Agitation Studies. The samples were aggregated at 150 rpm for 24 hours at 4° C. on a rockerplate. A control was prepared and placed next to the rocker plate for each sample that underwent agitation. pH Measurements. The pH each sample was measured using a micro-pH probe. Before the start of analysis the pH probe was calibrated with three pH standards ordered from fisher. The pH values of the stability samples were measured by transferring 60 μL of each stability sample to 100 μL PCR tube. The micro-pH probe was then submerged into the sample and after the value stabilized it was recorded. UV Absorbance Spectroscopy. UV spectroscopy was used to measure the protein concentration in the samples. The mole extinction coefficient at 280 nm for bulk substance was 1.6355 mg/mL, which was determined experiential. The protein concentrations of the all formulations for LB-140 were measured using a cell path length of 0.0096 cm. Below is the analysis parameters used for LB-140. Scan Range: 400 to 200 nm Average Time (min): 0.1 Date Interval (nm): 1 Scan Rate (nm/min): 600 Cycle Count: 5 Size Exclusion Chromatography (SEC) Method. The SEC method used to analyze the LB-140 stability samples was developed at Legacy BioDesign. Below is a brief summary of the SEC method parameter used for the analysis of the LB-140 samples. Method Parameters Column Information: ACQUITY UPLC BEH200 SEC, 1.7 urn Column, 4.6×150 mm Analysis Buffer: 50 mM Phosphate, 250 mM NaCl, pH 6.8 Flow rate: 0.3 mL/min Column temperature: 30° C. Detection: 280 nm Injection volume: 2 μL Sample temperature: Approx. 5° C. RP HPLC Method. The RP HPLC method was found to be stability indicating and was used to analyze LB-140 stability samples. Below is a summary of the RP method parameter used for the analysis of the LB-140. Method Parameters Column Information: Poroshell 300SB-C8, 2.1×75 mm, 5 um Mobile Phase A: 98% (v/v) H2O/2% (v/v) IPA/0.1% (v/v) TFA Mobile Phase B: 10% (v/v) H2O/70% (v/v) IPA/20% (v/v) ACN/0.1% (v/v) TFA Flow rate: 0.25 mL/min Column temperature: 80° C. Detection: 225 nm Injection volume: 1 μL Sample temperature: Approx. 5° C. Run time: 15 minutes Gradient: Time % A % B 0 100 0 10 50 50 10.1 100 0 15 100 0 CE-IEF Analysis. Capillary isoelectric focusing (cIEF) was conducted as described in the PA 800 plus Application Guide published by Beckman Coulter. A more detailed description can be found in a research article published by Mack et al1. All analyses were conducted using a Beckman Coulter P/ACE MDQ system (Beckman Coulter, Inc.; Brea, Calif.) operated at ambient temperature with a 30 cm total length (20 cm effective) neutral capillary. The neutral capillary was prepared by immobilizing poly(acrylamide) to the capillary wall using a method described by Gao et al.2 cIEF samples were prepared by mixing the protein of interest at 0.25 mg/mL with a mixture of 3M urea-cIEF gel containing ampholyte, cathodic stabilizer, anodic stabilizer, and pl markers. Sample was pressure injected at 9.5 psi into the capillary for 4.1 min, after which time it was focused by applying a voltage of 25 kV for 15 min between analyte and catholyte. This step was followed by chemical mobilization at 30 kV for 30 min between analyte and chemical mobilizer. The pl markers and the protein of interest were detected with absorbance at 280 nm during the mobilization step. The pl of the protein was calculated from the resultant regression equation of pl vs. first peak moment obtained from the pl standards. CE-SDS Analysis. Analysis by CE-SDS was conducted under reducing conditions utilizing a method adapted from the SOP published by Beckman-Coulter for determining IgG purity/heterogeneity. Briefly, the antibody was diluted with DDI water to 6 mg/mL, denatured by adding sample buffer (0.1 M Tris/1.0% SDS, pH 8.0), and reduced via addition of 2-mercaptoethanol; the final antibody concentration was 1.2 mg/mL. Denaturing and reduction was facilitated by heating the sample at 70° C. for 10 min. The sample was cooled for 10 min at room temperature prior to analysis. A centrifuge step (300 g, 5 min) was employed prior to heating the sample and directly after the cooling it. CE analysis was conducted using a Beckman Coulter P/ACE MDQ system operated at ambient temperature with a 30 cm total length (20 cm effective, 50 μm i.d.) capillary. Prior to sample introduction, the capillary was sequentially rinsed with 0.1 M NaOH, 0.1M HCL, DDI water, and SDS-gel buffer solution. Sample was injected electrokinetically at 5 kV for 30 s followed by separation at 30 kV for 30 min. For both injection and separation, the instrument was operated in reverse polarity mode. Antibody fragments were detected using absorbance at 214 nm (4 Hz acquisition) and time-normalized areas reported for measured peaks. Block a Formulation Studies The Block A studies examined different buffer systems and used a commercially available adalimumab material which was reprocessed for these studies. We note that U.S. Pat. No. 8,216,583 references stability of an adalimumab formulation in relation to use of a citrate/phosphate buffer system at pH 5.2, and in fact the patent required the use of such a buffer combination. The work we have done, reflected here, indicates that citrate/phosphate is in fact a rather poor buffer choice in comparison to others such as histidine and succinate. In the Block A studies below, pH was kept constant at 5.2. The concentrations of mannitol and polysorbate 80 were also held constant. Samples were kept at 40° C. for two weeks. The study design is summarized in the Table below. TABLE A BLOCK A STUDY DESIGN PS Form Citrate Phosphate Succinate Histidine Tartrate Maleate Mannitol 80 No. API (mM) (mM) (mM) (mM) (mM) (mM) (mM) (%) 1 Humira ® 8 18 0 0 0 0 12 0.1 2 Humira ® 10 0 0 0 0 0 12 0.1 3 Humira ® 0 10 0 0 0 0 12 0.1 4 Humira ® 0 0 10 0 0 0 12 0.1 5 Humira ® 0 0 0 10 0 0 12 0.1 6 Humira ® 0 0 0 0 10 0 12 0.1 7 Humira ® 0 0 0 0 0 10 12 0.1 Analysis by SEC showed that the formulation with citrate alone performed more poorly than the buffer combination (Table A), indicating that the phosphate was the primary stabilizer in that combination. This was surprising and unexpected, as this pH is outside of the nominal buffering capacity range of phosphate, but well within the buffering range for citrate. Furthermore, succinate, histidine, and tartrate did as well or better than the citrate/phosphate combination, indicating that other buffer systems would provide equal or superior stability for adalimumab. Accordingly, the present invention in one of its embodiments is directed to adalimumab formulations exhibiting long term stability, wherein a buffer combination of citrate and phosphate is avoided in favor of at least one buffer selected from the group consisting of histidine, phosphate, succinate and tartrate. Acetate is also a suitable replacement for the citrate phosphate buffer combination. The purity of these stored samples was checked using RP HPLC (FIG. 2). As with SEC, the citrate formulation exhibited the poorest stability, while all of the other buffers did as well or better than the buffer combination found in commercially available adalimumab (Humira®). These results demonstrate our discovery that changing the buffer (i.e. avoiding the citrate/phosphate buffer combination of the commercial adalimumab) could improve the stability profile of adalimumab. Block B Formulation Studies A second study (“BLOCK B”) was conducted examining just changes in the buffer species, where the pH (5.2) was not changed, as outlined in the table below labeled “BLOCK B Study Design. In this case, the commercially available formulation for Humira® was used as a control, while all of the other formulations employed a proprietary adalimumab biosimilar protein. Table B-1, below summarizes the percent monomer for the Block B formulations (as well the percentage amount of an impurity determined to be a fragment of the adalimumab protein). TABLE B BLOCK B STUDY DESIGN PS Form Citrate Phosphate Succinate Histidine Tartrate Maleate Mannitol 80 No. API (mM) (mM) (mM) (mM) (mM) (mM) (mM) (%) 1 Humira ® 8 18 0 0 0 0 12 0.1 2 Adalimumab 10 0 0 0 0 0 12 0.1 biosimilar 3 Adalimumab 0 10 0 0 0 0 12 0.1 biosimilar 4 Adalimumab 0 0 10 0 0 0 12 0.1 biosimilar 5 Adalimumab 0 0 0 10 0 0 12 0.1 biosimilar 6 Adalimumab 0 0 0 0 10 0 12 0.1 biosimilar 7 Adalimumab 0 0 0 0 0 10 12 0.1 biosimilar TABLE B-1 Percent monomer for Block B formulations at t0 and after two weeks at 40 C. (t2) Form Monomer Monomer Fragment Fragment No. API Buffer (t0) (t2) (t0) (t2) 1 Humira ® Citrate/phosphate 99.34 0.26 2 Adalimumab citrate 98.71 97.92 0.62 0.40 biosimilar 3 Adalimumab phosphate 99.21 98.07 0.05 0.30 biosimilar 4 Adalimumab succinate 99.19 98.04 0.04 0.31 biosimilar 5 Adalimumab histidine 99.19 98.41 0.07 0.23 biosimilar 6 Adalimumab tartrate 99.13 98.10 0.04 0.29 biosimilar 7 Adalimumab maleate 98.91 97.90 0.36 0.76 biosimilar As can be seen from Table B-1 above, upon storage for two weeks at 40 C, the monomer content decreases by more than 1% for all of the samples in Block B, except for the one containing histidine (His) buffer (Table B-1). From this study we discovered the likelihood that His would be a superior buffer system for adalimumab. (We note that the fragment level measured by SEC reported for Formulation 2 appears to be incorrect as all of the other initial fragment s levels are less than 0.1%.) Block C Formulation Studies A large-scale formulation screening study was carried out in the studies conducted in Block C (See Table C, below). Samples were stored for one week at 40 C (hereinafter referenced as “t1”) or two weeks at 25 C (hereinafter referenced as “t2”). These conditions were used throughout the remainder of our studies, so this terminology will be employed throughout the present detailed discussion. Block C was designed to expand on the buffer assessment conducted in Block B. In addition, it examined glycine (Gly) and/or arginine (Arg) as possible stabilizers in place of mannitol and/or NaCl (Table C). Note that the buffer system used in the Humira® product employs the 8 mM citrate/18 mM phosphate buffer, which is the composition of Formulation 1 of Block C. In this case, a proprietary adalimumab biosimilar protein was used for formulation 1 of Block C, instead of adalimumab protein obtained from commercially available Humira®. TABLE C BLOCK C STUDY DESIGN Form No. API citrate phosphate succinate histidine glycine arginine mannitol NaCl 1 Adalimurnab 8 18 0 0 0 0 65 100 biosimilar 2 Adalimumab 18 8 0 0 0 0 65 100 biosimilar 3 Adalimumab 20 0 0 0 0 0 65 100 biosimilar 4 Adalimumab 20 0 0 0 65 0 0 100 biosimilar 5 Adalimumab 0 20 0 0 65 0 0 100 biosimilar 6 Adalimumab 20 0 0 0 0 65 0 100 biosimilar 7 Adalimurnab 0 20 0 0 0 65 0 100 biosimilar 8 Adalimurnab 0 0 20 0 65 0 0 100 biosimilar 9 Adalimumab 0 0 20 0 0 65 0 100 biosimilar 10 Adalimumab 0 0 0 20 65 0 0 100 biosimilar 11 Adalimurnab 0 0 0 20 0 65 0 100 biosimilar 12 Adalimumab 0 20 0 0 0 130 0 35 biosimilar 13 Adalimumab 0 0 20 0 0 130 0 35 biosimilar 14 Adalimurnab 0 0 0 20 0 130 0 35 biosimilar 15 Adalimumab 0 20 0 0 130 0 0 60 biosimilar 16 Adalimumab 0 20 0 20 130 0 0 60 biosimilar TABLE C-1 Measured pH for Block C formulations at t0 and t1 (one week, 40° C.) Form pH pH No. citrate phosphate succinate histidine glycine arginine mannitol NaCl t0 t2 1 8 18 0 0 0 0 65 100 5.51 5.57 2 18 8 0 0 0 0 65 100 5.46 5.43 3 20 0 0 0 0 0 65 100 5.28 5.27 4 20 0 0 0 65 0 0 100 5.27 5.24 5 0 20 0 0 65 0 0 100 5.43 5.44 6 20 0 0 0 0 65 0 100 5.29 5.29 7 0 20 0 0 0 65 0 100 5.28 5.32 8 0 0 20 0 65 0 0 100 5.22 5.17 9 0 0 20 0 0 65 0 100 5.19 5.16 10 0 0 0 20 65 0 0 100 5.28 5.30 11 0 0 0 20 0 65 0 100 5.26 5.29 12 0 20 0 0 0 130 0 35 5.24 5.24 13 0 0 20 0 0 130 0 35 5.18 5.16 14 0 0 0 20 0 130 0 35 5.28 5.35 15 0 20 0 0 130 0 0 60 5.31 5.31 16 0 20 0 20 130 0 0 60 5.36 5.40 TABLE C-2 Monomer content by SEC for formulations in Block C at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. citrate phosphate succinate His Gly Arg mannitol NaCl t0 t1 t2 1 8 18 0 0 0 0 65 100 98.75 97.90 98.06 2 18 8 0 0 0 0 65 100 99.26 98.22 98.80 3 20 0 0 0 0 0 65 100 99.28 98.32 98.78 4 20 0 0 0 65 0 0 100 99.36 98.45 99.03 5 0 20 0 0 65 0 0 100 99.25 98.20 98.77 6 20 0 0 0 0 65 0 100 99.42 98.68 99.10 7 0 20 0 0 0 65 0 100 99.39 98.59 99.13 8 0 0 20 0 65 0 0 100 99.41 98.51 99.04 9 0 0 20 0 0 65 0 100 99.36 98.52 98.96 10 0 0 0 20 65 0 0 100 99.41 98.66 99.15 11 0 0 0 20 0 65 0 100 99.37 98.70 99.15 12 0 20 0 0 0 130 0 35 99.41 98.66 99.14 13 0 0 20 0 0 130 0 35 99.42 98.71 99.17 14 0 0 0 20 0 130 0 35 99.40 98.75 99.26 15 0 20 0 0 130 0 0 60 99.32 98.53 99.05 16 0 20 0 20 130 0 0 60 99.40 98.66 99.19 TABLE C-3 Percent purity by RP HPLC for formulations in Block C at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. citrate phosphate succinate His Gly Arg mannitol NaCl t0 t1 t2 1 8 18 0 0 0 0 65 100 98.04 97.92 98.10 2 18 8 0 0 0 0 65 100 97.94 97.83 98.03 3 20 0 0 0 0 0 65 100 98.03 97.92 98.00 4 20 0 0 0 65 0 0 100 97.94 97.75 97.98 5 0 20 0 0 65 0 0 100 97.98 97.69 97.95 6 20 0 0 0 0 65 0 100 97.89 97.72 97.92 7 0 20 0 0 0 65 0 100 97.80 97.70 97.91 8 0 0 20 0 65 0 0 100 97.98 97.77 98.01 9 0 0 20 0 0 65 0 100 97.98 97.73 97.94 10 0 0 0 20 65 0 0 100 97.98 97.76 98.00 11 0 0 0 20 0 65 0 100 97.87 97.78 97.97 12 0 20 0 0 0 130 0 35 97.88 97.71 97.95 13 0 0 20 0 0 130 0 35 97.95 97.62 97.93 14 0 0 0 20 0 130 0 35 97.98 97.72 98.04 15 0 20 0 0 130 0 0 60 97.91 97.72 97.96 16 0 20 0 20 130 0 0 60 98.00 97.79 97.78 TABLE C-4 Percentage of main bands seen in the cIEF profile of formulations in Block C at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. pH t0 t1 t2 1 8.59 1.94 1.97 1.82 8.43 11.76 11.30 12.49 8.27 58.29 49.88 51.54 8.20 7.18 7.59 8.05 21.49 22.38 19.79 7.86 6.53 5.35 4.66 2 8.60 1.96 1.84 8.44 12.08 10.89 8.29 51.70 47.63 8.22 9.74 12.32 8.09 16.29 18.25 7.91 3.50 3.64 3 8.60 1.83 1.82 1.12 8.43 11.58 9.67 10.40 8.27 45.80 32.99 44.04 8.20 12.44 22.27 18.68 8.01 17.57 16.21 14.40 7.86 4.39 3.61 4 8.57 2.31 2.04 2.13 8.41 12.94 11.51 12.62 8.25 33.37 59.98 61.97 8.20 23.03 8.02 15.21 18.33 16.07 7.88 3.45 5.32 3.70 5 8.58 2.40 2.00 2.30 8.41 13.01 11.02 12.34 8.25 42.09 46.32 37.30 8.21 15.58 10.65 15.80 8.03 18.48 20.58 16.80 7.86 3.74 6.13 4.83 6 8.57 2.83 8.38 13.17 13.23 8.23 32.66 31.18 8.18 17.52 18.54 8.02 17.48 13.82 7.91 5.30 5.83 7 8.58 2.08 2.41 2.64 8.44 13.42 12.64 12.63 8.27 56.79 52.48 54.76 8.16 5.36 6.16 6.38 8.04 16.91 20.09 18.45 7.94 5.44 4.12 5.15 8 8.57 1.76 2.37 1.55 8.44 14.41 12.13 11.61 8.29 60.01 48.87 52.94 8.19 7.07 10.66 8.10 16.22 16.55 17.10 7.95 7.61 5.02 4.55 9 8.58 2.19 2.06 0.99 8.41 11.69 10.64 12.73 8.26 50.07 44.21 60.33 8.19 10.66 10.39 8.01 15.62 21.51 17.79 7.87 4.67 5.37 8.16 10 8.57 1.78 2.64 1.62 8.41 10.55 10.95 8.11 8.25 43.82 42.93 36.11 8.21 15.96 15.24 17.66 8.02 14.63 14.58 14.22 7.88 3.82 4.21 3.95 11 8.58 1.59 1.81 1.89 8.41 12.98 11.58 12.86 8.23 62.74 29.63 12.00 8.19 22.86 34.77 8.02 17.15 19.52 17.06 7.87 5.54 5.56 4.77 12 8.61 0.35 1.57 1.47 8.35 13.24 13.41 8.83 8.19 43.18 60.12 26.52 8.15 15.43 20.46 25.60 7.98 16.74 17.38 7.88 4.96 4.44 4.99 13 8.58 1.71 1.67 8.41 11.63 10.01 8.26 49.19 42.65 8.20 14.25 16.64 8.03 17.35 18.12 7.86 4.28 4.18 14 8.56 1.64 1.79 1.73 8.39 13.17 10.45 10.96 8.25 58.68 46.06 45.60 8.21 11.03 13.34 8.07 14.10 20.24 14.50 7.92 2.10 5.13 4.28 15 8.57 1.74 1.22 1.60 8.41 10.49 15.21 10.78 8.25 46.06 55.05 44.98 8.20 14.46 13.79 8.02 13.90 20.31 10.79 7.89 4.23 4.90 3.43 16 8.56 1.96 1.08 8.40 9.25 12.23 12.58 8.24 38.08 31.03 58.61 8.20 19.02 22.08 21.50 8.03 12.00 13.24 7.31 7.89 4.73 4.82 TABLE C-5 Percentage of bands for light chain (LC), heavy chain (HC), non-glycosylated HC, and other species for formulations in Block C at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 35.87 63.20 0.51 0.42 t1 29.71 63.08 0.37 6.84 t2 31.01 67.83 0.54 0.61 2 t0 29.50 69.57 0.56 0.37 t1 30.51 67.28 0.56 1.65 t2 32.32 65.51 0.56 1.61 3 t0 32.53 66.45 0.54 0.47 t1 33.04 65.34 0.55 1.07 t2 31.94 66.60 0.57 0.90 4 t0 33.40 64.90 0.46 1.24 t1 30.96 67.16 0.52 1.36 t2 32.08 65.84 0.56 1.52 5 t0 34.17 63.89 0.49 1.45 t1 33.60 64.27 0.56 1.57 t2 32.15 66.20 0.48 1.17 6 t0 37.91 60.35 0.54 1.19 t1 34.80 62.88 0.73 1.59 t2 32.90 65.62 0.50 0.99 7 t0 32.17 66.80 0.55 0.49 t1 29.83 68.33 0.59 1.25 t2 33.32 65.97 0.55 0.15 8 t0 33.83 65.51 0.49 0.17 t1 30.37 68.48 0.58 0.57 t2 32.86 66.40 0.55 0.19 9 t0 30.69 69.31 0.00 0.00 t1 34.30 64.24 0.52 0.94 t2 29.08 69.87 0.62 0.43 10 t0 38.68 59.95 0.57 0.80 t1 36.52 58.65 0.00 4.83 t2 43.68 54.39 1.92 0.00 11 t0 35.25 59.00 1.75 4.00 t1 30.71 67.58 0.66 1.05 t2 30.18 67.14 0.47 2.21 13 t0 44.58 55.42 0.00 0.00 t1 37.73 60.75 0.25 1.28 t2 38.05 61.44 0.52 0.00 14 t0 32.50 66.66 0.60 0.24 t1 30.91 67.77 0.61 0.70 t2 29.14 70.32 0.23 0.31 15 t0 30.07 68.95 0.63 0.35 t1 30.14 68.49 0.62 0.75 t2 31.57 67.55 0.62 0.26 16 t0 30.54 68.61 0.63 0.22 t1 29.81 68.81 0.63 0.75 t2 29.46 69.14 0.59 0.81 Discussion of Block C Results Referring to Table C-1 above, the pH was measured and found to be relatively stable for all of the formulations. However, the initial pH values were slightly higher for the citrate/phosphate formulations. The least stable formulation by SEC analysis appears to be Formulation 1, the one using the Humira® buffer system. By comparison we discovered that formulations using His as the buffer and/or formulations containing Gly or Arg exhibited the greatest stability (See Table C-2). Similar trends are seen when the purity by RP HPLC is considered (See Table C-3). It appears that SEC may be a better stability-indicating method than RP HPLC, although, when taken as a whole, the RP HPLC method does appear to be stability-indicating. Based on the Block C data summarized above, we have discovered that Histidine is suitable as a preferred buffer in terms of formulation stability, and that glycine or arginine, or combinations thereof, are also stability enhancing components for inclusion in an adalimumab formulation. The stored samples were further analyzed by cIEF at t1 and t2 (Table C-4 above). A proprietary adalimumab material exhibit four to five peaks with integrated intensities above 1% or so. In general, there are some small decreases in the intensity of the main peak upon storage. These losses are usually greater at t1 than at t2. Still, no significant new peaks are observed, suggesting that there is minimal chemical degradation occurring that would lead to changes in the overall charge on the protein. The variance in the data indicates that this method, while useful for characterization, does not appear to be stability-indicating. The final analytical method used to evaluate the stability of adalimumab formulation is CE-SDS, which is essentially the CE version of SDS-PAGE slab gels. This method indicates that the relative areas of the LC peak do decrease when stored at elevated temperatures (Table C-5), while the amount of new peaks (cumulatively called ‘Other’) increases. Altogether, these changes are usually less than 2% for any of the formulations. There are some samples where the percentage of ‘Other’ is in the 4-6% range, but these are likely artifacts. Block D Formulation Studies Another set of formulations were evaluated as “Block D.” Sixteen formulations were designed to evaluate other stabilizers as alternatives to mannitol, such as sorbitol and trehalose (See Table D). Block D also examined using mannitol or NaCl as the sole tonicity agent, instead of using a mixture of the two excipients. The pH stability of the formulations was quite good, although the actual initial pH values were slightly lower than the target values for some formulations (Table D-1). TABLE D BLOCK D STUDY DESIGN Form No. API citrate phosphate sorbitol trehalose mannitol NaCl PS 80 1 Adalimumab 8 18 0 0 65 100 0.1 biosimilar 2 Adalimumab 8 18 0 0 65 100 0 biosimilar 3 Adalimumab 20 0 0 0 65 100 0.1 biosimilar 4 Adalimumab 20 0 0 0 65 100 0 biosimilar 5 Adalimumab 0 20 0 0 65 100 0.1 biosimilar 6 Adalimumab 0 20 0 0 65 100 0 biosimilar 7 Adalimumab 8 18 65 0 0 100 0.1 biosimilar 8 Adalimumab 8 18 0 65 0 100 0.1 biosimilar 9 Adalimumab 0 20 65 0 0 100 0.1 biosimilar 10 Adalimumab 0 10 0 0 240 0 0.1 biosimilar 11 Adalimumab 0 10 240 0 0 0 0.1 biosimilar 12 Adalimumab 0 10 0 240 0 0 0.1 biosimilar 13 Adalimumab 10 0 0 0 0 150 0.1 biosimilar 14 Adalimumab 10 0 0 0 0 150 0 biosimilar 15 Adalimumab 0 10 0 0 0 150 0.1 biosimilar 16 Adalimumab 0 10 0 0 0 150 0 biosimilar TABLE D-1 Measured pH for Block D formulations at t0 and t1 (one week, 40° C.) Form PS No. API citrate phosphate sorbitol trehalose mannitol NaCl 80 t0 t1 t2 1 Adalimumab 8 18 0 0 65 100 0.1 5.09 5.17 5.12 biosimilar 2 Adalimumab 8 18 0 0 65 100 0 5.12 5.16 5.16 biosimilar 3 Adalimumab 20 0 0 0 65 100 0.1 5.11 5.16 5.14 biosimilar 4 Adalimumab 20 0 0 0 65 100 0 5.13 5.17 5.18 biosimilar 5 Adalimumab 0 20 0 0 65 100 0.1 5.19 5.25 5.24 biosimilar 6 Adalimumab 0 20 0 0 65 100 0 5.16 5.24 5.17 biosimilar 7 Adalimumab 8 18 65 0 0 100 0.1 5.14 5.17 5.18 biosimilar 8 Adalimumab 8 18 0 65 0 100 0.1 5.15 5.21 5.16 biosimilar 9 Adalimumab 0 20 65 0 0 100 0.1 5.19 5.29 5.28 biosimilar 10 Adalimumab 0 10 0 0 240 0 0.1 5.23 5.28 5.27 biosimilar 11 Adalimumab 0 10 240 0 0 0 0.1 5.45 5.35 5.33 biosimilar 12 Adalimumab 0 10 0 240 0 0 0.1 5.44 5.32 5.31 biosimilar 13 Adalimumab 10 0 0 0 0 150 0.1 5.30 5.25 5.23 biosimilar 14 Adalimumab 10 0 0 0 0 150 0 5.39 5.20 5.18 biosimilar 15 Adalimumab 0 10 0 0 0 150 0.1 5.35 5.30 5.22 biosimilar 16 Adalimumab 0 10 0 0 0 150 0 5.41 5.33 5.28 biosimilar TABLE D-2 Monomer content by SEC for formulations in Block D at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. API citrate phosphate sorbitol trehalose mannitol NaCl 80 t0 t1 t2 1 Adalimumab 8 18 0 0 65 100 0.1 99.28 98.21 98.96 biosimilar 2 Adalimumab 8 18 0 0 65 100 0 99.25 98.11 98.85 biosimilar 3 Adalimumab 20 0 0 0 65 100 0.1 99.25 98.16 98.86 biosimilar 4 Adalimumab 20 0 0 0 65 100 0 99.27 98.26 98.92 biosimilar 5 Adalimumab 0 20 0 0 65 100 0.1 99.24 98.16 98.84 biosimilar 6 Adalimumab 0 20 0 0 65 100 0 99.21 98.23 98.82 biosimilar 7 Adalimumab 8 18 65 0 0 100 0.1 99.30 98.19 98.94 biosimilar 8 Adalimumab 8 18 0 65 0 100 0.1 99.28 98.14 98.85 biosimilar 9 Adalimumab 0 20 65 0 0 100 0.1 99.29 98.23 98.90 biosimilar 10 Adalimumab 0 10 0 0 240 0 0.1 97.93 98.54 biosimilar 11 Adalimumab 0 10 240 0 0 0 0.1 99.32 98.65 99.00 biosimilar 12 Adalimumab 0 10 0 240 0 0 0.1 99.32 98.53 98.96 biosimilar 13 Adalimumab 10 0 0 0 0 150 0.1 99.29 98.12 98.84 biosimilar 14 Adalimumab 10 0 0 0 0 150 0 99.28 98.28 98.90 biosimilar 15 Adalimumab 0 10 0 0 0 150 0.1 99.26 97.99 98.83 biosimilar 16 Adalimumab 0 10 0 0 0 150 0 99.20 97.76 98.62 biosimilar TABLE D-3 Percent purity by RP HPLC for formulations in Block D at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. API citrate phosphate sorbitol trehalose mannitol NaCl 80 t0 t1 t2 1 Adalimumab 8 18 0 0 65 100 0.1 98.17 97.75 98.02 biosimilar 2 Adalimumab 8 18 0 0 65 100 0 98.09 97.84 98.08 biosimilar 3 Adalimumab 20 0 0 0 65 100 0.1 98.03 97.81 98.19 biosimilar 4 Adalimumab 20 0 0 0 65 100 0 98.17 97.85 98.06 biosimilar 5 Adalimumab 0 20 0 0 65 100 0.1 98.11 97.88 98.18 biosimilar 6 Adalimumab 0 20 0 0 65 100 0 98.21 97.77 98.10 biosimilar 7 Adalimumab 8 18 65 0 0 100 0.1 98.11 97.80 98.14 biosimilar 8 Adalimumab 8 18 0 65 0 100 0.1 98.06 97.73 98.03 biosimilar 9 Adalimumab 0 20 65 0 0 100 0.1 98.09 97.80 98.07 biosimilar 10 Adalimumab 0 10 0 0 240 0 0.1 98.13 97.82 98.08 biosimilar 11 Adalimumab 0 10 240 0 0 0 0.1 98.10 97.90 98.06 biosimilar 12 Adalimumab 0 10 0 240 0 0 0.1 98.13 97.95 98.14 biosimilar 13 Adalimumab 10 0 0 0 0 150 0.1 98.07 97.79 98.02 biosimilar 14 Adalimumab 10 0 0 0 0 150 0 98.13 97.78 98.14 biosimilar 15 Adalimumab 0 10 0 0 0 150 0.1 98.17 97.80 98.10 biosimilar 16 Adalimumab 0 10 0 0 0 150 0 98.14 97.79 98.06 biosimilar TABLE D-4 Percentage of main bands seen in the cIEF profile of formulations in Block D at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. pH t0 t1 t2 1 8.56 2.26 1.81 8.41 13.84 12.88 11.73 8.25 62.27 59.80 56.15 8.14 6.48 8.04 15.71 22.93 13.73 7.99 5.92 4.39 4.13 2 8.55 2.08 1.58 8.40 12.89 12.58 8.24 60.15 53.24 8.14 5.98 6.69 8.03 11.92 9.72 7.98 3.65 5.67 3 8.57 1.58 2.10 1.89 8.41 11.87 11.83 11.99 8.26 54.93 54.45 54.51 8.16 9.10 6.31 8.24 8.05 9.21 11.16 10.22 7.91 7.60 4.16 5.26 4 8.57 3.57 1.82 1.05 8.40 11.12 10.66 10.83 8.24 49.37 47.85 42.34 8.14 3.01 1.83 3.68 8.03 10.11 10.06 17.12 7.90 2.78 4.72 3.84 5 8.55 2.30 2.18 2.13 8.40 7.63 8.86 8.63 8.25 33.90 14.41 16.64 8.20 23.41 33.90 33.75 8.03 10.14 20.39 19.42 7.99 6.76 5.42 4.63 6 8.59 1.87 1.39 8.42 11.25 11.18 11.89 8.27 50.07 61.72 64.17 8.20 12.43 22.08 19.18 8.03 10.20 7.91 2.70 5.01 3.38 7 8.55 8.40 8.25 8.20 8.03 7.99 8 8.59 1.46 2.64 1.16 8.39 13.52 13.62 7.37 8.22 60.79 50.83 55.40 8.08 5.21 11.28 9.78 8.02 15.24 8.55 11.94 7.91 3.79 3.02 5.18 9 8.53 2.64 3.25 1.94 8.38 13.83 12.72 11.67 8.25 64.97 51.32 54.14 8.17 8.33 11.21 8.61 8.06 11.75 9.98 9.03 8.01 5.79 4.80 7.31 10 8.54 1.78 3.26 8.38 13.04 11.19 8.21 60.53 44.83 8.15 19.60 10.95 7.99 9.41 7.90 5.05 4.27 11 8.52 1.95 2.11 1.89 8.36 11.24 12.43 12.43 8.21 48.64 54.10 59.90 8.13 11.69 6.31 8.00 10.30 21.14 11.14 8.01 5.27 5.64 8.32 12 8.51 1.85 8.29 11.31 11.38 8.18 63.11 45.14 8.14 2.54 8.05 16.16 22.03 7.94 5.03 6.88 13 8.62 3.51 3.05 8.44 12.44 12.30 8.29 65.10 51.44 8.21 12.18 8.06 15.37 17.25 7.91 3.58 3.77 14 8.61 2.74 1.73 8.43 10.60 12.19 8.27 46.23 41.11 8.21 13.97 10.49 8.05 18.56 17.52 7.91 5.15 15 8.62 8.35 12.40 10.91 8.34 8.21 31.87 30.32 36.39 8.20 41.14 25.57 30.62 8.02 12.42 13.72 18.26 7.89 2.18 5.44 3.86 16 8.61 8.48 12.96 12.86 13.19 8.34 34.40 31.45 39.25 8.31 27.74 20.29 18.81 8.05 22.76 19.35 7.89 8.17 7.69 4.83 TABLE D-5 Percentage of bands for light chain (LC), heavy chain (HC), non-glycosylated HC, and other species for formulations in Block D at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 t1 34.11 62.58 0.58 2.73 t2 33.19 64.28 0.60 1.92 2 t0 30.25 66.81 0.64 2.31 t1 30.61 65.79 0.54 3.07 t2 29.22 67.04 0.64 3.10 3 t0 27.48 68.51 0.59 3.42 t1 30.84 67.27 0.54 1.35 t2 30.30 68.13 0.58 0.99 4 t0 30.88 68.33 0.60 0.19 t1 29.76 68.32 0.57 1.34 t2 31.49 66.95 0.55 1.01 5 t0 33.77 64.50 0.56 1.17 t1 31.59 66.54 0.52 1.34 t2 29.19 69.16 0.59 1.06 6 t0 30.90 68.08 0.56 0.47 t1 29.32 69.88 0.54 0.26 t2 31.08 67.58 0.54 0.79 7 t0 30.41 68.60 0.56 0.43 t1 30.87 66.95 0.55 1.63 t2 30.14 68.28 0.55 1.03 8 t0 31.68 67.41 0.60 0.31 t1 t2 9 t0 29.62 68.12 0.51 1.75 t1 t2 29.46 68.10 0.61 1.83 10 t0 29.80 67.99 0.58 1.64 t1 30.04 65.53 0.45 3.98 t2 30.41 66.27 0.53 2.80 11 t0 29.85 67.63 0.61 1.91 t1 29.02 68.18 0.60 2.20 t2 30.44 67.14 0.58 1.84 12 t0 29.38 68.11 0.55 1.96 t1 30.16 65.55 0.49 3.80 t2 28.20 69.19 0.59 2.02 13 t0 31.38 66.28 0.55 1.79 t1 33.67 64.10 0.56 1.67 t2 29.72 67.99 0.58 1.71 14 t0 37.34 60.53 0.52 1.62 t1 33.03 63.46 0.53 2.97 t2 34.39 63.62 0.54 1.45 15 t0 30.20 68.42 0.59 0.79 t1 28.67 69.42 0.58 1.33 t2 29.96 68.24 0.56 1.24 16 t0 31.62 66.95 0.58 0.85 t1 30.48 66.36 0.55 2.61 t2 27.94 70.17 0.60 1.29 Results of Block D The pH stability was quite good for these formulations (Table D-1). Once again, the commercial adalimumab (Humira®) formulation was used as a control (but using a proprietary adalimumab biosimilar protein as the API). The commercial formulation again showed poorer stability by SEC than those using single buffers like phosphate and His (See Table D-2). Of the two buffers used in Humira®, we have now discovered that phosphate is the better stabilizer. This is surprising, as phosphate has virtually no buffer capacity at pH 5.2, while citrate buffers well at this pH. This suggests that the differences in stability profile may be due to direct interaction of the buffer with the protein, a phenomenon that, in the case of the commercial Humira® formulation, we believe was not previously understood or appreciated. Accordingly, the comparative benefit of selecting phosphate as a buffer in an adalimumab formulation, due to superior stability in the formulation versus the selection of a citrate/phosphate combination constitutes one of the important aspects of our invention. Both sorbitol and trehalose display better stability profiles than mannitol when used as the sole tonicity agent in these formulations. It also appears that removal of the polysorbate 80 (PS 80) decreases stability somewhat. The best stability profile by SEC appears to be for Formulations 10 and 11, which contain high concentrations of sorbitol or trehalose in place of mannitol/NaCl (Table D-2). These results indicate to us that removing NaCl from the formulation, or limiting its concentration below certain targeted levels (for example less than about 100 mM), will be beneficial for stability. (We note that mannitol does appear to be a stabilizing ingredient, but at levels preferably above 150.) The RP data indicates that either citrate or phosphate provides better stability than the combination used in Humira® (Table D-3). Again, the avoidance of the citrate/phosphate combination represents an important feature of our invention. It could not have been known or predicted that citrate alone, or phosphate alone would provide better formulation stability than the commercial buffer system comprising a combination of citrate and phosphate. The cIEF analyses were run for Block D samples (Table D-4 above). As before, there is some decrease in the intensity of the main peak, but no new peaks are observed. In some cases, there is some small increase in the intensity of the more acidic peaks. The decreases in the main peak appear to be greater at t1 than at t2, suggesting that degradation at 5° C. would be almost imperceptible. Still, overall it looks like less than 5% (and probably much less than 5%) is degrading as measured by cIEF (Table D-4). Likewise, little degradation is seen by CE-SDS (Table D-5). At most 2 to 4% degradation is seen, but the variability in the method makes it difficult to determine if these are real changes. There does appear to be higher impurity levels (Other) for Formulations 1 and 2 and 10 through 14. Block E Formulation Studies This block of formulations was designed to evaluate the stability of formulations at different pH levels. If a buffer is not specified, acetate buffer (10 mM) was employed (Table E). A secondary objective was to evaluate Gly and Arg at higher concentrations and in combination as alternative stabilizers to mannitol and NaCl. TABLE E BLOCK E STUDY DESIGN Form PS No. API pH citrate phosphate sorbitol Gly Arg mannitol NaCl 80 1 Adalimumab 5.2 8 18 0 0 0 65 100 0.1 biosimilar 2 Adalimumab 3.5 8 18 0 0 0 65 100 0.1 biosimilar 3 Adalimumab 5.2 0 0 0 0 0 65 100 0.1 biosimilar 4 Adalimumab 3.5 0 0 0 0 0 65 100 0.1 biosimilar 5 Adalimumab 3.5 0 0 65 0 0 0 100 0.1 biosimilar 6 Adalimumab 3.5 0 0 0 0 130 0 0 0.1 biosimilar 7 Adalimumab 3.5 0 0 0 0 130 0 0 0 biosimilar 8 Adalimumab 3.5 0 0 0 240 0 0 0 0 biosimilar 9 Adalimumab 5.2 0 0 0 240 0 0 0 0 biosimilar 10 Adalimumab 3.5 0 0 0 100 100 0 0 0 biosimilar 11 Adalimumab 5.2 0 0 0 100 100 0 0 0 biosimilar 12 Adalimumab 3.5 0 0 0 150 50 0 0 0 biosimilar TABLE E-1 Measured pH for Block E formulations at t0 and t1 (one week, 40° C.) Form PS No. pH citrate phosphate sorbitol Gly Arg mannitol NaCl 80 t0 t1 t2 1 5.2 8 18 0 0 0 65 100 0.1 5.15 5.11 5.21 2 3.5 8 18 0 0 0 65 100 0.1 3.36 3.49 3.50 3 5.2 0 0 0 0 0 65 100 0.1 5.13 5.24 5.24 4 3.5 0 0 0 0 0 65 100 0.1 3.31 3.43 3.45 5 3.5 0 0 65 0 0 0 100 0.1 3.30 3.48 3.42 6 3.5 0 0 0 0 130 0 0 0.1 3.24 3.52 3.42 7 3.5 0 0 0 0 130 0 0 0 3.27 3.59 3.48 8 3.5 0 0 0 240 0 0 0 0 3.27 3.33 3.39 9 5.2 0 0 0 240 0 0 0 0 5.05 5.25 5.20 10 3.5 0 0 0 100 100 0 0 0 3.30 3.45 3.41 11 5.2 0 0 0 100 100 0 0 0 5.20 5.38 5.39 12 3.5 0 0 0 150 50 0 0 0 3.24 3.38 3.37 TABLE E-2 Monomer content by SEC for formulations in Block E at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. pH citrate phosphate sorbitol Gly Arg mannitol NaCl 80 t0 t1 t2 1 5.2 8 18 0 0 0 65 100 0.1 99.23 98.20 98.85 2 3.5 8 18 0 0 0 65 100 0.1 98.82 44.15 86.37 3 5.2 0 0 0 0 0 65 100 0.1 99.30 98.37 99.02 4 3.5 0 0 0 0 0 65 100 0.1 95.85 33.51 76.21 5 3.5 0 0 65 0 0 0 100 0.1 97.37 26.21 77.80 6 3.5 0 0 0 0 130 0 0 0.1 97.79 35.67 65.83 7 3.5 0 0 0 0 130 0 0 0 99.00 55.51 90.60 8 3.5 0 0 0 240 0 0 0 0 99.24 75.60 98.24 9 5.2 0 0 0 240 0 0 0 0 99.08 98.63 99.18 10 3.5 0 0 0 100 100 0 0 0 99.28 51.03 91.66 11 5.2 0 0 0 100 100 0 0 0 99.32 98.54 99.09 12 3.5 0 0 0 150 50 0 0 0 99.29 45.86 93.06 TABLE E-3 Percent purity by RP HPLC for formulations in Block E at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. pH citrate phosphate sorbitol Gly Arg mannitol NaCl 80 t0 t1 t2 1 5.2 8 18 0 0 0 65 100 0.1 98.58 96.88 96.91 2 3.5 8 18 0 0 0 65 100 0.1 98.51 90.29 95.99 3 5.2 0 0 0 0 0 65 100 0.1 98.50 96.90 96.83 4 3.5 0 0 0 0 0 65 100 0.1 98.56 91.18 95.55 5 3.5 0 0 65 0 0 0 100 0.1 98.45 90.96 95.71 6 3.5 0 0 0 0 130 0 0 0.1 98.71 93.28 95.38 7 3.5 0 0 0 0 130 0 0 0 98.40 90.65 96.54 8 3.5 0 0 0 240 0 0 0 0 98.03 93.94 96.82 9 5.2 0 0 0 240 0 0 0 0 98.23 97.19 97.12 10 3.5 0 0 0 100 100 0 0 0 98.13 91.10 96.67 11 5.2 0 0 0 100 100 0 0 0 98.13 97.17 97.12 12 3.5 0 0 0 150 50 0 0 0 98.07 93.40 96.48 TABLE E-4 Percentage of bands for light chain (LC), heavy chain (HC), non-glycosylated HC, and other species for formulations in Block E at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 29.97 68.80 0.59 0.64 t1 28.49 70.07 0.60 0.81 t2 28.21 70.29 0.59 0.90 2 t0 28.50 68.67 0.52 2.31 t1 29.69 50.92 0.30 19.09 t2 28.76 69.64 0.60 1.00 3 t0 24.30 74.01 0.60 1.09 t1 28.27 69.63 0.60 1.51 t2 28.17 69.89 0.54 1.40 4 t0 29.45 68.73 0.56 1.26 t1 29.52 51.33 0.30 18.86 t2 27.92 65.73 0.52 5.83 5 t0 35.59 63.85 0.56 0.00 t1 32.47 48.72 0.30 18.52 t2 34.98 60.88 0.46 3.68 6 t0 34.33 63.39 0.51 1.77 t1 t2 35.32 61.31 0.45 2.92 7 t0 30.13 68.87 0.60 0.40 t1 28.13 54.79 0.59 16.49 t2 34.39 63.32 0.53 1.76 8 t0 33.27 64.97 0.55 1.21 t1 33.20 52.62 0.33 13.85 t2 33.25 65.26 0.58 0.92 9 t0 32.28 66.34 0.57 0.81 t1 31.81 65.76 0.57 1.86 t2 31.23 66.81 0.57 1.39 10 t0 35.66 63.36 0.43 0.56 t1 24.96 58.61 0.33 16.10 t2 33.44 66.03 0.53 0.00 11 t0 29.75 69.08 0.60 0.57 t1 27.67 70.83 0.61 0.89 t2 28.81 69.86 0.59 0.73 12 t0 30.23 49.07 0.26 20.44 t1 28.14 70.11 0.58 1.18 t2 29.75 69.08 0.60 0.57 TABLE E-5 Percentage of main bands seen in the cIEF profile of formulations in Block E at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C. Form No. pH t0 t1 t2 1 8.56 8.37 12.52 12.65 8.23 51.77 50.04 8.14 8.03 21.54 12.40 7.93 14.17 16.26 2 1.88 1.49 8.37 10.07 17.66 14.15 8.21 37.52 32.26 33.88 8.13 19.03 9.96 8.01 16.57 28.70 7.93 4.12 7.45 4 8.54 1.04 2.67 8.38 10.50 9.32 8.21 68.34 31.91 8.13 28.52 8.02 16.55 10.05 7.88 3.57 8.67 5 6 7 8 9 8.60 1.40 2.60 3.26 8.43 10.04 12.33 12.03 8.26 62.39 63.19 63.89 8.14 8.03 15.00 16.95 16.57 7.88 7.08 4.93 4.25 Results of Block E Studies The pH stability was modest, with increases in pH occurring at t1 for many of the formulations, especially those buffered with acetate at low pH (Table E-1 above). Two of the samples (Formulations 6 and 12) gelled at t1. There were sizable losses in monomer content for the pH3.5 samples (Table E-3), whereas the pH 5.2 samples displayed stability comparable to what was seen in the preceding Blocks. It was also clear that the degradation was much more pronounced at 40 C than at 25, despite being stored for twice the length of time. In fact, Formulation 8 lost less than 1% monomer at t2 (Table E-2). The Gly and Arg formulations all displayed good stability, provided the pH was held 5.2. The data in this block of studies confirm our discovery that glycine or arginine, or a mixture thereof are good stabilizers in an adalimumab formulation. The RP HPLC data shows large decreases in purity, although not nearly as great as for monomer loss by SEC (Table E-3). This suggests that chemical instability is less than physical instability. As with the SEC results, the loss of stability is more pronounced at t1 than at t2. The CE-SDS results show large increases in new peaks, with the Other category increasing to 15-20% for low pH samples at t1 (Table E-4). The most stable formulation by CE-SDS appears to be Formulation 11, which contains both Gly and Arg as the tonicity modifiers/stabilizers. We encountered difficulties running the cIEF for many of the Block E samples. However, given the clearly inferior stability at pH 3.5, it is unlikely that cIEF would provide any new information on those stability profiles. For example, Formulation 4 (pH 3.5) shows a splitting of the main peak at t1. Block F Formulation Studies The Block F studies were intended to investigate the stability for His-containing formulation using either mannitol, Gly or Arg as the sole tonicity modifier (Table F below). It also served as an opportunity to evaluate additives such as EDTA and methionine (Met), which can be effective at slowing oxidation. In addition, one high citrate concentration and one high phosphate concentration formulation were examined. TABLE F BLOCK F STUDY DESIGN Form PS No. API pH citrate phosphate His Gly Arg mannitol NaCl 80 EDTA Met 1 Adalimurnab 5.2 8 18 0 0 0 65 100 0.1 0 0 biosimilar 2 Adalimumab 5.2 8 18 0 0 0 65 100 0.1 0.5 0 biosimilar 3 Adalimumab 5.2 0 0 10 0 150 0 0 0 0.1 0 biosimilar 4 Adalimumab 5.2 0 0 10 0 150 0 0 0 0.5 0 biosimilar 5 Adalimumab 5.2 0 0 10 0 0 240 0 0 0 0 biosimilar 6 Adalimumab 5.2 0 0 10 0 0 240 0 0 0 10 biosimilar 7 Adalimurnab 5.2 0 0 10 0 0 240 0 0 0 50 biosimilar 8 Adalimurnab 5.2 30 0 0 240 0 0 0 0 0 0 biosimilar 9 Adalimumab 5.2 0 30 0 240 0 0 0 0 0 0 biosimilar 10 Adalimumab 5.2 0 0 30 240 0 0 0 0 0 0 biosimilar 11 Adalimurnab 5.2 0 0 20 0 25 120 0 0.1 0 0 biosimilar 12 Adalimumab 5.2 0 0 20 0 25 120 0 0.1 0 0 biosimilar TABLE F-1 Measured pH for Block F formulations at t0 and t1 (one week, 40° C.) Form PS No. citrate phosphate His Gly Arg mannitol NaCl 80 EDTA Met t0 t1 t2 1 8 18 0 0 0 65 100 0.1 0 0 4.67 4.88 4.77 2 8 18 0 0 0 65 100 0.1 0.5 0 5.05 5.15 5.20 3 0 0 10 0 150 0 0 0 0.1 0 5.11 5.22 5.27 4 0 0 10 0 150 0 0 0 0.5 0 4.95 5.06 5.15 5 0 0 10 0 0 240 0 0 0 0 5.12 5.25 5.29 6 0 0 10 0 0 240 0 0 0 10 4.45 4.74 4.67 7 0 0 10 0 0 240 0 0 0 50 5.03 5.24 5.24 8 30 0 0 240 0 0 0 0 0 0 5.09 5.18 5.22 9 0 30 0 240 0 0 0 0 0 0 5.13 5.25 5.32 10 0 0 30 240 0 0 0 0 0 0 5.08 5.24 5.24 11 0 0 20 0 25 120 0 0.1 0 0 5.01 5.17 5.18 12 0 0 20 0 25 120 0 0.1 0 0 5.06 5.20 5.19 TABLE F-2 Monomer content by SEC for formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. citrate phosphate His Gly Arg mannitol NaCl 80 EDTA Met t0 t1 t2 1 8 18 0 0 0 65 100 0.1 0 0 97.69 94.75 96.06 2 8 18 0 0 0 65 100 0.1 0.5 0 99.25 98.14 98.92 3 0 0 10 0 150 0 0 0 0.1 0 99.30 98.54 99.16 4 0 0 10 0 150 0 0 0 0.5 0 99.28 98.31 99.14 5 0 0 10 0 0 240 0 0 0 0 99.17 98.64 99.14 6 0 0 10 0 0 240 0 0 0 10 99.07 98.50 99.07 7 0 0 10 0 0 240 0 0 0 50 99.29 98.92 99.24 8 30 0 0 240 0 0 0 0 0 0 99.28 98.40 99.04 9 0 30 0 240 0 0 0 0 0 0 99.30 98.50 99.08 10 0 0 30 240 0 0 0 0 0 0 99.31 98.60 99.23 11 0 0 20 0 25 120 0 0.1 0 0 99.27 98.64 99.16 12 0 0 20 0 25 120 0 0.1 0 0 99.29 98.51 99.17 TABLE F-3 Percent purity by RP HPLC for formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form PS No. citrate phosphate His Gly Arg mannitol NaCl 80 EDTA Met t0 t1 t2 1 8 18 0 0 0 65 100 0.1 0 0 97.47 96.89 97.98 2 8 18 0 0 0 65 100 0.1 0.5 0 97.33 97.02 97.99 3 0 0 10 0 150 0 0 0 0.1 0 97.64 97.14 98.04 4 0 0 10 0 150 0 0 0 0.5 0 97.59 97.00 97.97 5 0 0 10 0 0 240 0 0 0 0 97.11 97.30 98.03 6 0 0 10 0 0 240 0 0 0 10 97.61 97.27 98.03 7 0 0 10 0 0 240 0 0 0 50 97.55 97.37 98.08 8 30 0 0 240 0 0 0 0 0 0 97.48 97.51 98.05 9 0 30 0 240 0 0 0 0 0 0 97.64 97.58 98.03 10 0 0 30 240 0 0 0 0 0 0 97.68 97.41 98.06 11 0 0 20 0 25 120 0 0.1 0 0 97.67 97.18 98.03 12 0 0 20 0 25 120 0 0.1 0 0 97.68 97.33 98.02 TABLE F-4 Percentage of bands for light chain (LC), heavy chain (HC), non-glycosylated HC, and other species for formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 27.36 71.86 0.60 0.17 t1 t2 25.34 73.18 0.63 0.86 2 t0 27.80 71.07 0.60 0.53 t1 28.29 71.08 0.63 0.00 t2 27.53 70.97 0.64 0.86 3 t0 27.78 70.62 0.65 0.95 t1 28.26 70.85 0.66 0.23 t2 28.26 70.50 0.63 0.61 4 t0 28.20 70.24 0.60 0.96 t1 29.17 69.30 0.74 0.80 t2 29.17 70.27 0.56 0.00 5 t0 27.50 70.74 0.59 1.17 t1 29.56 65.79 0.41 4.24 t2 28.24 69.90 0.58 1.28 6 t0 29.10 68.84 0.54 1.52 t1 28.58 69.18 0.54 1.70 t2 27.47 70.39 0.54 1.60 7 t0 27.87 70.28 0.55 1.30 t1 t2 8 t0 34.72 64.87 0.41 0.00 t1 34.94 64.53 0.53 0.00 t2 33.21 65.76 0.50 0.52 9 t0 31.96 68.04 0 0 t1 48.51 51.49 0 0 t2 33.15 65.82 0.57 0.46 10 t0 27.81 71.27 0.51 0.40 t1 29.59 68.46 0.53 1.43 t2 31.25 67.89 0.50 0.36 11 t0 27.33 70.80 0.61 1.26 t1 26.54 71.00 0.64 1.82 t2 29.46 69.85 0.69 0.00 12 t0 24.18 71.21 0 4.61 t1 t2 28.95 68.98 0.59 1.46 TABLE F-5 Percentage of main bands seen in the cIEF profile of formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C. Form No. pH t0 t1 t2 1 8.65 2.11 8.31 13.07 11.43 34.17 8.24 64.66 67.99 28.67 8.14 2.29 8.08 16.13 17.73 15.98 7.95 6.14 4.80 2 8.60 1.56 1.93 1.12 8.48 12.95 11.26 11.12 8.24 58.99 55.85 60.37 8.13 20.98 22.43 18.77 7.93 3.56 6.41 6.09 8.60 1.56 1.93 1.12 3 8.56 1.56 1.69 8.34 10.88 12.85 10.83 8.18 66.93 55.35 62.00 8.02 17.28 19.04 20.13 7.89 4.91 11.21 5.35 4 8.58 1.86 1.68 8.45 13.79 10.61 12.84 8.27 65.06 51.89 61.94 8.06 19.29 18.85 25.22 7.96 6.28 4.91 5 8.60 1.35 1.78 1.45 8.45 12.35 13.63 8.59 8.27 60.12 55.07 64.28 8.07 20.50 20.35 19.73 7.94 5.69 9.17 5.95 6 8.55 1.30 1.30 1.08 8.43 13.29 13.26 13.23 8.24 54.83 56.88 61.67 8.08 20.76 19.79 17.19 7.96 9.82 8.76 6.84 7 8.57 1.28 1.41 2.40 8.44 12.08 12.63 13.05 8.27 61.50 55.33 60.70 8.08 17.55 19.48 17.43 7.94 5.93 8.92 4.25 8 8.55 1.32 0.90 8.43 11.51 12.47 10.09 8.24 62.99 54.09 63.81 8.05 15.43 22.71 20.91 7.90 8.75 9.83 5.19 9 8.59 1.35 1.63 8.45 11.59 13.67 11.40 8.28 63.60 52.70 63.11 8.06 17.98 24.08 18.57 7.94 2.28 7.05 5.29 10 8.57 1.56 2.50 2.08 8.45 13.22 11.93 12.90 8.28 61.86 55.12 61.87 8.08 17.87 20.99 18.74 7.97 5.50 4.71 4.41 11 8.59 1.43 1.19 8.45 12.25 11.42 9.85 8.28 58.83 59.88 64.13 8.08 18.18 22.06 17.46 7.97 9.61 5.45 6.97 12 8.56 1.64 1.39 0.94 8.39 15.30 13.07 15.71 8.21 63.76 59.71 62.92 8.02 16.72 20.51 16.60 7.97 2.58 4.21 3.85 Results of Block F In this block of formulations, the pH values were all slightly lower than the target value of pH 5.2 (Table F-1). In addition, the pH does change by about 0.1 units for most of the formulations when measured at t1. These differences were considered when constructing mathematical models of the data, as discussed below. The addition of EDTA does appear to improve stability for the worst formulation (Formulation 1). Whether it increases stability in general was less clear, based on the SEC data (Table F-2). The formulations containing high concentrations of Arg or Gly all performed quite well upon storage (Table F-2). The initial purities by RP HPLC were universally lower than expected for these formulations (Table F-3). Upon storage at t1 and t2, there are some slight differences, with Gly- and Arg-based formulations showing the greatest stability. Based upon the RP HPLC data, EDTA does not appear to be a significant stabilizer (Table F-3). Likewise, the effect of Met appears to be minimal on stability as measured by RP HPLC or SEC, with the exception of the monomer content for the highest Met concentration (Table F-2, Formulation 7). Analysis by CE-SDS indicates that very little degradation occurs upon storage (usually less than 1% increase in ‘Other’) (Table F-4). However, there are some formulations that begin with higher ‘Other’ contents (Formulations 4 through 7, for example). These are all formulations using a high concentration of mannitol (240 mM). The same seems to be true for formulations containing 120 mM mannitol. As for analysis by cIEF, there is little change in the relative intensities of the main peak, at least in a systematic fashion that would allow one to discern stability trends (Table F-5). In general, the changes are smaller at t2 than at t1. Block G Formulation Studies The Block G formulation studies examined a variety of formulations with combinations of Gly and Arg as the primary stabilizers (Table XXXIV). In addition, two other surfactants (Pluronic F-68 and polysorbate 20, PS 20) were evaluated in addition to PS 80. Finally, a range of PS 80 concentrations was evaluated. TABLE G BLOCK G STUDY DESIGN Form No. API citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 1 Adalimumab 8 18 0 0 0 0 65 100 0 0 0.1 biosimilar 2 Adalimumab 8 18 0 0 0 0 65 100 0 0.1 0 biosimilar 3 Adalimumab 8 18 0 0 0 0 65 100 0.1 0 0 biosimilar 4 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.1 biosimilar 5 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.05 biosimilar 6 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.01 biosimilar 7 Adalimumab 0 0 0 10 120 120 0 0 0 0.05 0 biosimilar 8 Adalimumab 0 0 0 10 120 120 0 0 0.1 0 0 biosimilar 9 Adalimumab 0 0 10 0 120 120 0 0 0 0 0.05 biosimilar 10 Adalimumab 0 0 20 0 150 100 0 0 0 0.05 0 biosimilar 11 Adalimumab 0 0 0 20 150 100 0 0 0 0 0.01 biosimilar 12 Adalimumab 0 0 0 20 120 120 0 0 0 0.01 0 biosimilar TABLE G-1 Measured pH for Block G formulations at t0, t1 (one week, 40° C.), and t2 (two weeks, 40° C.) Form No. citrate phosphate succinate His Gly Arg mannitol NaCl F68 PS20 PS80 t0 t1 t2 1 8 18 0 0 0 0 65 100 0 0 0.1 5.19 5.38 5.25 2 8 18 0 0 0 0 65 100 0 0.1 0 5.23 5.28 5.24 3 8 18 0 0 0 0 65 100 0.1 0 0 5.22 5.26 5.20 4 0 0 0 10 120 120 0 0 0 0 0.1 5.20 5.33 5.29 5 0 0 0 10 120 120 0 0 0 0 0.05 5.23 5.34 5.29 6 0 0 0 10 120 120 0 0 0 0 0.01 5.19 5.40 5.27 7 0 0 0 10 120 120 0 0 0 0.05 0 5.23 5.39 5.42 8 0 0 0 10 120 120 0 0 0.1 0 0 5.19 5.38 5.41 9 0 0 10 0 120 120 0 0 0 0 0.05 5.19 5.27 5.24 10 0 0 20 0 150 100 0 0 0 0.05 0 5.23 5.28 5.24 11 0 0 0 20 150 100 0 0 0 0 0.01 5.23 5.33 5.27 12 0 0 0 20 120 120 0 0 0 0.01 0 5.22 5.29 5.29 TABLE G-2 Monomer content by SEC for formulations in Block G at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. citrate phosphate succinate His Gly Arg mannitol NaCl F68 PS20 PS80 t0 t1 t2 1 8 18 0 0 0 0 65 100 0 0 0.1 99.17 97.45 98.09 2 8 18 0 0 0 0 65 100 0 0.1 0 99.11 97.78 98.09 3 8 18 0 0 0 0 65 100 0.1 0 0 98.99 97.74 97.92 4 0 0 0 10 120 120 0 0 0 0 0.1 99.12 98.67 98.68 5 0 0 0 10 120 120 0 0 0 0 0.05 99.05 98.57 98.53 6 0 0 0 10 120 120 0 0 0 0 0.01 99.05 98.66 98.70 7 0 0 0 10 120 120 0 0 0 0.05 0 99.04 98.63 98.50 8 0 0 0 10 120 120 0 0 0.1 0 0 99.11 98.64 98.55 9 0 0 10 0 120 120 0 0 0 0 0.05 99.12 98.56 98.98 10 0 0 20 0 150 100 0 0 0 0.05 0 99.10 98.49 98.88 11 0 0 0 20 150 100 0 0 0 0 0.01 99.07 98.76 98.45 12 0 0 0 20 120 120 0 0 0 0.01 0 99.11 98.48 TABLE G-3 Percent purity by RP HPLC for formulations in Block G at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C. Form No. citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 t0 t1 t2 1 8 18 0 0 0 0 65 100 0 0 0.1 99.74 99.66 98.93 2 8 18 0 0 0 0 65 100 0 0.1 0 99.59 99.66 98.97 3 8 18 0 0 0 0 65 100 0.1 0 0 99.58 99.60 99.22 4 0 0 0 10 120 120 0 0 0 0 0.1 99.62 99.62 98.99 5 0 0 0 10 120 120 0 0 0 0 0.05 99.70 99.61 99.01 6 0 0 0 10 120 120 0 0 0 0 0.01 99.60 99.66 99.00 7 0 0 0 10 120 120 0 0 0 0.05 0 99.71 99.65 98.99 8 0 0 0 10 120 120 0 0 0.1 0 0 99.70 99.61 99.03 9 0 0 10 0 120 120 0 0 0 0 0.05 99.71 99.60 99.03 10 0 0 20 0 150 100 0 0 0 0.05 0 99.72 99.60 99.02 11 0 0 0 20 150 100 0 0 0 0 0.01 99.72 99.61 99.05 12 0 0 0 20 120 120 0 0 0 0.01 0 99.61 99.04 TABLE G-4 Percentage of bands for light chain (LC), heavy chain (HC), non-glycosylated HC, and other species for formulations in Block G at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 28.55 70.77 0.50 0.17 t1 29.71 69.42 0.57 0.30 t2 30.32 68.80 0.53 0.35 2 t0 37.14 62.38 0.49 0.00 t1 30.31 69.38 0.28 0.03 t2 31.60 67.87 0.53 0.00 3 t0 28.95 70.40 0.65 0.00 t1 28.17 70.26 0.58 0.99 t2 27.32 71.52 0.56 0.59 4 t0 29.56 69.02 0.65 0.77 t1 32.19 66.09 0.53 1.19 t2 31.58 66.03 0.57 1.81 5 t0 36.54 62.48 0.56 0.42 t1 28.77 69.28 0.62 1.33 t2 23.76 74.49 0.60 1.16 6 t0 29.60 68.61 0.58 1.21 t1 30.37 67.42 0.59 1.61 t2 32.27 66.08 0.59 1.06 7 t0 31.90 65.50 0.63 1.97 t1 31.26 66.66 0.56 1.51 t2 31.37 66.64 0.67 1.31 8 t0 31.04 67.38 0.54 1.04 t1 30.34 67.99 0.62 1.05 t2 30.21 67.63 0.68 1.48 9 t0 33.12 65.34 0.61 0.94 t1 34.01 63.97 0.56 1.46 t2 34.47 63.77 0.57 1.19 10 t0 36.78 61.61 0.54 1.07 t1 39.25 58.66 0.53 1.56 t2 32.83 65.42 0.55 1.21 11 t0 36.37 61.97 0.54 1.11 t1 t2 34.97 63.14 0.54 1.36 12 t0 34.26 64.16 0.52 1.05 t1 t2 34.90 63.35 0.56 1.19 TABLE G-5 Percentage of main bands seen in the cIEF profile of formulations in Block G at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C. Form No. pH t0 t1 t2 1 8.53 1.24 1.21 8.36 14.30 12.69 13.67 8.24 64.03 53.50 60.30 8.14 8.01 15.77 9.32 19.12 7.86 3.73 3.35 4.48 2 8.52 1.06 1.37 0.88 8.35 13.10 13.30 12.53 8.16 66.28 59.68 57.99 7.97 17.14 19.60 21.55 7.83 2.42 4.78 4.92 3 8.51 0.65 0.65 1.03 8.34 13.31 14.00 15.31 8.16 65.13 59.04 60.70 8.14 7.98 17.26 18.90 17.56 7.82 2.89 5.68 4.16 4 8.36 1.87 2.43 1.00 8.19 7.74 10.89 11.69 7.99 61.91 54.27 59.10 7.82 20.94 22.72 19.81 7.66 6.35 7.98 6.92 5 8.44 1.79 0.95 071 8.26 13.33 12.85 10.43 8.06 61.67 59.94 60.12 7.88 17.49 21.08 20.82 7.69 4.02 4.50 6.50 6 8.36 1.71 4.76 8.21 12.37 12.93 10.95 8.04 62.53 54.16 56.48 7.87 19.24 26.08 17.97 7.64 4.15 2.07 6.50 7 8.54 0.77 1.19 0.79 8.34 7.15 12.32 13.15 8.17 54.73 42.64 60.58 8.02 22.18 29.90 17.28 7.83 7.12 11.47 4.77 7.69 1.41 2.48 2.11 8 8.55 1.04 2.11 8.39 7.28 10.69 14.82 8.23 64.01 57.42 55.68 8.05 20.81 23.86 23.76 7.96 6.79 5.37 5.74 9 8.54 8.48 10.99 7.91 8.31 53.85 61.43 8.17 31.58 23.83 7.99 8.82 7.85 3.58 3.27 10 8.50 0.95 2.16 8.36 9.10 10.65 15.79 8.18 59.02 55.35 58.56 8.02 23.76 24.79 25.66 7.87 5.63 7.05 11 8.58 2.08 1.68 8.40 9.74 10.05 9.67 8.21 62.70 56.96 57.36 8.05 21.39 24.14 25.18 7.99 5.24 6.77 6.11 12 8.54 1.67 8.37 15.99 8.22 63.18 8.02 15.41 7.82 3.75 TABLE G-6 Block G study design for F/T and agitation studies Form No. API citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 1 Adalimumab 8 18 0 0 0 0 65 100 0 0 0.1 biolsimilar 2 Adalimumab 8 18 0 0 0 0 65 100 0 0.1 0 biolsimilar 3 Adalimumab 8 18 0 0 0 0 65 100 0.1 0 0 biolsimilar 4 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.1 biolsimilar 5 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.05 biolsimilar 6 Adalimumab 0 0 0 10 120 120 0 0 0 0 0.01 biolsimilar 7 Adalimumab 0 0 0 10 120 120 0 0 0 0.05 0 biolsimilar 8 Adalimumab 0 0 0 10 120 120 0 0 0.1 0 0 biolsimilar 9 Adalimumab 0 0 10 0 120 120 0 0 0 0 0.05 biolsimilar 10 Adalimumab 0 0 20 0 150 100 0 0 0 0.05 0 biolsimilar 11 Adalimumab 0 0 0 20 150 100 0 0 0 0 0.01 biolsimilar 12 Adalimumab 0 0 0 20 120 120 0 0 0 0.01 0 biolsimilar TABLE G-7 Monomer content by SEC for select formulations in Block G that were untreated (Q, quiescent), underwent 5 F/T cycles or subjected to agitation for 24 hours Form No. citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 Q F/T agit 1 8 18 0 0 0 0 65 100 0 0 0.1 99.15 99.03 99.14 4 0 0 0 10 120 120 0 0 0 0 0.1 99.21 99.11 99.18 8 0 0 0 10 120 120 0 0 0.1 0 0 99.18 99.14 99.17 11 0 0 0 20 150 100 0 0 0 0 0.01 99.16 99.09 99.13 12 0 0 0 20 120 120 0 0 0 0.01 0 99.10 TABLE G-8 Percent purity by RP HPLC for select formulations in Block G that were untreated (Q, quiescent), underwent 5 F/T cycles or subjected to agitation for 24 hours Form No. citrate phosphate succinate HIS Gly Arg mannitol NaCl F68 PS20 PS80 Q F/T agit 1 8 18 0 0 0 0 65 100 0 0 0.1 99.60 99.72 99.76 4 0 0 0 10 120 120 0 0 0 0 0.1 99.56 99.70 99.59 8 0 0 0 10 120 120 0 0 0.1 0 0 99.58 99.57 99.73 11 0 0 0 20 150 100 0 0 0 0 0.01 99.72 99.59 99.65 12 0 0 0 20 120 120 0 0 0 0.01 0 99.75 99.56 Results of Block G All of the pH values were close to the target values (Table G-1), with relatively small changes occurring upon storage. There appears to be some preference in terms of polysorbates over F-68 in terms of stability, as measured by SEC (Table G-2). However, the differences are relatively small. It does appear that succinate formulations (Formulations 9 and 10) fared reasonably well as far as monomer content retained. The RP HPLC data are all very close, making any determination of stability differences virtually impossible (Table G-3). These data will only be interpretable when examined in the larger context of all of the blocks of screening studies. The CE-SDS results suggest that PS 20 is the best stabilizer at 0.1% concentration for the Humira® formulation (Formulations 1 through 3) (Table G-4). Otherwise, the differences appear to be too small and variable to make any general conclusions. As seen before, the results for cIEF data are variable enough to make interpretation difficult (Table G-5). It does appear that the changes are smaller in the Gly/Arg formulations than for formulations using other stabilizers, like mannitol. Still, overall, the stability by cIEF looks to be quite good for many of the formulations in this study. Block G (F/T and Agitation) Studies. For a liquid formulation, it is important to evaluate the sensitivity to interfacial stress. Two kinds of stress studies were selected. The first is agitation at 150 rpm on an orbital shaker for 24 hours at 2-8° C. The second is five successive cycles of freezing and thawing (F/T), where this cycle should generate increasing amounts of damage protein, if the protein is sensitive to interfacial damage. Four formulations from Block G were selected for assessment, and they are highlighted in blue bold text Table G-6. Upon repeated F/T cycling, there is a very small decrease in monomer content for all of the formulations tested (Table G-7). Thus, it seems like there is little interfacial sensitivity form this stress and that the presence of PS 80 is not critical for protection. As for agitated samples, the losses are even smaller. The trends in the RP HPLC data are essentially the same (Table G-8). There are little, if any, losses in purity upon exposure to interfacial stress. Block H Formulation Studies The Block H formulations focused on three aspects of the adalimumab formulation: (1) higher protein concentrations, (2) formulations with no buffers present (other than the protein), and (3) the use of various buffer combinations beside citrate-phosphate (See Table H). TABLE H BLOCK H STUDY DESIGN Form No. API protein citrate phosphate succinate HIS ACETATE Gly Arg mannitol NaCl PS80 1 *** 100 8 18 0 0 0 0 0 65 100 0.1 2 *** 100 0 0 0 10 0 120 120 0 0 0.1 3 *** 50 0 0 0 0 0 0 0 65 100 0.1 4 *** 50 0 0 0 0 0 120 120 0 0 0.1 5 *** 50 0 0 0 0 0 120 120 0 0 0 6 *** 50 0 0 0 10 10 0 0 65 100 0.1 7 *** 50 0 0 10 10 0 0 0 65 100 0.1 8 *** 50 0 10 0 10 0 0 0 65 100 0.1 9 *** 50 0 0 10 0 10 0 0 65 100 0.1 10 *** 50 10 0 10 0 0 0 0 65 100 0.1 11 *** 50 10 0 0 10 0 0 0 65 100 0.1 12 *** 50 0 0 10 10 0 120 100 0 0 0.1 *** denotes proprietary adalimumab biosimilar TABLE H-1 Measured pH for Block H formulations at t0, t1 (one week, 40° C.), and t2 (two weeks, 40° C.) Form No. protein Citrate Phosphate Succinate Histidine acetate Gly Arg Mannitol NaCl PS80 t0 t1 t2 1 100 8 18 0 0 0 0 0 65 100 0.1 5.19 5.30 5.29 2 100 0 0 0 10 0 120 120 0 0 0.1 5.20 5.19 5.15 3 50 0 0 0 0 0 0 0 65 100 0.1 5.21 5.23 5.21 4 50 0 0 0 0 0 120 120 0 0 0.1 5.21 5.41 5.46 5 50 0 0 0 0 0 120 120 0 0 0 5.21 5.30 5.39 6 50 0 0 0 10 10 0 0 65 100 0.1 5.20 5.28 5.28 7 50 0 0 10 10 0 0 0 65 100 0.1 5.21 5.24 5.24 8 50 0 10 0 10 0 0 0 65 100 0.1 5.20 5.17 5.16 9 50 0 0 10 0 10 0 0 65 100 0.1 5.21 5.24 5.29 10 50 10 0 10 0 0 0 0 65 100 0.1 5.20 5.24 5.26 11 50 10 0 0 10 0 0 0 65 100 0.1 5.21 5.24 5.26 12 50 0 0 10 10 0 120 100 0 0 0.1 5.21 5.26 5.29 TABLE H-2 Monomer content by SEC for formulations in Block H at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. protein Citrate Phosphate Succinate Histidine acetate Gly Arg mannitol NaCl PS80 t0 t1 t2 1 100 8 18 0 0 0 0 0 65 100 0.1 99.25 98.36 98.42 2 100 0 0 0 10 0 120 120 0 0 0.1 99.19 98.88 98.47 3 50 0 0 0 0 0 0 0 65 100 0.1 99.06 98.81 98.74 4 50 0 0 0 0 0 120 120 0 0 0.1 99.19 99.06 98.99 5 50 0 0 0 0 0 120 120 0 0 0 99.26 99.03 98.96 6 50 0 0 0 10 10 0 0 65 100 0.1 99.26 98.92 98.86 7 50 0 0 10 10 0 0 0 65 100 0.1 99.14 98.98 98.93 8 50 0 10 0 10 0 0 0 65 100 0.1 99.11 98.93 98.66 9 50 0 0 10 0 10 0 0 65 100 0.1 99.16 98.79 98.63 10 50 10 0 10 0 0 0 0 65 100 0.1 99.10 98.79 98.49 11 50 10 0 0 10 0 0 0 65 100 0.1 99.21 98.93 98.18 12 50 0 0 10 10 0 120 100 0 0 0.1 99.30 99.22 98.65 TABLE H-3 Percent purity by RP HPLC for formulations in Block F at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. protein citrate phosphate succinate histidine acetate Gly Arg mannitol NaCl PS80 t0 t1 t2 1 100 8 18 0 0 0 0 0 65 100 0.1 99.36 99.64 99.64 2 100 0 0 0 10 0 120 120 0 0 0.1 99.37 99.68 99.74 3 50 0 0 0 0 0 0 0 65 100 0.1 99.45 99.47 99.70 4 50 0 0 0 0 0 120 120 0 0 0.1 99.50 99.69 99.59 5 50 0 0 0 0 0 120 120 0 0 0 99.47 99.71 99.56 6 50 0 0 0 10 10 0 0 65 100 0.1 99.48 99.56 99.72 7 50 0 0 10 10 0 0 0 65 100 0.1 99.43 99.45 99.72 8 50 0 10 0 10 0 0 0 65 100 0.1 99.43 99.51 99.72 9 50 0 0 10 0 10 0 0 65 100 0.1 99.47 99.55 99.72 10 50 10 0 10 0 0 0 0 65 100 0.1 99.48 99.53 99.67 11 50 10 0 0 10 0 0 0 65 100 0.1 99.45 99.69 99.60 12 50 0 0 10 10 0 120 100 0 0 0.1 99.44 99.54 99.72 TABLE H-4 Percentage of bands for light chain (LC), heavy chain (HC), non-glycosylated HC, and other species for formulations in Block H at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. Time LC HC ngHC Other 1 t0 32.87 65.48 0.54 1.11 t1 28.08 70.09 0.58 1.25 t2 52.57 47.43 0.00 0.00 2 t0 36.20 62.40 0.55 0.86 t1 29.64 68.68 0.57 1.11 t2 43.09 55.23 0.57 1.10 3 t0 34.70 63.55 0.57 1.18 t1 28.24 69.72 0.61 1.57 t2 34.25 63.97 0.67 1.11 4 t0 41.04 57.61 0.51 0.84 t1 27.58 70.65 0.62 1.15 t2 34.14 64.01 0.60 1.26 5 t0 37.64 60.77 0.50 1.09 t1 28.07 70.02 0.61 1.30 t2 37.67 60.76 0.55 1.02 6 t0 31.64 66.46 0.55 1.34 t1 27.67 70.19 0.50 1.64 t2 34.07 63.49 0.62 1.81 7 t0 30.38 69.10 0.53 0.00 t1 27.14 70.55 0.62 1.69 t2 46.41 51.21 0.00 2.38 8 t0 28.46 71.19 0.35 0.00 t1 30.05 68.71 0.55 0.69 t2 34.14 63.97 0.63 1.25 9 t0 27.74 70.63 0.60 1.03 t1 27.48 70.48 0.61 1.43 t2 36.56 61.59 0.49 1.36 10 t0 t1 27.69 70.46 0.60 1.24 t2 11 t0 27.64 70.83 0.57 1.13 t1 31.85 66.08 0.61 1.46 t2 38.58 59.26 0.52 1.64 12 t0 29.48 68.55 0.58 1.40 t1 29.53 68.68 0.58 1.40 t2 30.64 68.20 0.70 0.46 TABLE H-5 Percentage of main bands seen in the cIEF profile of formulations in Block H at t0, t1 (one week at 40° C.), and t2 (two weeks at 25° C.) Form No. pH t0 t1 t2 1 8.55 1.20 1.17 1.21 8.39 9.57 5.57 8.23 8.23 46.84 38.18 39.78 7.99 13.67 12.64 11.62 7.81 6.93 4.61 3.70 2 8.43 1.17 1.06 1.38 8.26 8.97 8.15 8.38 8.09 45.46 40.27 39.95 7.87 13.37 16.45 6.77 7.72 5.47 5.39 9.55 7.56 1.64 1.52 3.33 3 8.36 0.80 0.74 0.61 8.16 6.02 6.03 7.30 7.98 35.60 35.58 37.24 7.83 11.75 14.10 13.15 7.64 2.17 4.78 2.00 7.51 1.23 1.81 4 8.40 0.82 0.74 0.30 8.22 7.87 7.38 6.29 8.04 42.46 34.42 35.89 7.89 14.44 13.71 11.34 7.71 3.18 3.31 2.69 7.56 0.98 0.95 5 8.42 0.82 1.02 8.25 7.22 5.09 8.07 34.68 28.99 7.91 2.67 3.63 7.86 10.63 7.83 7.72 2.52 2.05 6 8.42 1.17 1.28 1.22 8.23 9.88 8.56 7.90 8.09 45.26 40.45 40.80 7.94 13.23 16.50 13.28 7 8.59 1.79 1.45 1.90 8.45 11.74 11.32 11.51 8.28 59.90 61.63 56.22 8.05 20.34 19.49 22.98 7.92 6.24 6.11 7.39 8 8.58 1.59 2.94 1.38 8.44 11.86 12.83 12.12 8.26 61.08 60.20 63.05 8.05 20.21 24.03 23.45 7.88 5.25 6.55 9 8.61 1.22 1.42 1.21 8.48 12.47 12.36 11.00 8.33 56.64 54.59 55.34 8.10 23.37 23.81 25.31 7.94 6.30 7.83 Results of Block H The pH stability of these formulations was acceptable (<0.1 units), except for Formulations 4 and 5. These are the buffer-free formulations using Gly and Arg as the stabilizers (Table H-1). There was also a slight rise in pH for Formulation 1 (the Humira® formulation at 100 mg/ml protein concentration). Stability of Block H formulations was monitored using SEC and RP HPLC. There is little loss in monomer content, with Formulation 1 appearing to be the least stable by SEC (Table H-2). At 100 mg/ml of adalimumab biosimilar API the histidine-buffered formulation containing Gly and Arg appears to be quite stable. In general, the best buffer combination appears to be His-succinate (Formulations 7 and 12). Buffer-free formulations with Gly and Arg show acceptable stability as well (Table H-2). The RP HPLC data indicate that the buffer-free formulations (4 and 5) may not do quite as well as shown by SEC (Table H-3), with measurable decreases in purity, but are believed to be satisfactory for obtaining a formulation having long term stability. The CE-SDS data detect the least change in Formulation 12, which is a His-succinate formulation (Table H-4). The largest change at t1 occurs with Formulation 7, which is also a His-succinate formulation, but using mannitol and NaCl as the tonicity modifiers. PLS Modeling PLS Method The data for the adalimumab formulations in Blocks A through H were analyzed together using a chemometric method termed partial least squares (PLS). Detailed descriptions of PLS modeling have been published. See, for example, Katz, M. H. Multivariate Analysis: A Practice Guide for Clinicians. Cambridge University Press, New York, pp. 158-162 (1999); Stahle, L., Wold, K., Multivariate data analysis and experimental design in biomedical research. Prog. Med. Chem. 1988, 25: 291-338; Wold S. PLS-regression: a basic tool of chemometrics. Chemom. Intell. Lab. Syst. 2001, 58: 109-130; and Martens, H.; Martens, M. Multivariate Analysis of Quality: An Introduction, Wiley and Sons, Chichester, UK (2001). For any large matrix of values, where there are a reasonable number of samples (together forming the so-called X-matrix), mathematical models can be constructed that explain the largest amount of variance in the dependent variable(s) of interest (the Y-matrix). The best single description of the relationship between the variation in the X-matrix and the endpoint (the Y matrix) is called the first principal component, PC1. The next important (in terms of describing the variance in the Y-matrix) component is called the second principal component, PC2, and so on. Quite often, only one or two PCs are required to explain most of the variance in the Y-matrix. Each of these PCs contains some contribution from each of the variables in the X-matrix. If a variable within the X-matrix contributes heavily to the construction of a given PC, then it is ranked as being significant. In fact, regression coefficients can be calculated for each variable in the X-matrix for a given model, where a model is the composite of a certain number of PCs in order to provide an adequate description of the Y-matrix. In summary, PLS takes information from the X-matrix, calculates the desired number of PCs, and constructs a suitable model. The model that includes all of the samples is termed a calibration model [1,2]. The overall coefficient of determination (r2) indicates the quality of the model. All PLS calculations were conducted using Unscrambler® software (CAMO, Corvallis, Oreg.). A PLS analysis done with a single variable in the Y-matrix is termed PLS1 analysis. Building a model that fits multiple variables in the Y-matrix is called PLS2 analysis. A full cross validation was performed on all calibration models using standard techniques. Briefly, one sample is removed at a time, the data set is recalibrated, and a new model is constructed. This process is repeated until all of the calibration samples are removed once and quantified as a validation model. Therefore, the first set, containing all samples is referred to as the calibration set and the one after cross-validation as the validation set. The jack-knife algorithm (See, Martens et al) was used to determine statistical significance for any factor used in constructing the PLS models described above. PLS Modeling of Adalimumab Formulations Blocks B, C and D See FIGS. 3 Through 12 Note: The PLS surface graphs depicted in FIGS. 3 through 12 are based on the data obtained from Blocks B, C and D. The following is a discussion of the findings reflected in the PLS surface plots shown in FIGS. 3 through 12. PLS Model 1—FIG. 3. FIG. 3 contains a depiction of the monomer content at t1 (model 1) as a function of citrate and phosphate concentrations. The pH has been fixed at 5.2. The model indicated that phosphate and citrate by themselves were weak destabilizers (not to statistical significance), along with tartrate and maleate. By comparison, succinate, which is structurally similar to citrate, tartrate and maleate, was a weak stabilizer. The only buffer found to be a significant stabilizer was histidine. None of these findings could have been predicted based on the literature or examination of the chemical structure of each buffer. The model also indicated that when citrate and phosphate buffer are used together, the formulation is least stable. If one only uses a single buffer, especially phosphate, stability improves. This is surprising, as phosphate has little or no buffer capacity at pH 5.2, while citrate buffer does. None of this behavior could have been predicted based on what was known in the art. PLS Model 2—FIG. 4. FIG. 4 contains a depiction of the monomer content at t2 (model 2). Likewise, a model was constructed using the monomer content by SEC at t2 as the endpoint. This model also demonstrated that the stability is lowest when citrate and phosphate are used together. The lowest stability was shown when citrate is above 10 mM and phosphate is between 5 and 15 mM. Stability improves when the citrate concentration is lowered and/or phosphate concentration is lowered or raised. These findings suggest that a single buffer composition is preferred. The same trend in buffer stabilization is seen as with PLS Model 1, with citrate and phosphate being weak stabilizers (not statistically significant), while histidine is a strong stabilizer (statistically significant). PLS Model 1—FIG. 5. FIG. 5 is a PLS model 1 showing the effect of histidine and glycine on the stability of formulations. It contains a depiction of the monomer content at t1 (model 1). This model indicated that the combination of histidine and glycine yielded very good stability results. Both histidine (His) and glycine (Gly) were determined to be stabilizers. The lowest stability on the response surface (shown in blue) is when there is the lowest concentration of His and Gly. The effect of His on stability is greater, with 20 mM His providing comparable stabilization to 120 mM Gly (note the opposite corners of the graph). The model indicates that there will be an additive benefit to stability by using both excipients, with the highest stability occurring when the His concentration is 20 mM and the Gly concentration is 120 mM. PLS Model 1—FIG. 6. FIG. 6 is a PLS model 1 showing the effect of arginine and sorbitol on the stability of formulations. It contains a depiction of the monomer content at t1 (model 1). This model indicated that arginine was a good stabilizer, while sorbitol was a poor stabilizer. Likewise, arginine (Arg) provides a degree of stabilization that is similar to that found for Gly. The poorest stability as indicated by this model is when the Arg concentration is low and the sorbitol concentration is low (the blue area of the graph). As the concentrations of each excipient are increased, the monomer content at t1 is increased. The effect of sorbitol is roughly linear with concentration, while the effect of Arg appears to be increasing more rapidly once the concentration exceeds 60 mM. Even though sorbitol is predicted to increase the stability of adalimumab in terms of retained monomer content, its ability to increase stability is less than that found for Gly and Arg (on a molar basis). PLS Model 1—FIG. 7. FIG. 7 is a PLS model 1 showing the effect of pH and histidine on the stability of formulations. It contains a depiction of the monomer content at t1 (model 1). This model indicated that histidine appears to be the best buffer, while pH should preferably be at 5 or higher for best stability. PLS Model 2—FIG. 8. FIG. 8 is a PLS model 2 showing the effect of pH and histidine on the stability of formulations. It contains a depiction of the monomer content at t2 (model 2). This model indicated that histidine appears to be the best buffer, while pH should preferably be at 5 or higher for best stability. The results indicate that the optimal pH is near 5.2. Of all of the buffers that were examined, histidine provides the greatest degree of stabilization. This response surface illustrates two important points. First, the stability appears to be maximal near pH 5.2, falling off at a higher and lower pH. Second, histidine is shown to provide a significant increase in stability. When histidine is used at 20 mM, it provides a marked increase in stability over lower buffer concentrations. In fact, the effect appears to be non-linear, with more stabilization occurring from 10 to 20 mM than from 0 to 10 mM. Further, the loss in stability is more abrupt at higher pH than at lower pH. PLS Model 2—FIG. 9. FIG. 9 is a PLS model 2 showing the effect of trehalose and PS80 on the stability of formulations. It contains a depiction of the monomer content at t2. This model indicated that trehalose appears to be a weak stabilizer, while PS80 improves thermal stability. The response surface shown in FIG. 9 indicates that PS 80 is a potent stabilizer for protecting adalimumab against thermal stress, with a concentration of 0.1% providing maximal stability. The concentration of PS 80 has not been varied other than at 0 and 0.1%. By comparison, this model shows that the stabilization effect of trehalose is quite small, certainly less than what was seen with sorbitol. PLS Model 2—FIG. 10. FIG. 10 is a PLS model 2 showing the effect of mannitol and PS80 on the stability of formulations. It contains a depiction of the monomer content at t2 (model 2). This model indicated that mannitol appears to be a destabilizer, while PS80 improves thermal stability. The PLS model using monomer content by SEC at t2 allows one to examine the relative effects of any of the factors included in the model. As the mannitol concentration increases, the overall stability decreases. By comparison, the impact of PS80 on the stability is rather small. PLS Model 1—FIG. 11. FIG. 11 is a PLS model 1 showing the effect of mannitol and NaCl on the stability of formulations. It contains a depiction of the monomer content at t1 (model 1). This model indicated that mannitol and NaCl both appear to be destabilizers. The stability, as indicated by the monomer content at t1, is lowest when the mannitol concentration is anywhere below 150 mM. Likewise, addition of NaCl also diminishes the stability of adalimumab. PLS Model 1—FIG. 12. FIG. 12 is a PLS model 1 showing the effect of EDTA and methionine on the stability of formulations. It contains a depiction of the monomer content at t1. In the case of EDTA, the stability decreases slightly as the concentration of this additive increases. In contrast, addition, of Met appears to improve stability. PLS Modeling of Adalimumab Formulations for Blocks B Through G See FIGS. 13 Through 28 The First PLS Model (“PLS Model A) The first PLS model (PLS Model A) used difference in monomer content at t1 as the endpoint. The model employed three PCs and had a correlation coefficient for the calibration set of 0.83 and a r-value of 0.67 for the validation set. It was a quadratic model including pH-buffer and buffer-buffer interaction terms. TABLE J PLS “MODEL A” COEFFICIENTS Factor r-value pH t0 0.041 protein −0.025 citrate +0.123 phos +0.267 succinate −0.089 histidine −0.174 acetate −0.053 glycine −0.190 arginine −0.128 sorbitol −0.003 trehalose +0.020 mannitol −0.104 NaCl +0.250 F68 +0.018 PS 20 +0.021 PS 80 −0.152 EDTA +0.112 Met −0.062 Note: Overall correlation coefficients for each linear factor includes in the first PLS model (PLS Model A) using the difference in monomer content by SEC at t1 as the endpoint. Factors deemed to be statistically significant are highlighted in bold text. The model quality is acceptable, considering the correlation coefficients of the calibration and validation sets. The overall correlation coefficients for the various factors included in the model are summarized in Table J. Note that the quadratic and interaction terms are not listed here. As the endpoint is the difference in monomer content, one wishes to minimize this value. Thus, stabilizers exhibit negative correlation coefficients, while destabilizers have positive r-values. Of the stabilizers, His, Gly, Arg, and PS 80 are the most potent, although mannitol and succinate also have a stabilizing effect (Table J). Meanwhile, there are some significant destabilizers, such as NaCl, citrate, and phosphate. Keep in mind that these models are a composite of all of the stability data gathered across the various blocks of formulations, A through H, and individual formulations could vary from the model. While the table of correlation coefficients is helpful to gauge the effects of various factors, they do not capture the non-linear and interaction effects, so it is helpful to view response surfaces to examine the effects of various parameters in greater detail, as shown in the response surfaces that are reproduced in FIGS. 13 through 28. Discussion of PLS Model A—FIGS. 13 and 14. The Krause '583 patent describes the citrate-phosphate buffer system as being integral to product stability. Our studies show this not to be the case. The poorest stability would occur when these two buffers were used in combination and the effect would get worse as the buffer concentrations increase, according to this model (FIG. 13[1]). The response surface indicates that the phosphate and citrate are equally destabilizing, contrary to some earlier observations, but the quantitative nature of these surfaces must be considered with some care as they include data from all of the formulations from Blocks B through H. The effect of pH and His is shown in FIG. 14. It shows that His is destabilizing at low pH, where it is clearly outside of the buffer capacity of His. Again, this result is a function of all pH observations in this study, not just those involving His (although this could be done). According to this response surface, the optimal pH may be nearer to 5.4 than 5.2, although the surface is relatively flat through this region, indicating a shallow response surface from pH 5 to 5.4 (FIG. 14). Discussion of PLS Model A—FIG. 15 The response surface for Gly and Arg is shown in FIG. 15. The studies repeatedly show that these two amino acids can be potent stabilizers of adalimumab. Note that the minimum difference in monomer content (i.e., the blue part of the surface) is reached at 100 mM Arg, but at 200 mM Gly, suggesting that Arg may be the better stabilizer for adalimumab at pH 5.2. Discussion of PLS Model A—FIG. 16 The final response surface shown for PLS Model A is for the effect of NaCl and PS 80 (FIG. 16). It shows that the stability of adalimumab decreases upon addition of NaCl, especially above 100 mM. Meanwhile, PS 20 provides significant stability when used above 0.04%. The Second PLS Model (PLS Model B) The second PLS model (PLS Model B) used the monomer content at t1 and at t2 as the endpoints. The model employed four PCs and had a correlation coefficient for the calibration set of 0.82 and a r-value of 0.67 for the validation set. It was a quadratic model including pH-buffer and buffer-buffer interaction terms. In terms of model quality, this is comparable to the first PLS Model A described above. TABLE K (L) PLS “MODEL B” CORRELATION COEFFICIENTS Factor r-value pH −0.086 protein +0.030 citrate −0.079 phos −0.157 succinate +0.060 histidine +0.185 acetate +0.063 glycine +0.126 arginine +0.150 sorbitol +0.025 trehalose +0.006 mannitol +0.014 NaCl −0.215 F68 −0.044 PS 20 −0.028 PS 80 +0.227 EDTA −0.097 Met +0.096 The endpoints for PLS Model B are the total monomer contents at both t1 and t2. Therefore, one will wish to maximize these values. This means that stabilizers with have positive correlation coefficients and destabilizers will display negative r-values (Table K). As with the previous model, citrate, phosphate, and NaCl are significant destabilizers. On the other hand, His, Gly Arg, and PS 20 are potent stabilizers. In this model, trehalose, sorbitol and mannitol have very little effect. The primary differences are that pH is now a significant factor and that EDTA is a significant destabilizer, while Met appears to be a stabilizer as well. Discussion of PLS Model B—FIG. 17 This model suggests that addition of citrate has little effect on stability if phosphate is absent (view the back edge of the response surface of FIG. 5). On the other hand, added phosphate does decrease monomer content (view the right hand edge) and the combination is even more destabilizing (FIG. 5). Thus, the citrate-phosphate buffer combination is not effective at stabilizing adalimumab, contrary to what is taught by the '583 patent. The destabilizing effect of phosphate is about three-fold greater than for citrate according to this model. Discussion of PLS Model 6—FIG. 18 The use of His at low pH has little or detrimental effects (FIG. 18[6\\). However, when employed at pH 5.2 or above, the His provides a significant increase in stability (as measured by monomer content by SEC). Discussion of PLS Model B—FIG. 19 The response surface for Gly and Arg is shown in FIG. 19. Including both stabilizers at high concentrations would be beneficial for stability, but impractical for tonicity reasons. It does appear that Arg is the more potent stabilizer in this model compared to Gly, where a 75 mM concentration of Arg has the same effect as ˜120 mM Gly. The model indicates either one alone would work well, or that a combination would be effective as well. Discussion of PLS Model 6—FIG. 20 The PLS model B shows a modest effect of mannitol on stability, whereas PS 80 is an effective stabilizer above concentrations near 0.05% (FIG. 20). Thus, one could conclude from this data that a stable formulation could be comprised of 240 mM mannitol and 0.1% PS 80 at pH 5.2. Discussion of PLS Model B—FIG. 21 Throughout the project, it appears that NaCl is a destabilizer of adalimumab, especially when the concentration reach 100 mM or above, as shown in this response surface (FIG. 21). While only a few formulations were tested that included EDTA, it appears that this excipient is destabilizing, unless the concentration were ˜0.1%. We also note that the effect of Met was favorable with respect to stability, but it did not prove to be a significant effect, probably because relatively few examples were evaluated. Discussion of PLS Model B—FIG. 22 The final response surface from the PLS Model B to be considered is the effect of succinate and His (FIG. 22). The model did include all relevant buffer-buffer interactions. This surface shows that succinate has little or even deleterious effects on its own (see the front edge of the plot). However, in conjunction with His it proves to increase the overall stability (e.g., note that back edge of the surface). Therefore, a His-succinate buffer system appear to be the most favorable of all of the buffer combinations tested to date. The Third PLS Model (PLS Model C) The third PLS model C used the difference in percent purity by RP HPLC at t1 as the endpoint. The model employed two PCs and had a correlation coefficient for the calibration set of 0.86 and a r-value of 0.67 for the validation set. It was a quadratic model including pH-buffer and buffer-buffer interaction terms. In terms of model quality, this is very similar to the previous model. TABLE L PLS “MODEL C” CORRELATION COEFFICIENTS Factor r-value pH −0.115 protein −0.139 citrate +0.014 phosphate +0.084 succinate −0.051 histidine −0.075 acetate +0.159 glycine −0.096 arginine −0.045 sorbitol +0.029 trehalose +0.020 mannitol −0.060 NaCl +0.068 F68 −0.047 PS 20 −0.067 PS 80 −0.028 EDTA +0.099 Met −0.015 PLS Model C demonstrates that RP HPLC is stability-indicating, even though the sensitivity may be less than for SEC. The model finds that both phosphate and citrate are destabilizing, with the effect of phosphate being statistically significant (Table LI). Likewise, acetate is a strong destabilizer as is EDTA. Both Gly and Arg are shown to be stabilizers, but the effects are not deemed to be statistically significant. Only His was found to be a significant stabilizer (along with protein concentration). Discussion of PLS Model C—FIG. 23 The response surface for citrate and phosphate at pH 5.2 is shown in FIG. 23[11]. Both buffers are destabilizing (follow the front and left-hand edges of the plot). Above concentrations of ˜10 mM, the combination becomes quite destabilizing. Overall, phosphate is predicted to be more destabilizing according to this model (FIG. 11). Discussion of PLS Model C—FIG. 24 As seen in previous models, the stability of adalimumab decreases as the pH is reduced to less than 5.0 (FIG. 12). In this model the stabilizing effect of His is seen across all pH values, but is most pronounced when the pH is lower. Discussion of PLS Model C—FIG. 25 The effects of Gly and Arg are seen in FIG. 25. Both excipients decrease loss of purity as the concentration increases and they are predicted to be roughly equipotent, as judged by the slopes along the edges of the response surface. Otherwise, it appears that it takes less Arg (75 mM) to achieve optimal loss of purity (the blue region of the graph) than for Gly (˜200 mM). Discussion of PLS Model C—FIG. 26 The effect of mannitol and PS 80 is seen in the response surface in FIG. 26[14]. It is clear that chemical stability is greatly improved by adding PS 80, especially at concentrations above 0.04%. Meanwhile, mannitol is also stabilizing, but even 240 mM mannitol has less effect than a small about of the surfactant. Discussion of PLS Model C—FIG. 27 While mannitol is believed to be a stabilizer in the Humira® formulation, NaCl is clearly a destabilizer, both in this model (See FIG. 27[15]), and in previous PLS models. The effect is substantial when the NaCl concentration exceeds 75 mM or so. Discussion of PLS Model C—FIG. 28 The final response surface from PLS Model C is seen in FIG. 28[16] describing the effects of pH and protein concentration. As seen before, the stability is best when the pH is above 4.8 or 5.0. As for the protein effect, this model predicts that the stability, based on RP HPLC, is better at higher protein concentrations. A similar trend, albeit a fairly weak one, was seen for the SEC data (monomer content at t1 and t2). Therefore, it may be possible to achieve similar stability profiles at concentrations at 100 mg/ml as one could obtain at 50 mg/ml. Summary of Findings for Blocks a Through H The formulation studies in Blocks A through H evaluated adalimumab formulations stored at elevated temperature and held for either one week at 40° C. or for two weeks at 25° C. The stability was monitored using SEC, RP HPLC, cIEF and CE-SDS. The optimal pH appears to be 5.2±0.2. Of all of the buffer compositions tested, the citrate-phosphate combination is inferior to nearly any other buffer system evaluated, hence an important aspect of the present invention is the avoidance of this combined buffer system altogether. The best single buffer appears to be His, while a His-succinate buffer also offers very good stability. Even buffer-free systems, which rely on the ability of the protein to buffer the formulation, appear to have acceptable stability profiles under accelerated stress conditions. Of all of the stabilizers/tonicity modifiers evaluated, both Arg and Gly elicit very good stabilization of adalimumab. They both work better than mannitol. Mannitol does appear to be a stabilizer, however we have discovered that if used it should be at the highest possible concentrations, but in any event exceeding about 150 mM, ad most preferably at or exceeding about 200 mM. By comparison, NaCl is clearly a destabilizer, especially when the concentrations exceed 75-100 mM; hence, NaCl, if present should be controlled to levels below about 75 mM. Other polyols, such as sorbitol and trehalose, appear to work about as well as mannitol and therefore may be substituted for mannitol if desired. Surprisingly, polysorbate 80 (PS 80) provides significant protection against thermal stress. While the mechanism of stabilization is not known, it appears that other surfactants tested (PS 20 and F-68), do not appear to be nearly as effective as PS 80. Hence the selection of PS80 versus PS 20 is a preferred feature of the present invention. Formulations according to the present invention preferably contain at least 0.04% (w/v) PS 80. Based on the findings in the formulation studies of Blocks A through H, the following are particularly preferred adalimumab formulations according to the present invention. TABLE M SELECTED FORMULATIONS NaCl PS 80 Form No pH His (mM) succinate (mM) Gly (mM) Arg (mM) mannitol (mM) (mM) (wt %) A 5.2 30 0 240 0 0 0 0.1 B 5.2 30 0 240 0 0 0 0.02 C 5.2 30 0 0 0 240 0 0.1 D 5.2 30 15 0 0 220 0 0.1 E 5.2 30 0 90 0 150 0 0.1 F 5.2 30 0 240 0 0 0 0 G 5.2 20 0 0 0 240 0 0 H 5.4 30 0 240 0 0 0 0.02 I 5.2 30 0 120 80 0 0 0.1 J 5.2 30 15 90 80 0 0 0.1 K 5.2 30 0 0 0 240 0 0.1 L 5.2 30 0 0 50 160 0 0.1 M 5.2 30 0 90 100 0 0 0.1 N 5.2 20 0 120 90 0 0 0.1 O 5.4 30 0 120 80 0 0 0.1 P 5.2 30 0 120 0 0 50 0.01 Q 5.2 30 0 0 0 240 0 0.02 Additional Components of the Provided Pharmaceutical Compositions The formulations of the invention may also include other buffers (unless they are specifically excluded in the description of the specific embodiments of the invention), tonicity modifiers, excipients, pharmaceutically acceptable carriers and other commonly used inactive ingredients of the pharmaceutical compositions. A tonicity modifier is a molecule that contributes to the osmolality of a solution. The osmolality of a pharmaceutical composition is preferably adjusted to maximize the active ingredient's stability and/or to minimize discomfort to the patient upon administration. It is generally preferred that a pharmaceutical composition be isotonic with serum, i.e., having the same or similar osmolality, which is achieved by addition of a tonicity modifier. In a preferred embodiment, the osmolality of the provided formulations is from about 180 to about 420 mOsM. However, it is to be understood that the osmolality can be either higher or lower as specific conditions require. Examples of tonicity modifiers suitable for modifying osmolality include, but are not limited to amino acids (not including arginine) (e.g., cysteine, histidine and glycine), salts (e.g., sodium chloride or potassium chloride) and/or sugars/polyols (e.g., sucrose, sorbitol, maltose, and lactose). In a preferred embodiment, the concentration of the tonicity modifier in the formulation is preferably between about 1 mM to about 1 M, more preferably about 10 mM to about 200 mM. Tonicity modifiers are well known in the art and are manufactured by known methods and available from commercial suppliers. Suitable tonicity modifiers may be present in the compositions of the invention unless they are specifically excluded in the description of the specific embodiments of the invention. Excipients, also referred to as chemical additives, co-solutes, or co-solvents, that stabilize the polypeptide while in solution (also in dried or frozen forms) can also be added to a pharmaceutical composition. Excipients are well known in the art and are manufactured by known methods and available from commercial suppliers. Examples of suitable excipients include but are not limited to sugars/polyols such as: sucrose, lactose, glycerol, xylitol, sorbitol, mannitol, maltose, inositol, trehalose, glucose; polymers such as: serum albumin (bovine serum albumin (BSA), human SA or recombinant HA), dextran, PVA, hydroxypropyl methylcellulose (HPMC), polyethyleneimine, gelatin, polyvinylpyrrolidone (PVP), hydroxyethylcellulose (HEC); non-aqueous solvents such as: polyhydric alcohols, (e.g., PEG, ethylene glycol and glycerol) dimethysulfoxide (DMSO) and dimethylformamide (DMF); amino acids such as: proline, L-serine, sodium glutamic acid, alanine, glycine, lysine hydrochloride, sarcosine and gamma-aminobutyric acid; surfactants such as: Tween®-80 (polysorbate 80), Tween®-20 (polysorbate 20), SDS, polysorbates, poloxamers; and miscellaneous excipients such as: potassium phosphate, sodium acetate, ammonium sulfate, magnesium sulfate, sodium sulfate, trimethylamine N-oxide, betaine, CHAPS, monolaurate, 2-O-beta-mannoglycerate or any combination of the above. Suitable excipients may be present in the compositions of the invention unless they are specifically excluded in the description of the specific embodiments of the invention. The concentration of one or more excipients in a formulation of the invention is/are preferably between about 0.001 to 5 weight percent, more preferably about 0.1 to 2 weight percent. Methods of Treatment In another embodiment, the invention provides a method of treating a mammal comprising administering a therapeutically effective amount of the pharmaceutical compositions of the invention to a mammal, wherein the mammal has a disease or disorder that can be beneficially treated with adalimumab. In a preferred embodiment, the mammal is a human. Diseases or disorders that can be treated with the provided compositions include but are not limited to rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Wegener's disease (granulomatosis), Crohn's disease (or inflammatory bowel disease), chronic obstructive pulmonary disease (COPD), Hepatitis C, endometriosis, asthma, cachexia, psoriasis, and atopic dermatitis. Additional diseases or disorders that can be treated with the compositions of the present invention include those described in U.S. Pat. Nos. 6,090,382 and 8,216,583 the relevant portions of which are incorporated herein by reference. The provided pharmaceutical compositions may be administered to a subject in need of treatment by injection systemically, such as by intravenous injection; or by injection or application to the relevant site, such as by direct injection, or direct application to the site when the site is exposed in surgery; or by topical application. In one embodiment, the invention provides a method of treatment and/or prevention of rheumatoid arthritis comprises administering to a mammal in need thereof a therapeutically effective amount of one of the provided adalimumab compositions. The therapeutically effective amount of the adalimumab in the provided compositions will depend on the condition to be treated, the severity of the condition, prior therapy, and the patient's clinical history and response to the therapeutic agent. The proper dose can be adjusted according to the judgment of the attending physician such that it can be administered to the patient one time or over a series of administrations. In one embodiment, the effective adalimumab amount per adult dose is from about 1-500 mg/m2, or from about 1-200 mg/m2, or from about 1-40 mg/m2 or about 5-25 mg/m2. Alternatively, a flat dose may be administered, whose amount may range from 2-500 mg/dose, 2-100 mg/dose or from about 10-80 mg/dose. If the dose is to be administered more than one time per week, an exemplary dose range is the same as the foregoing described dose ranges or lower and preferably administered two or more times per week at a per dose range of 25-100 mg/dose. In another embodiment, an acceptable dose for administration by injection contains 80-100 mg/dose, or alternatively, containing 80 mg per dose. The dose can be administered weekly, biweekly, or separated by several weeks (for example 2 to 8). In one embodiment, adalimumab is administered at 40 mg by a single subcutaneous (SC) injection. In some instances, an improvement in a patient's condition will be obtained by administering a dose of up to about 100 mg of the pharmaceutical composition one to three times per week over a period of at least three weeks. Treatment for longer periods may be necessary to induce the desired degree of improvement. For incurable chronic conditions the regimen may be continued indefinitely. For pediatric patients (ages 4-17), a suitable regimen may involve administering a dose of 0.4 mg/kg to 5 mg/kg of adalimumab, one or more times per week. In another embodiment, the pharmaceutical formulations of the invention may be prepared in a bulk formulation, and as such, the components of the pharmaceutical composition are adjusted to be higher than would be required for administration and diluted appropriately prior to administration. The pharmaceutical compositions can be administered as a sole therapeutic or in combination with additional therapies as needed. Thus, in one embodiment, the provided methods of treatment and/or prevention are used in combination with administering a therapeutically effective amount of another active agent. The other active agent may be administered before, during, or after administering the pharmaceutical compositions of the present invention. Another active agent may be administered either as a part of the provided compositions, or alternatively, as a separate formulation. Administration of the provided pharmaceutical compositions can be achieved in various ways, including parenteral, oral, buccal, nasal, rectal, intraperitoneal, intradermal, transdermal, subcutaneous, intravenous, intra-arterial, intracardiac, intraventricular, intracranial, intratracheal, intrathecal administration, intramuscular injection, intravitreous injection, and topical application. The pharmaceutical compositions of this invention are particularly useful for parenteral administration, i.e., subcutaneously, intramuscularly, intravenously, intraperitoneal, intracerebrospinal, intra-articular, intrasynovial, and/or intrathecal. Parenteral administration can be by bolus injection or continuous infusion. Pharmaceutical compositions for injection may be presented in unit dosage form, e.g., in ampoules or in multi-dose containers, with an added preservative. In addition, a number of recent drug delivery approaches have been developed and the pharmaceutical compositions of the present invention are suitable for administration using these new methods, e.g., Inject-Ease®, Genject®, injector pens such as GenPen®, and needleless devices such as MediJector® and BioJector®. The present pharmaceutical composition can also be adapted for yet to be discovered administration methods. See also Langer, 1990, Science, 249:1527-1533. The provided pharmaceutical compositions can also be formulated as a depot preparation. Such long acting formulations may be administered by implantation (for example subcutaneously or intramuscularly) or by intramuscular injection. Thus, for example, the formulations may be modified with suitable polymeric or hydrophobic materials (for example as an emulsion in an acceptable oil) or ion exchange resins, or as sparingly soluble derivatives, for example, as a sparingly soluble salt. The pharmaceutical compositions may, if desired, be presented in a vial, pack or dispenser device which may contain one or more unit dosage forms containing the active ingredient. In one embodiment the dispenser device can comprise a syringe having a single dose of the liquid formulation ready for injection. The syringe can be accompanied by instructions for administration. In another embodiment, the present invention is directed to a kit or container, which contains an aqueous pharmaceutical composition of the invention. The concentration of the polypeptide in the aqueous pharmaceutical composition can vary over a wide range, but is generally within the range of from about 0.05 to about 20,000 micrograms per milliliter (μg/ml) of aqueous formulation. The kit can also be accompanied by instructions for use. In addition to the formulations referenced in the formulation studies of Blocks A through H, the following additional examples are provided as further embodiments of the invention, as are the representative embodiments which are included in Appendices A through C which are to be understood as part of this specification. Example 1 Stabilized Adalimumab Formulation (Simile Buffer) Containing Polyol; without Surfactant A stable aqueous pharmaceutical composition containing adalimumab, using a single buffer, and substantially free of a surfactant may be prepared as follows: Each solid formulation component may be weighed to the amount required for a given volume of formulation buffer. These components may then be combined into a beaker or vessel capable of carrying and measuring the given volume of formulation buffer. A volume of deionized water equal to approximately ¾ of the target given formulation buffer may be added to the beaker, and the components may be solubilized through use of a magnetic stir bar. The pH of the buffer may be adjusted to the target formulation pH using 1 molar sodium hydroxide and/or 1 molar hydrogen chloride. The final formulation buffer volume may then be raised to the target volume through the addition of deionized water. The solution may then be mixed with a magnetic stir bar after final water addition. Adalimumab solution may then be placed in dialysis material housing (such as Thermo Scientific Slide-A-Lyzer MINI Dialysis Unit 10,000 MWCO), which may then be placed in contact with the desired formulation buffer for 12 hours at 4° C. Formulation buffer volume to protein solution volume ratio should be no less than 1000:1. The dialysis housing and protein solution it contains may then be placed in a second, equal volume of formulation buffer for an additional 12 hours at 4° C. Resulting adalimumab solution may then be removed from the dialysis material housing, and the concentration of adalimumab may then be determined using ultraviolet spectroscopy. Adalimumab concentration may then be adjusted to the desired level using centrifugation (such as Amicon Ultra 10,000 MWCO Centrifugal Concentrators) and/or dilution with formulation buffer. A sample composition of the invention is represented in Table 1 below: TABLE 1 Ingredient concentration Adalimumab (active ingredient) 50 mg/ml Mannitol (inactive ingredient) 4% Citrate (pH 5.2) (single buffer) 15 mM The composition disclosed in Table 1 does not contain a combination of citrate and phosphate buffer. It also does not require the presence of a surfactant. Example 2 Stabilized Adalimumab Formulation (Single Buffer) without Polyol or Surfactant Ingredient concentration Adalimumab (active ingredient) 50 mg/ml Citrate (pH 5.2) 15 mM Glycine (inactive ingredient) 100 mM Example 3 Stabilized Adalimumab Formulation (Single Buffer) Containing Polyol without Surfactant Ingredient concentration Adalimumab (active ingredient) 50 mg/ml Mannitol (inactive ingredient) 4% Citrate (pH 5.2) 15 mM The compositions of examples 2 and 3 have long term stability and do not contain a combination of citrate and phosphate buffer, and do not require the presence of a surfactant. Example 4 Stabilized Adalimumab Formulation (Simile Buffer) Containing Surfactant; without Polyol Ingredient concentration 4A Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Histidine Buffer (pH 5.2) (sole buffer) 20 mM Glycine (stabilizer) 50 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) 4B Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Histidine Buffer (pH 5.2) (sole buffer) 20 mM Glycine (stabilizer) 120 mM Arginine (stabilizer) 100 mM Polysorbate 80 0.1 (wt %) (w/v) 4C Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Histidine Buffer (pH 5.2) (sole buffer) 10 mM Glycine (stabilizer) 50 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) 4D Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Succinate Buffer (pH 5.2) (sole buffer) 20 mM Glycine (stabilizer) 50 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) 4E Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Succinate Buffer (pH 5.2) (sole buffer) 20 mM Glycine (stabilizer) 120 mM Arginine (stabilizer) 100 mM Polysorbate 80 0.1 (wt %) (w/v) 4F Adalimumab (active ingredient) 50 mg/ml (No polyol ingredient) — Succinate Buffer (pH 5.2) (sole buffer) 10 mM Glycine (stabilizer) 50 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) The compositions disclosed in Examples 4(a) through 4(f) above will afford stability without need for polyol and without need for a combined buffer system. Insofar as the present invention has discovered that the citrate/phosphate buffer combination required in U.S. Pat. No. 8,216,583 is not required for stabilization of adalimumab formulations according to the present invention, persons skilled in the art may appreciate, in practicing examples 4(a) through 4(f), that additional buffers may be employed in combination with the histidine and succinate buffers disclosed herein (e.g, acetate, citrate, maleate, tartrate, and phosphate buffers); provided the formulation does not use a buffer combination of citrate and phosphate. Example 5 Stabilized Adalimumab Formulation (Simile Buffer) Containing Surfactant; and Polyol Ingredient Concentration 5A Adalimumab (active ingredient) 50 mg/ml Sorbitol 65 mM Histidine Buffer (pH 5.2) (sole buffer) 20 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) 5B Adalimumab (active ingredient) 50 mg/ml Sorbitol 65 mM Succinate Buffer (pH 5.2) (sole buffer) 20 mM Arginine (stabilizer) 130 mM Polysorbate 80 0.1 (wt %) (w/v) The foregoing description of the exemplary embodiments of the invention in the block studies A through H, in the examples above, and in the Appendices A through C, are presented only for the purposes of illustration and description and is not intended to be exhaustive or to limit the invention to the precise forms disclosed. Many modifications and variations are possible in light of the above teaching. Other embodiments of the invention will be apparent to those skilled in the art from consideration of the specification and practice of the invention disclosed herein. It is intended that the specification and examples be considered as exemplary only, with a true scope and spirit of the invention being indicated by the following claims. APPENDIX A Further Representative Embodiments Disclosed in Priority Application U.S. Ser. No. 61/698,138 A. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 5 to about 6, and wherein said buffer does not comprise both of citrate and phosphate. B. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a surfactant, wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a buffer. C. The composition of any of embodiments A-B, wherein said adalimumab is at a concentration from about 20 to about 150 mg/ml. D. The composition of any of embodiments A-C, wherein said adalimumab is at a concentration from about 20 to about 100 mg/ml. E. The composition of any of embodiments A-D, wherein said adalimumab is at a concentration from about 30 to about 50 mg/ml. F. The composition of any of embodiments A-E, wherein said buffer is at a concentration from about 5 mM to about 50 mM. G. The composition of any of embodiments A-F, wherein said buffer is at a concentration from about 5 mM to about 20 mM. H. The composition of any of embodiments A-G, wherein said buffer is at a concentration from about 10 mM to about 20 mM. I. The composition of any of embodiments A-G, wherein said surfactant is a polysorbate. J. The composition of embodiment I, wherein said polysorbate is polysorbate 80. K. The composition of any of embodiments A-J, wherein said polyol is a sugar alcohol. L. The composition of embodiment K, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. M. The composition of embodiment L, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. N. The composition of any of embodiments L-M, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. O. The composition of any of embodiments L-N, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. P. The composition of any of embodiments A-O further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. Q. The composition of embodiment P, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. R. The composition of embodiment P, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. S. The composition of embodiment P, wherein said metal ion is selected from zinc, magnesium and calcium. T. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, mannitol at a concentration from about 1 to 10% weight by volume, polysorbate 80 at a concentration from about 1 to 50 μM, and citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of phosphate. U. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a surfactant. V. The composition of embodiment U, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. W. The composition of any of embodiments U-V, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. X. The composition of any of embodiments U-V, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. Y. The composition of any of embodiments U-Y, wherein said buffer is at a concentration from about 5 mM and about 50 mM. Z. The composition of any of embodiments U-Y, wherein said buffer is at a concentration from about 5 mM and about 20 mM. AA. The composition of any of embodiments U-Z, wherein said buffer is at a concentration from about 10 mM and about 20 mM. BB. The composition of any of embodiments U-AA, wherein said polyol is a sugar alcohol. CC. The composition of embodiment BB, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. DD. The composition of embodiment CC, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. EE. The composition of any of embodiments CC-DD, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. FF. The composition of any of embodiments CC-EE, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. GG. The composition of any of embodiments CC-FF further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. HH. The composition of embodiment GG, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. II. The composition of embodiment GG, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. JJ. The composition of embodiment GG, wherein said metal ion is selected from zinc, magnesium and calcium. KK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, mannitol at a concentration from about 1 to 10% weight by volume, and citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a surfactant. LL. A stable aqueous pharmaceutical composition comprising adalimumab, a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion, and wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a polyol. MM. The composition of embodiment LL, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. NN. The composition of any of embodiments LL-MM, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. OO. The composition of any of embodiments LL-NN, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. PP. The composition of any of embodiments LL-OO, wherein said buffer is at a concentration from about 5 mM and about 50 mM. QQ. The composition of any of embodiments LL-PP, wherein said buffer is at a concentration from about 5 mM and about 20 mM. RR. The composition of any of embodiments LL-QQ, wherein said buffer is at a concentration from about 10 mM and about 20 mM. SS. The composition of embodiment LL, wherein said stabilizer is selected from the group consisting of an amino acid, a salt, EDTA and a metal ion. TT. The composition of embodiment SS, wherein said amino acid is selected from the group consisting of glycine, alanine and arginine. UU. The composition of embodiment SS wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. VV. The composition of embodiment TT, wherein said glycine is at a concentration from about 20 to about 200 mM. WW. The composition of embodiment W, wherein said glycine is at a concentration from about 50 to about 200 mM. XX. The composition of embodiment SS, wherein said arginine is at a concentration from about 1 to about 250 mM. YY. The composition of embodiment XX, wherein said arginine is at a concentration from about 20 to about 200 mM. ZZ. The composition of embodiment YY, wherein said arginine is at a concentration from about 20 to about 100 mM. AAA. The composition of embodiment UU, wherein said sodium chloride is at a concentration from about 5 to about 150 mM. BBB. The composition of embodiment AAA, wherein said sodium chloride is at a concentration from about 20 to about 140 mM. CCC. The composition of embodiment BBB, wherein said sodium chloride is at a concentration from about 75 to about 125 mM. DDD. The composition of embodiment UU, wherein said sodium sulfate is at a concentration from about 5 to about 150 mM. EEE. The composition of embodiment UU, wherein said sodium chloride is at a concentration from about 20 to about 120 mM. FFF. The composition of embodiment EEE, wherein said sodium chloride is at a concentration from about 60 to about 100 mM. GGG. The composition of any of embodiments LL-FF further comprising a surfactant. HHH. The composition of embodiment GGG, wherein said surfactant is a polysorbate. III. The composition of embodiment HHH, wherein said polysorbate is polysorbate 80. JJJ. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, glycine at a concentration from about 20 to about 200 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. KKK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, arginine at a concentration from about 1 to about 250 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH from about 5 to about 5.5, and wherein said composition is substantially free of a polyol. LLL. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. MMM. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, polysorbate 80 at a concentration from about 1 to 50 μM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. NNN. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion, and a buffer selected from the group consisting of citrate, phosphate, succinate, tartrate and maleate, wherein said composition has a pH from about 5 to about 6. OOO. The composition of embodiment NNN, wherein the buffer does not comprise a combination of citrate and phosphate. PPP. The composition of embodiment NNN, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. QQQ. The composition of any of embodiments NNN-PPP, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. RRR. The composition of any of embodiments NNN-QQQ, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. SSS. The composition of any of embodiments NNN-RRR, wherein said buffer is at a concentration from about 5 mM and about 50 mM. TTT. The composition of any of embodiments NNN-SSS, wherein said buffer is at a concentration from about 5 mM and about 20 mM. UUU. The composition of any of embodiments NNN-TTT, wherein said buffer is at a concentration from about 10 mM and about 20 mM. VVV. The composition of any of embodiments NNN-UUU, wherein said surfactant is a polysorbate. WWW. The composition of embodiment VVV, wherein said polysorbate is polysorbate 80. XXX. The composition of any of embodiments NNN-WWW, wherein said polyol is a sugar alcohol. YYY. The composition of embodiment XXX, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. ZZZ. The composition of embodiment XXX, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. AAAA. The composition of any of embodiments XXX-ZZZ, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. BBBB. The composition of any of embodiments YYY-AAAA, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. CCCC. The composition of any of embodiments NNN-BBBB, wherein said stabilizer is EDTA. DDDD. The composition of embodiment CCCC, wherein said EDTA is at a concentration from about 0.01% to about 0.5%. EEEE. The composition of embodiment DDDD, wherein said EDTA is at a concentration from about 0.05% to about 0.25%. FFFF. The composition of embodiment EEEE, wherein said EDTA is at a concentration from about 0.08% to about 0.2%. GGGG. The composition of any of embodiments NNN-BBBB, wherein said stabilizer is methionine. HHHH. The composition of embodiment GGGG, wherein said methionine is at a concentration from about 1 to about 10 mg/ml. IIII. The composition of embodiment GGGG, wherein said methionine is at a concentration from about 1 to about 5 mg/ml. JJJJ. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol at a concentration from about 1 to 10% weight by volume, EDTA at a concentration from about 0.01% to about 0.5%, citrate at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. KKKK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol at a concentration from about 1 to 10% weight by volume, methionine at a concentration from about 1 to about 10 mg/ml, citrate at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. LLLL. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, tartrate and maleate, wherein said composition has a pH of about 3.5. MMMM. The composition of embodiment LLLL, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. NNNN. The composition of any of embodiments LLLL-MMMM, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. OOOO. The composition of any of embodiments LLLL-NNNN, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. PPPP. The composition of any of embodiments LLLL-OOOO, wherein said buffer is at a concentration from about 5 mM and about 50 mM. QQQQ. The composition of any of embodiments LLLL-PPPP, wherein said buffer is at a concentration from about 5 mM and about 20 mM. RRRR. The composition of any of embodiments LLLL-QQQQ, wherein said buffer is at a concentration from about 10 mM and about 20 mM. SSSS. The composition of any of embodiments LLLL-RRRR, wherein said polyol is a sugar alcohol. TTTT. The composition of embodiment SSSS, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. UUUU. The composition of embodiment TTTT, wherein said mannitol is at a concentration from about 1 to about 10% weight by volume of the total composition. VVVV. The composition of any of embodiments TTTT-UUUU, wherein said mannitol is at a concentration from about 2 to about 6% weight by volume of the total composition. WWWW. The composition of any of embodiments TTTT-VVVV, wherein said mannitol is at a concentration from about 3 to about 5% weight by volume of the total composition. XXXX. The composition of any of embodiments LLLL-WWWW further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. YYYY. The composition of embodiment XXXX, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. ZZZZ. The composition of embodiment XXXX, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. AAAAA. The composition of embodiment XXXX, wherein said metal ion is selected from zinc, magnesium and calcium. BBBBB. The composition of any of embodiments TTTT-AAAAA further comprising a surfactant. CCCCC. The composition of embodiment BBBBB, wherein said surfactant is a polysorbate. DDDDD. The composition of embodiment CCCCC, wherein said polysorbate is polysorbate 80. APPENDIX B Further Representative Embodiments Disclosed in Priority Application U.S. Ser. No. 61/770,421 A. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 5 to about 6, and wherein said buffer does not comprise both of citrate and phosphate. B. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a surfactant, wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a buffer. C. The composition of any of embodiments A-B, wherein said adalimumab is at a concentration from about 20 to about 150 mg/ml. D. The composition of any of embodiments A-C, wherein said adalimumab is at a concentration from about 20 to about 100 mg/ml. E. The composition of any of embodiments A-D, wherein said adalimumab is at a concentration from about 30 to about 50 mg/ml. F. The composition of any of embodiments A-E, wherein said buffer is at a concentration from about 5 mM to about 50 mM. G. The composition of any of embodiments A-F, wherein said buffer is at a concentration from about 5 mM to about 20 mM. H. The composition of any of embodiments A-G, wherein said buffer is at a concentration from about 10 mM to about 20 mM. I. The composition of any of embodiments A-H, wherein said surfactant is a polysorbate. J. The composition of embodiment I, wherein said polysorbate is polysorbate 80. K. The composition of any of embodiments A-J, wherein said polyol is a sugar alcohol. L. The composition of embodiment K, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. M. The composition of embodiment L, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. N. The composition of any of embodiments L-M, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. O. The composition of any of embodiments L-N, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. P. The composition of any of embodiments A-O further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. Q. The composition of embodiment P, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. R. The composition of embodiment P, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. S. The composition of embodiment P, wherein said metal ion is selected from zinc, magnesium and calcium. T. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, mannitol at a concentration from about 1 to 10% weight by volume, polysorbate 80 at a concentration from about 1 to 50 μM, and citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of phosphate. UA stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a surfactant. V. The composition of embodiment U, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. W. The composition of any of embodiments U-V, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. X. The composition of any of embodiments U-W, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. Y. The composition of any of embodiments U-X, wherein said buffer is at a concentration from about 5 mM and about 50 mM. Z. The composition of any of embodiments U-Y, wherein said buffer is at a concentration from about 5 mM and about 20 mM. AA. The composition of any of embodiments U-Z, wherein said buffer is at a concentration from about 10 mM and about 20 mM. BB. The composition of any of embodiments U-AA, wherein said polyol is a sugar alcohol. CC. The composition of embodiment BB, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. DD. The composition of embodiment CC, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. EE. The composition of any of embodiments CC-DD, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. FF. The composition of any of embodiments CC-EE, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. GG. The composition of any of embodiments U-FF further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. HH. The composition of embodiment GG, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. II. The composition of embodiment GG, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. JJ. The composition of embodiment GG, wherein said metal ion is selected from zinc, magnesium and calcium. KK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, mannitol at a concentration from about 1 to 10% weight by volume, and citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a surfactant. LL. A stable aqueous pharmaceutical composition comprising adalimumab, a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion, and wherein said composition has a pH of about 5 to about 6, and wherein said composition is substantially free of a polyol. MM. The composition of embodiment LL, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. NN. The composition of any of embodiments LL-MM, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. OO. The composition of any of embodiments LL-NN, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. PP. The composition of any of embodiments LL-OO, wherein said buffer is at a concentration from about 5 mM and about 50 mM. QQ. The composition of any of embodiments LL-PP, wherein said buffer is at a concentration from about 5 mM and about 20 mM. RR. The composition of any of embodiments LL-QQ, wherein said buffer is at a concentration from about 10 mM and about 20 mM. SS. The composition of embodiment LL, wherein said stabilizer is selected from the group consisting of an amino acid, a salt, EDTA and a metal ion. TT. The composition of embodiment TT, wherein said amino acid is selected from the group consisting of glycine, alanine and arginine. UU. The composition of embodiment TT, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. VV. The composition of embodiment TT, wherein said glycine is at a concentration from about 20 to about 200 mM. WW. The composition of embodiment VV, wherein said glycine is at a concentration from about 50 to about 200 mM. XX. The composition of embodiment TT, wherein said arginine is at a concentration from about 1 to about 250 mM. YY. The composition of embodiment XX, wherein said arginine is at a concentration from about 20 to about 200 mM. ZZ. The composition of embodiment YY, wherein said arginine is at a concentration from about 20 to about 100 mM. AAA. The composition of embodiment UU, wherein said sodium chloride is at a concentration from about 5 to about 150 mM. BBB. The composition of embodiment AAA, wherein said sodium chloride is at a concentration from about 20 to about 140 mM. CCC. The composition of embodiment AAA, wherein said sodium chloride is at a concentration from about 75 to about 125 mM. DDD. The composition of embodiment UU, wherein said sodium sulfate is at a concentration from about 5 to about 150 mM. EEE. The composition of embodiment UU, wherein said sodium chloride is at a concentration from about 20 to about 120 mM. FFF. The composition of embodiment EEE, wherein said sodium chloride is at a concentration from about 60 to about 100 mM. GGG. The composition of any of embodiments LL-FF further comprising a surfactant. HHH. The composition of embodiment GGG, wherein said surfactant is a polysorbate. III. The composition of embodiment HHH, wherein said polysorbate is polysorbate 80. JJJ. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, glycine at a concentration from about 20 to about 200 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. KKK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, arginine at a concentration from about 1 to about 250 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH from about 5 to about 5.5, and wherein said composition is substantially free of a polyol. LLL. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. MMM. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, sodium chloride at a concentration from about 5 to about 150 mM, polysorbate 80 at a concentration from about 1 to 50 μM, citrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of a polyol. NNN. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion, and a buffer selected from the group consisting of citrate, phosphate, succinate, tartrate and maleate, wherein said composition has a pH from about 5 to about 6. OOO. The composition of embodiment NNN, wherein the buffer does not comprise a combination of citrate and phosphate. PPP. The composition of embodiment NNN, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. QQQ. The composition of any of embodiments NNN-PPP, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. RRR. The composition of any of embodiments NNN-QQQ, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. SSS. The composition of any of embodiments NNN-RRR, wherein said buffer is at a concentration from about 5 mM and about 50 mM. TTT. The composition of any of embodiments NNN-SSS, wherein said buffer is at a concentration from about 5 mM and about 20 mM. UUU. The composition of any of embodiments NNN-TTT, wherein said buffer is at a concentration from about 10 mM and about 20 mM. VVV. The composition of any of embodiments NNN-UUU, wherein said surfactant is a polysorbate. WWW. The composition of embodiment VVV, wherein said polysorbate is polysorbate 80. XXX. The composition of any of embodiments NNN-WWW, wherein said polyol is a sugar alcohol. YYY. The composition of embodiment XXX, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. ZZZ. The composition of embodiment YYY, wherein said mannitol is at a concentration from about 1 to 10% weight by volume of the total composition. AAAA. The composition of any of embodiments YYY-ZZZ, wherein said mannitol is at a concentration from about 2 to 6% weight by volume of the total composition. BBBB. he composition of any of embodiments YYY-AAAA, wherein said mannitol is at a concentration from about 3 to 5% weight by volume of the total composition. CCCC. The composition of any of embodiments NNN-BBBB, wherein said stabilizer is EDTA. DDDD. The composition of embodiment CCCC, wherein said EDTA is at a concentration from about 0.01% to about 0.5%. EEEE. The composition of embodiment DDDD, wherein said EDTA is at a concentration from about 0.05% to about 0.25%. FFFF. The composition of embodiment EEEE, wherein said EDTA is at a concentration from about 0.08% to about 0.2%. GGGG. The composition of any of embodiments NNN-BBBB, wherein said stabilizer is methionine. HHHH. The composition of embodiment GGGG, wherein said methionine is at a concentration from about 1 to about 10 mg/ml. IIII. The composition of embodiment GGGG, wherein said methionine is at a concentration from about 1 to about 5 mg/ml. JJJJ. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol at a concentration from about 1 to 10% weight by volume, EDTA at a concentration from about 0.01% to about 0.5%, citrate at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. KKKK. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, mannitol at a concentration from about 1 to 10% weight by volume, methionine at a concentration from about 1 to about 10 mg/ml, citrate at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. LLLL. A stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, tartrate and maleate, wherein said composition has a pH of about 3.5. MMMM. The composition of embodiment LLLL, wherein said adalimumab is at a concentration from about 20 and about 150 mg/ml. NNNN. The composition of any of embodiments LLLL-MMMM, wherein said adalimumab is at a concentration from about 20 and about 100 mg/ml. OOOO. The composition of any of embodiments LLLL-NNNN, wherein said adalimumab is at a concentration from about 20 and about 40 mg/ml. PPPP. The composition of any of embodiments LLLL-OOOO, wherein said buffer is at a concentration from about 5 mM and about 50 mM. QQQQ. The composition of any of embodiments LLLL-PPPP, wherein said buffer is at a concentration from about 5 mM and about 20 mM. RRRR. The composition of any of embodiments LLLL-QQQQ, wherein said buffer is at a concentration from about 10 mM and about 20 mM. SSSS. The composition of any of embodiments LLLL-RRRR, wherein said polyol is a sugar alcohol. TTTT. The composition of embodiment SSSS, wherein said sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. UUUU. The composition of embodiment TTTT, wherein said mannitol is at a concentration from about 1 to about 10% weight by volume of the total composition. VVVV. The composition of any of embodiments TTTT-UUUU, wherein said mannitol is at a concentration from about 2 to about 6% weight by volume of the total composition. WWWW. The composition of any of embodiments TTTT-VVVV, wherein said mannitol is at a concentration from about 3 to about 5% weight by volume of the total composition. XXXX. The composition of any of embodiments LLLL-WWWW further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. YYYY. The composition of embodiment XXXX, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. ZZZZ. The composition of embodiment XXXX, wherein said salt is selected from the group consisting of sodium chloride and sodium sulfate. AAAAA. The composition of embodiment XXXX, wherein said metal ion is selected from zinc, magnesium and calcium. BBBBB. The composition of any of embodiments LLLL-AAAAA further comprising a surfactant. CCCCC. The composition of embodiment BBBBB, wherein said surfactant is a polysorbate. DDDDD. The composition of embodiment CCCCC, wherein said polysorbate is polysorbate 80. EEEEE. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM; polyol selected from sorbitol, mannitol or trehalose at a concentration from about 1 to about 10% weight by volume, and at least one amino acid stabilizer selected from the group consisting of (a) arginine at a concentration from about 1 to about 250 mg/ml and (b) glycine at a concentration of about 20 to 200 mg/ml, and histidine buffer or succinate buffer at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5. FFFFF. The composition of embodiment EEEEE wherein the polyol is sorbitol, and the composition is free or substantially free of any citrate/phosphate buffer combination, and the formulation comprises arginine or glycine, but not both. GGGGG. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 1 to about 50 μM, arginine at a concentration from about 1 to about 250 mg/ml, glycine at a concentration of about 20 to 200 mg/ml, and histidine buffer or succinate buffer at a concentration from about 5 mM and about 50 mM, and wherein said composition has a pH of about 5 to about 5.5 and said composition is free or substantially free of polyol. HHHHH. The composition of embodiment GGGGG wherein the composition is free or substantially free of any citrate/phosphate buffer combination. APPENDIX C Further Representative Embodiments Disclosed in Priority Application U.S. Ser. No. 61/769,581 A. A stable aqueous pharmaceutical composition comprising adalimumab and a single buffer. B. The composition of embodiment A, wherein said single buffer is selected from the group consisting of succinate, histidine, citrate, phosphate, tartrate and maleate. C. The composition of any of the preceding embodiments, wherein said composition has a pH of about 5 to about 6. D. The composition of any of the preceding embodiments, wherein said adalimumab contained in said pharmaceutical compositions does not lose more than 20% of its activity relative to activity of the composition at the beginning of storage. E. The composition of any of the preceding embodiments, further comprising a surfactant. F. The composition of embodiment E, wherein said surfactant is a polysorbate. G. The composition of embodiment F wherein said polysorbate is polysorbate 80. H. The composition of any of the preceding embodiments, further comprising a polyol. I. The composition of embodiment H, wherein said polyol is a sugar alcohol. J. The composition of embodiment I, wherein said sugar alcohol is sorbitol. K. The composition of any of the preceding embodiments, further comprising a sugar. L. The composition of embodiment K, wherein said sugar is selected from the group consisting of sucrose and trehalose. M. The composition of any of the preceding embodiments, wherein said adalimumab is at a concentration from about 20 to about 150 mg/ml. N. The composition of any of the preceding embodiments, wherein said buffer is at a concentration from about 5 mM to about 50 mM. O. The composition of any of embodiments A-N further comprising a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. P. The composition of embodiment O, wherein said amino acid is selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. Q. The composition of embodiment O, wherein said metal ion is selected from zinc, magnesium and calcium. R. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 0.01% w/v to 0.5% w/v by weight of the total formulation, and succinate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. S. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 0.01% w/v to 0.5% w/v by weight of the total formulation, and histidine at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. T. A stable aqueous pharmaceutical composition comprising adalimumab at a concentration from about 20 and about 150 mg/ml, polysorbate 80 at a concentration from about 0.01% w/v to 0.5% w/v by weight of the total formulation, and tartrate at a concentration from about 5 mM and about 50 mM, wherein said composition has a pH of about 5 to about 5.5, and wherein said composition is substantially free of any other buffers. U. A method of treating a mammal comprising administering to said mammal a therapeutically effective amount of the composition of any of preceding embodiments, wherein said mammal has a disease or disorder that can be beneficially treated with adalimumab. V. The method of embodiment U, wherein said disease or disorder is selected from the group consisting of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Wegener's disease (granulomatosis), Crohn's disease (or inflammatory bowel disease), chronic obstructive pulmonary disease (COPD), Hepatitis C, endometriosis, asthma, cachexia, psoriasis, and atopic dermatitis."},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE INVENTION <EOH>Tumor necrosis factor alpha (TNFα) is a naturally occurring mammalian cytokine produced by various cell types, including monocytes and macrophages in response to endotoxin or other stimuli. TNFα is a major mediator of inflammatory, immunological, and pathophysiological reactions (Grell, M., et al. (1995) Cell, 83: 793-802). Soluble TNFα is formed by the cleavage of a precursor transmembrane protein (Kriegler, et al. (1988) Cell 53: 45-53), and the secreted 17 kDa polypeptides assemble to soluble homotrimer complexes (Smith, et al. (1987), J. Biol. Chem. 262: 6951-6954; for reviews of TNF, see Butler, et al. (1986), Nature 320:584; Old (1986), Science 230: 630). These complexes then bind to receptors found on a variety of cells. Binding produces an array of pro-inflammatory effects, including (i) release of other pro-inflammatory cytokines such as interleukin (IL)-6, IL-8, and IL-1, (ii) release of matrix metalloproteinases and (iii) up-regulation of the expression of endothelial adhesion molecules, further amplifying the inflammatory and immune cascade by attracting leukocytes into extravascular tissues. There are many disorders associated with elevated levels of TNFα. For example, TNFα has been shown to be up-regulated in a number of human diseases, including chronic diseases such as rheumatoid arthritis (RA), inflammatory bowel disorders, including Crohn's disease and ulcerative colitis, sepsis, congestive heart failure, asthma bronchiale and multiple sclerosis. TNFα is also referred to as a pro-inflammatory cytokine. Physiologically, TNFα is also associated with protection from particular infections (Cerami. et al. (1988), Immunol. Today 9:28). TNFα is released by macrophages that have been activated by lipopolysaccharides of Gram-negative bacteria. As such, TNFα appears to be an endogenous mediator of central importance involved in the development and pathogenesis of endotoxic shock associated with bacterial sepsis. Adalimumab (Humira®, AbbVie, Inc.) is a recombinant human IgG1 monoclonal antibody specific for human TNF. This antibody is also known as D2E7. Adalimumab consists of 1330 amino acids and has a molecular weight of approximately 148 kilodaltons. Adalimumab has been described and claimed in U.S. Pat. No. 6,090,382, the disclosure of which is hereby incorporated by reference in its entirety. Adalimumab is usually produced by recombinant DNA technology in a mammalian cell expression system, such as, for example, Chinese Hamster Ovary cells. Adalimumab binds specifically to TNFα and neutralizes the biological function of TNF by blocking its interaction with the p55 and p75 cell surface TNF receptors. Various formulations of adalimumab are known in the art. See, for example, U.S. Pat. Nos. 8,216,583 and 8,420,081. There is still need for stable liquid formulations of adalimumab that allow its long term storage without substantial loss in efficacy."},"summary":{"kind":"string","value":"<SOH> SUMMARY OF THE INVENTION <EOH>The invention provides stable aqueous formulations comprising adalimumab that allow its long term storage. In a first embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab; a stabilizer comprising at least one member selected from the group consisting of a polyol and a surfactant; and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said buffer does not comprise a combination of citrate and phosphate, and preferably does not comprise any citrate buffer. In this embodiment, the stabilizer preferably comprises both polyol and surfactant. In a second embodiment, utilizing a single buffer system, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, a surfactant, and a buffer system comprising a single buffering agent, said single buffering agent being selected from citrate, phosphate, succinate, histidine, tartrate or maleate, but not including combinations of the foregoing; wherein the formulation has a pH of about 4 to 8, and preferably about 5 to about 6. Histidine and succinate are particularly preferred for use as single buffering agents. As used herein the term buffer, buffer system, or buffering agent, and like terminology, is intended to denoted buffer components that introduce buffer capacity in the formulation in addition to any buffering capacity offered by the protein itself, hence the term “buffer”, etc, is not intended to include the protein itself as a self buffering entity. In a third embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a stabilizer comprising at least one member selected from a polyol and a surfactant, wherein said composition has a pH of about 4 to about 8, and preferably about 5 to about 6, and wherein said composition is substantially free of a buffer. In a fourth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a polyol, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to about 8 and preferably about 5 to about 6, and wherein said composition is free or substantially free of a surfactant. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate; and (iii) the polyol is selected from the group consisting of mannitol, sorbitol and trehalose. In a fifth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, a surfactant, and a buffer selected from the group consisting of citrate, phosphate, succinate, histidine, tartrate and maleate, wherein said composition has a pH of about 4 to 8 and preferably about 5 to about 6, and wherein said composition is substantially free of polyol. Preferably, the composition (i) does not contain the buffer combination of citrate and phosphate; and (ii) the buffer is at least one member selected from the group consisting of histidine and succinate, including combinations thereof. In each of the five embodiments discussed above, the composition may optionally further comprise a stabilizer selected from the group consisting of an amino acid, a salt, ethylenediaminetetraacetic acid (EDTA) and a metal ion. The amino acid stabilizer may be selected from the group consisting of glycine, alanine, glutamate, arginine and methionine. The salt stabilizer may be selected from the group consisting of sodium chloride and sodium sulfate. The metal ion stabilizer may be selected from the group consisting of zinc, magnesium and calcium. Preferably, adalimumab formulations containing the stabilizers mentioned above also do not contain buffer systems in which phosphate buffer and citrate buffer are present in combination, and, most preferably contains buffer systems free or substantially free of citrate buffer. In particularly preferred embodiments, (i) the optional additional stabilizer present in this embodiment is not sodium chloride, or comprises sodium chloride present in amounts not to exceed about 100 mM, and comprises at least one of arginine and glycine, including combinations of the two amino acids; (ii) the buffer, when present, contains no citrate, or at least no citrate and phosphate combination, but is instead at least one of histidine and succinate, including combinations thereof; and (iii) the stabilizer when it includes a polyol is preferably mannitol in amounts exceeding about 150 mM. In further embodiments the invention is directed to an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of a buffer combination that comprises both a citrate buffer and a phosphate buffer; and (ii) the composition exhibits long term stability. Another embodiment of the invention concerns an aqueous, buffered pharmaceutical composition exhibiting long term stability, said composition comprising: (i) adalimumab; (ii) a buffer selected from the group consisting of histidine buffer, succinate buffer, and combinations thereof; (iii) a polysorbate or poloxamer surfactant, or combinations thereof; and (iv) one or both of the following: (a) a stabilizer selected from the group consisting of glycine, alanine, glutamate, arginine, methionine, EDTA, sodium chloride, sodium sulfate, metal ions, and combinations thereof; and (b) a polyol selected from sorbitol, mannitol, and trehalose, or combinations thereof. Optionally, the formulation may also include a sugar, such as sucrose. In a further embodiment the invention is an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of a polyol; and (ii) the composition exhibits long term stability. In still a further embodiment the invention is directed to an aqueous, buffered pharmaceutical composition comprising adalimumab and a buffer, wherein (i) the composition is free or substantially free of surfactant; and (ii) the composition exhibits long term stability. Another embodiment of the inventions concerns an aqueous pharmaceutical composition comprising adalimumab wherein: (i) the composition is free or substantially free of buffer; and (ii) the composition exhibits long term stability. In another embodiment, the adalimumab formulation of the present invention comprises, consists of, or consists essentially of, adalimumab, histidine buffer as the sole buffer in the formulation, glycine (or arginine, or combinations thereof) as the sole stabilizer among the non-surfactant stabilizers referenced earlier, and polysorbate 80. In this formulation, the amount of adalimumab is 20 to 150 mg/ml; the amount of histidine buffer is up to about 50 mM; the amount of glycine is up to about 300 mM; and the amount of polysorbate 80 is in the range of about 0.01 to about 0.2 wt %. Optionally, this formulation may include up to about 100 mM NaCl. The present invention also contemplates modification of this formulation to combine the histidine buffer with one or more of citrate, acetate, phosphate, maleate, tartrate buffers. In yet another embodiment, the adalimumab formulation of the present invention comprises, consists of, or consists essentially of, adalimumab, histidine buffer as the sole buffer, mannitol (or sorbitol or trehelose), and polysorbate 80, and further being free or substantially free of the non-surfactant stabilizers (e.g. glycine, arginine, etc.) referenced above. In this formulation, the amount of adalimumab is 20 to 150 mg/ml; the amount of histidine buffer is up to about 50 mM; the amount of polyol is up to about 300 mM; and the amount of polysorbate 80 is in the range of about 0.01 to about 0.2 wt %. Optionally, this formulation may include up to about 100 mM NaCl. The present invention also contemplates modification of this formulation to combine the histidine buffer with one or more of citrate, acetate, phosphate, maleate, tartrate buffers. In a method aspect, the invention is directed to a method for enhancing long term stability in an aqueous, buffered adalimumab formulation, comprising one or more of the steps of: (a) incorporating histidine buffer, succinate buffer, or a combination thereof, in the formulation based on empirical data indicating that such buffers contribute to the stability of the formulation to a greater extent than other buffers or buffer combinations; or (b) incorporating glycine, arginine or a combination thereof as stabilizers in the formulation, based upon empirical data indicating that such stabilizer contribute to the stability of the formulation to a greater extent than other stabilizers; or (c) substantially excluding the presence of buffer or buffer combinations comprising citrate buffer (especially buffer combinations comprising both citrate and phosphate) based upon empirical data indicating that such buffer or buffer combinations perform poorly in terms of stabilizing the formulation in comparison to other buffers. The method may further comprise the selection of PS 80 as a surfactant based on empirical data indicating that PS 80 imparts better thermal stability to the adalimumab formulation than other surfactants, including PS 20. The method is useful to obtain a formulation of adalimumab that exhibits long term stability comparable to or better than commercially available adalimumab formulations marketed under the trademark Humira®. In a further method aspect, the invention is directed to a method for treating an inflammatory condition in a subject which comprises administering to such subject any of the adalimumab formulation embodiments as described herein. In the foregoing embodiments, where the above referenced stabilizers may be included in the formulations, it is further discovered that satisfactory stabilization can be attained when such stabilizers are used in place of both polyol and surfactant and hence stabilized formulations of the present invention can be free or substantially free of both polyol and surfactant. Accordingly, in a sixth embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab, optionally a buffer, a stabilizer selected from the group consisting of an amino acid, a salt, EDTA, and a metal ion, and wherein said composition has a pH of about 4 to about 8, and preferably 5 to about 6, and wherein said composition is either substantially free of both polyol and surfactant. When buffer is present in this embodiment, it is especially preferred that (i) the buffer not include the combination of citrate and phosphate; (ii) the buffer is selected from the group consisting of histidine and succinate; and (iii) the stabilizer does not comprise sodium chloride, but instead is at least one member selected from the group consisting of arginine and glycine. Important aspects of the present invention in certain embodiments include (i) that sorbitol and trehalose are discovered to be significantly better stabilizers of adalimumab formulations than mannitol, unless mannitol is used at concentrations in excess of about 200-300 mM in which case the three are generally equivalent; (ii) arginine and glycine (and combinations) are discovered to be significantly better stabilizers of adalimumab formulations than sodium chloride; and; (iii) when buffers are used in the formulation, it is discovered that the combination of citrate and phosphate is surprisingly significantly poorer in stabilizing adalimumab than other buffers such as succinate, histidine, phosphate and tartrate. The relatively poor performance of the buffer combination of citrate and phosphate is rather unexpected considering the apparent importance attributed to the use of a citrate/phosphate combined buffer in U.S. Pat. No. 8,216,583. To the contrary, we have now found that a phosphate/citrate buffer combination is not an optimal choice for obtaining a stabilized adalimumab formulation, and in fact, an element of our invention is the discovery that this combination should be avoided altogether in favor of other buffer systems. Preferably, a polyol is a sugar alcohol; and even more preferably, the sugar alcohol is selected from the group consisting of mannitol, sorbitol and trehalose. However, as between mannitol and sorbitol, the invention has discovered, as noted above, a distinct stabilization advantage in using sorbitol or trehalose instead of mannitol, unless mannitol is used at concentrations in excess of about 200 mM, in which case mannitol, sorbitol and trehalose are generally equivalent. At concentrations below about 200 mM, mannitol has been found to be a poorer stabilizer than sorbitol or trehalose in an adalimumab formulation. Preferably, a surfactant is a polysorbate or poloxamer; and even more preferably PS 80, PS 40, PS20, Pluronic F-68 and combinations. We have discovered a distinct and surprising thermal stabilization advantage in selecting PS 80 instead of PS-20. These and other aspects will become apparent from the following description of the various embodiments, although variations and modifications therein may be affected without departing from the spirit and scope of the novel concepts of the disclosure. It is to be understood that both the foregoing general description and the following detailed description are exemplary and explanatory only and are not restrictive of the invention, as claimed. Further representative embodiments are set forth in the numerous formulation studies reported in the detailed description, as well as the various embodiments listed in Appendices A, B and C attached hereto and made a part hereof."},"cpc_label":{"kind":"string","value":"A61K3939591"},"filing_date":{"kind":"string","value":"20171005"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180215"},"examiner_id":{"kind":"string","value":"72243.0"},"ipc_label":{"kind":"string","value":"A61K39395"},"npe_litigated_count":{"kind":"number","value":1,"string":"1"},"examiner_full_name":{"kind":"string","value":"KIM, YUNSOO"},"invention_title":{"kind":"string","value":"Stable Aqueous Formulations of Adalimumab"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"A61K"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32898,"cells":{"application_number":{"kind":"number","value":15726899,"string":"15,726,899"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"WIRELESS PRINTING DEVICES THAT PROVIDE PRINTING SERVICES OVER A NETWORK WITHOUT A PRINTER SPECIFIC PRINTER DRIVER AFTER HAVING REGISTERED THE PRINTING DEVICE WITH A SERVICE OVER THE NETWORK"},"abstract":{"kind":"string","value":"Wireless printing devices that are configured to register with a service over a network (e.g., Internet) for providing printing services for one or more client devices without printer drivers are herein disclosed and enabled. The printing device may include a touch sensitive screen interface to receive security information for connecting to a wireless local area network (LAN). While connected to the wireless LAN, the printing device accesses the service for registering the printing device, and transmits device information related the printing device to the service. Subsequent to registration, one or more client devices using the service over the network may select the registered printing device for printing, and the printing device is configured to receive output data either from the service or via a computing device within the wireless LAN, and wherein output data is related to the device information transmitted to the service."},"claims":{"kind":"string","value":"1. A printing device that is a wireless printing device for wirelessly providing printing services to one or more client devices over a network without the need for the one or more client devices to install a device specific printer driver that is device specific to the printing device, the printing device includes: an interface for interacting with a user; wireless communication circuitry for establishing a connection to a wireless local area network; memory or storage component storing software for connecting to one or more computing devices over the network; and wherein the printing device: (1) receives, via the interface of the printing device from the user, security information for establishing the connection to a wireless local area network; (2) establishes, via the wireless communication circuitry of the printing device, the connection to a wireless local area network using, at least in part, the security information received in (1); (3) wirelessly accesses, via the wireless communication circuitry of the printing device and using the connection to a wireless local area network established in (2), the network; (4) wirelessly connects, via the wireless communication circuitry of the printing device and using the software stored in the memory or storage component of the printing device, to the one or more computing devices over the network accessed in (3); (5) wirelessly transmits, via the wireless communication circuitry, device information from the printing device to the one or more computing devices over the network connected in (4), the device information includes at least one of identification information, capability information, address information, status information, or attribute information, individually or in any combination, related to the printing device, and the transmitting of the device information is for registering the printing device; and (6) wirelessly receives, via the wireless communication circuitry of the printing device, output data from the one or more computing devices subsequent to having registered the printing device in (5), the output data is related to digital content for rendering at the printing device; and wherein the output data received in (6) is further related, at least in part, to the device information transmitted in (5) from the printing device to the one or more computing devices over the network. 2. The printing device of claim 1, wherein the wireless communication circuitry includes one or more chips or chipsets, the one or more chips or chipsets are compatible, at least in part, with at least part of a protocol within IEEE 802.11 standards for wirelessly connecting to the wireless local area network in (1). 3. The printing device of claim 2, wherein the device information transmitted from the printing device to the one or more computing devices in (5) includes identification information of the printing device, the identification information includes one or more of a name, a model, a brand, an identifier, a registration, a URL, a security key, a PIN, or an IP address, individually or in any combination, and the identification information is to facilitate identification of the printing device for service. 4. The printing device of claim 3, wherein the device information transmitted from the printing device to the one or more computing devices in (5) includes capability information related to one or more languages or formats supported by the printing device, and wherein the output data received at the printing device is in accordance, at least in part, to the one or more languages or formats supported by the printing device and specified in the device information. 5. The printing device of claim 4, wherein the printing device further includes a display screen with a touch sensitive screen interface for interacting with a user, and wherein the receiving of the security information in (1) for establishing the connection to a wireless local area network is received via the touch sensitive screen interface. 6. The printing device claim 5, wherein the network in (3) includes the Internet, and the one or more computing devices over the network being one or more servers over the Internet, and wherein the one or more servers are operated, at least in part, by a service provided over the Internet, and wherein the wireless transmitting of the device information in (5) is from the printing device to the one or more servers for registering the printing device with the service. 7. The printing device claim 5, wherein the network in (3) includes the wireless local area network, and the one or more computing devices includes an information apparatus that is in the wireless local area network, and wherein the information apparatus includes a client application for communicating with the printing device over the established wireless local area network, and wherein the client application: obtains security information or authentication information for connecting to one or more servers over the Internet, the one or more servers operated, at least in part, by a service provided over the Internet; receives, via the wireless local area network, the device information from the printing device; transmits the received device information over the Internet from the computing device to the one or more servers, the transmitting of the device information is for registering the printing device with the service or for selecting the printing device for the service. 8. The printing device of claim 5, wherein the software includes an application programming interface (API) and the printing device uses the application programming interface (API) to register the printing device with the service; and wherein the output data received from the one or more computing devices over the network includes an encryption scheme that is device specific for rendering at the printing device. 9. The printing device of claim 4, wherein the interface of the printing device is a wireless interface that wirelessly communicates with a portable wireless communication device over a local or a short range wireless communication link, and wherein the receiving of the security information for establishing the connection to a wireless area network in (1) is received using the wireless interface of the printing device and from the portable wireless communication device."},"description":{"kind":"string","value":"CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 10/053,765 filed Jan. 18, 2002, which claims priority to U.S. Provisional Patent Application Ser. No. 60/262,764, filed Jan. 19, 2001. Additionally, this application is a continuation-in-part of U.S. patent application Ser. No. 09/992,413 filed Nov. 18, 2001, which claims benefit of U.S. Provisional Patent Application Ser. No. 60/252,682 filed Nov. 20, 2000. Moreover, this application is a continuation-in-part of U.S. patent application Ser. No. 13/710,299 filed Dec. 10, 2012, which is a continuation of U.S. patent application Ser. No. 12/903,048 filed Oct. 12, 2010 and now issued as U.S. Pat. No. 8,332,521, which is a continuation of U.S. patent application Ser. No. 10/016,223 filed Nov. 1, 2001 and now issued as U.S. Pat. No. 7,941,541, and which claims benefit of U.S. Provisional Patent Application Ser. No. 60/245,101, filed Nov. 1, 2000. The complete disclosures of the above patent applications are hereby incorporated by reference for all purposes. TECHNICAL FIELD OF THE INVENTION Present invention relates to providing content to an output device and, in particular, to providing universal output in which an information apparatus can pervasively output content to an output device without the need to install a dedicated device dependent driver or applications for each output device. BACKGROUND OF THE DISCLOSURE The present invention relates to universal data output and, in particular, to providing a new data output method and a new raster image process for information apparatuses and output devices. As described herein, information apparatuses refer generally to computing devices, which include both stationary computers and mobile computing devices (pervasive devices). Examples of such information apparatuses include, without limitation, desktop computers, laptop computers, networked computers, palmtop computers (hand-held computers), personal digital assistants (PDAs), Internet enabled mobile phones, smart phones, pagers, digital capturing devices (e.g., digital cameras and video cameras), Internet appliances, e-books, information pads, and digital or web pads. Output devices may include, without limitation, fax machines, printers, copiers, image and/or video display devices (e.g., televisions, monitors and projectors), and audio output devices. For simplicity and convenience, hereafter, the following descriptions may refer to an output device as a printer and an output process as printing. However, it should be understood that the term printer and printing used in the discussion of present invention refer to one embodiment used as a specific example to simplify the description of the invention. The references to printer and printing used here are intended to be applied or extended to the larger scope and definition of output devices and should not be construed as restricting the scope and practice of present invention. Fueled by an ever-increasing bandwidth, processing power, wireless mobile devices, and wireless software applications, millions of users are or will be creating, downloading, and transmitting content and information using their pervasive or mobile computing devices. As a result, there is a need to allow users to conveniently output content and information from their pervasive computing devices to any output device. As an example, people need to directly and conveniently output from their pervasive information apparatus, without depending on synchronizing with a stationary computer (e.g., desktop personal computer) for printing. To illustrate, a mobile worker at an airport receiving e-mail in his hand-held computer may want to walk up to a nearby printer or fax machine to have his e-mail printed. In addition, the mobile worker may also want to print a copy of his to-do list, appointment book, business card, and his flight schedule from his mobile device. As another example, a user visiting an e-commerce site using his mobile device may want to print out transaction confirmation. In still another example, a user who takes a picture with a digital camera may want to easily print it out to a nearby printer. In any of the above cases, the mobile user may want to simply walk up to a printer and conveniently print a file (word processing document, PDF, HTML etc) that is stored on the mobile device or downloaded from a network (e.g., Internet, corporate network). Conventionally, an output device (e.g., a printer) is connected to an information apparatus via a wired connection such as a cable line. A wireless connection is also possible by using, for example, radio communication or infrared communication. Regardless of wired or wireless connection, a user must first install in the information apparatus an output device driver (e.g., printer driver in the case the output device is a printer) corresponding to a particular output device model and make. Using a device-dependent or specific driver, the information apparatus may process output content or digital document into a specific output device's input requirements (e.g., printer input requirements). The output device's input requirements correspond to the type of input that the output device (e.g., a printer) understands. For example, a printer's input requirement may include printer specific input format (e.g., one or more of an image, graphics or text format or language). Therefore, an output data (or print data in the case the output device is a printer) herein refers to data that is acceptable for input to an associated output device. Examples of input requirements may include, without limitation, audio format, video format, file format, data format, encoding, language (e.g., page description language, markup language etc), instructions, protocols or data that can be understood or used by a particular output device make and model. Input requirements may be based on proprietary or published standards or a combination of the two. An output device's input requirements are, therefore, in general, device dependent. Different output device models may have their own input requirements specified, designed or adopted by the output device manufacturer (e.g., the printer manufacturer) according to a specification for optimal operation. Consequently, different output devices usually require use of specific output device drivers (e.g., printer drivers) for accurate output (e.g., printing). Sometimes, instead of using a device driver (e.g., printer driver), the device driving feature may be included as part of an application software. Installation of a device driver (e.g., printer driver) or application may be accomplished by, for example, manual installation using a CD or floppy disk supplied by the printer manufacturer. Or alternatively, a user may be able to download a particular driver or application from a network. For a home or office user, this installation process may take anywhere from several minutes to several hours depending on the type of driver and user's sophistication level with computing devices and networks. Even with plug-and-play driver installation, the user is still required to execute a multi-step process for each printer or output device. This installation and configuration process adds a degree of complexity and work to end-users who may otherwise spend their time doing other productive or enjoyable work. Moreover, many unsophisticated users may be discouraged from adding new peripherals (e.g., printers, scanners, etc.) to their home computers or networks to avoid the inconvenience of installation and configuration. It is therefore desirable that an information apparatus can output to more than one output device without the inconvenience of installing multiple dedicated device dependent drivers. In addition, conventional output or printing methods may pose significantly higher challenges and difficulties for mobile device users than for home and office users. The requirement for pre-installation of a device-dependent driver diminishes the benefit and concept of mobile (pervasive) computing and output. For example, a mobile user may want to print or output e-mail, PowerPoint® presentation documents, web pages, or other documents at an airport, gas station, convenience store, kiosk, hotel, conference room, office, home, etc. It is highly unlikely that the user would find at any of these locations a printer of the same make and model as is at the user's base station. As a consequence, under the conventional printing method, the user would have to install and configure a printer driver each time at each such remote location before printing. It is usually not a viable option given the hundreds, or even thousands of printer models in use, and the limited storage, memory space, and processing power of the information apparatus. Moreover, the user may not want to be bothered with looking for a driver or downloading it and installing it just to print out or display one page of email at the airport. This is certainly an undesirable and discouraging process to promote pervasive or mobile computing. Therefore, a more convenient printing method is needed in support of the pervasive computing paradigm where a user can simply walk up to an output device (e.g., printer or display device) and easily output a digital document without having to install or pre-install a particular output device driver (e.g., printer driver). Another challenge for mobile users is that many mobile information apparatuses have limited memory space, processing capacity and power. These limitations are more apparent for small and low-cost mobile devices including, for example, PDAs, mobile phones, screen phones, pagers, e-books, Internet Pads, Internet appliances etc. Limited memory space poses difficulties in installing and running large or complex printer or device drivers, not to mention multiple drivers for a variety of printers and output devices. Slow processing speed and limited power supply create difficulties driving an output device. For example, processing or converting a digital document into output data by a small mobile information apparatus may be so slow that it is not suitable for productive output. Intensive processing may also drain or consume power or battery resources. Therefore, a method is needed so that a small mobile device, with limited processing capabilities, can still reasonably output content to various output devices. To output or render content (e.g. digital document) to an output device, a raster image processing (RIP) operation on the content is usually required. RIP operation can be computationally intensive and may include (1) a rasterization operation, (2) a color space conversion, and (3) a halftoning operation. RIP may also include other operations such as scaling, segmentation, color matching, color correction, GCR (Grey component replacement), Black generation, image enhancement compression/decompression, encoding/decoding, encryption/decryption GCR, image enhancement among others. Rasterization operation in RIP involves converting objects and descriptions (e.g. graphics, text etc) included in the content into an image form suitable for output. Rasterization may include additional operations such as scaling and interpolation operations for matching a specific output size and resolution. Color space conversion in RIP includes converting an input color space description into a suitable color space required for rendering at an output device (e.g. RGB to CMYK conversion). Digital halftoning is an imaging technique for rendering continuous tone images using fewer luminance and chrominance levels. Halftoning operations such as error diffusion can be computationally intensive and are included when the output device's bit depth (e.g. bits per pixel) is smaller than the input raster image bit depth. Conventionally, RIP operations are included either in an information apparatus, or as part of an output device or output system (e.g. in a printer controller). FIG. 1A illustrates a flow diagram of a conventional data output method 102 in which RIP 110 is implemented in the information apparatus. Output devices that do not include a printer controller to perform complex RIP operations, such as a lower-cost, lower speed inkjet printer, normally employ data output method 102. In data output method 102, an information apparatus obtains content (e.g. a digital document) in step 100 for rendering or output at an output device. The information apparatus may includes an application (e.g. device driver), which implements RIP operation 110. The information apparatus generates an output data in step 120 and transmits the output data to the output device in step 130 for rendering. The output data relating to the content is in an acceptable form (e.g. in an appropriate output size and resolution) to the output engine (e.g. display engine, printer engine etc.) included in the output device. The output data in a conventional output method 102 is usually device dependent. One drawback for the data output method 102 of FIG. 1A is that the information apparatus performs most if not the entire raster image processing operations 110 required for output. The RIP operations may require intensive computation. Many information apparatus such as mobile information device might have insufficient computing power and/or memory to carry out at an acceptable speed the RIP operations 110 required in an output process. Another drawback for the conventional data output method 102 of FIG. 1A is that the generated output data is device dependent and therefore is typically not very portable to other output devices. As a result, the information apparatus may need to install multiple applications or device drivers for multiple output devices, which may further complicate its feasibility for use in information apparatuses with limited memory, storage and processing power. FIG. 1B illustrates a flow diagram of another conventional data output method 104 in which the RIP is implemented in an output device. An example of an output device that implements process 104 is a high-speed laser printer which includes a printer controller for performing RIP operations and an output engine (e.g. printer engine) for rendering content. Printer controller may be internally installed or externally connected to an output device (printer in this example). In data output method 104, an information apparatus obtains content for output in step 100 and generates in step 160 an output data or print data for transmitting to the output device in step 170. Print data includes information related to the content and is usually encoded in a page description language (PDL) such as PostScript and PCL etc. In step 180, the printer receives the output data or print data (in a PDL). In step 190, a printer controller included in the printer interprets the PDL, performs RIP operations, and generates a printer-engine print data that is in a form acceptable to the printer engine (e.g. a raster image in an appropriate output size, bit depth, color space and resolution). In step 150 the printer engine renders the content with the printer-engine print data. It will be understood that a reference to print data or output data including a language, such as PDL, should be interpreted as meaning that the print data or output data is encoded using that language. Correspondingly, a reference to a data output process generating a language, such as PDL, should be interpreted as meaning that the data output process encodes data using that language. There are many drawbacks in the conventional data output method 104 shown in FIG. 1B. These drawbacks are especially apparent for mobile computing devices with limited processing power and memory. One such drawback is that the output data or print data, which include a page description language (PDL) such as PostScript or PCL, can be very complex. Generating complex PDL may increase memory and processing requirements for an information apparatus. Furthermore, interpreting, decoding and then raster image processing complex PDL can increase computation, decrease printing speed, and increase the cost of the output device or its printer controller. Another drawback is that the output data that includes PDL can creates a very large file size that would increase memory and storage requirements for the information apparatus, the output device and/or the printer controller etc. Large file size may also increase the bandwidth required in the communication link between the information apparatus and the output device. Finally, to rasterize text in an output device, a printer controller may need to include multiple fonts. When a special font or international characters is not included or missing in the printer controller, the rendering or output can potentially become inaccurate or inconsistent. SUMMARY OF THE INVENTION Accordingly, this invention provides a convenient universal data output method in which an information apparatus and an output device or system share the raster image processing operations. Moreover, the new data output method eliminates the need to install a plurality of device-dependent dedicated drivers or applications in the information apparatus in order to output to a plurality of output devices. In accordance with present invention, an electronic system and method of pervasive and universal output allow an information apparatus to output content conveniently to virtually any output device. The information apparatus may be equipped with a central processing unit, input/output control unit, storage unit, memory unit, and wired or wireless communication unit or adapters. The information apparatus preferably includes a client application that may be implemented as a software application, a helper application, or a device driver (a printer driver in case of a printer). The client application may include management and control capabilities with hardware and software components including, for example, one or more communication chipsets residing in its host information apparatus. The client application in the information apparatus may be capable of communicating with, managing and synchronizing data or software components with an output device equipped with an output controller of present invention. Rendering content in an output device refers to printing an image of the content onto an substrate in the case of a printing device; displaying an image of the content in the case of a displaying device; playing an audio representation of the content in a voice or sound output device or system. An output controller may be a circuit board, card or software components residing in an output device. Alternatively, the output controller may be connected externally to an output device as an external component or “box.” The output controller may be implemented with one or more combinations of embedded processor, software, firmware, ASIC, DSP, FPGA, system on a chip, special chipsets, among others. In another embodiment, the functionality of the output controller may be provided by application software running on a PC, workstation or server connected externally to an output device. In conventional data output method 102 as described with reference to FIG. 1A, an information apparatus transmits output data to an output device for rendering. Output data corresponds to content intended for output and is mostly raster image processed (RIPed) and therefore is device dependent because raster image processing is a typical device dependent operation. Output data may be encoded or compressed with one or more compression or encoding techniques. In present invention, an information apparatus generates an intermediate output data for transmitting to an output device. The intermediate output data includes a rasterized image corresponding to the content; however, device dependent image processing operations of a RIP (e.g. color matching and halftoning) have not been performed. As a result, an intermediate output data is more device independent and is more portable than the output data generated by output method with reference to FIG. 1A. In one implementation of this invention, the intermediate output data includes MRC (Mixed raster content) format, encoding and compression techniques, which further provides improved image quality and compression ratio compared to conventional image encoding and compression techniques. In an example of raster image process and data output method of the present invention, a client application such as a printer driver is included in an information apparatus and performs part of raster image processing operation such as rasterization on the content. The information apparatus generates an intermediate output data that includes an output image corresponding to the content and sends the intermediate output data to an output device or an output system for rendering. An output controller application or component included in the output device or output system implements the remaining part of the raster image processing operations such as digital halftoning, color correction among others. Unlike conventional raster image processing methods, this invention provides a more balanced distribution of the raster image processing computational load between the Information apparatus and the output device or the output system. Computational intensive image processing operations such as digital halftoning and color space conversions can be implemented in the output device or output system. Consequently, this new raster image processing method reduces the processing and memory requirements for the information apparatus when compared to conventional data output methods described with reference to FIG. 1A in which the entire raster image process is implemented in the information apparatus. Additionally, in this invention, a client application or device driver included in the information apparatus, which performs part of the raster image processing operation, can have a smaller size compared to a conventional output application included in the information apparatus, which performs raster image processing operation. In another implementation, the present invention provides an information apparatus with output capability that is more universally accepted by a plurality of output devices. The information apparatus, which includes a client application, generates an intermediate output data that may include device independent attributes. An output controller includes components to interpret and process the intermediate output data. The information apparatus can output content to different output devices or output systems that include the output controller even when those output devices are of different brand, make, model and with different output engine and input data requirements. Unlike conventional output methods, a user does not need to preinstall in the information apparatus multiple dedicated device dependent drivers or applications for each output device. The combination of a smaller-sized client application, a reduced computational requirement in the information apparatus, and a more universal data output method acceptable for rendering at a plurality of output devices enable mobile devices with less memory space and processing capabilities to implement data output functions which otherwise would be difficulty to implement with conventional output methods. In addition, this invention can reduce the cost of an output device or an output system compared to conventional output methods 104 that include a page description language (PDL) printer controller. In the present invention, an information apparatus generates and sends an intermediate output data to an output device or system. The intermediate output data in one preferred embodiment includes a rasterized output image corresponding to the content intended for output. An output controller included in an output device or an output system decodes and processes the intermediate output data for output, without performing complex interpretation and rasterization compared to conventional methods described in process 104. In comparison, the conventional data output process 104 generates complex PDL and sends this PDL from an information apparatus to an output device that includes a printer controller (e.g. a PostScript controller or a PCL5 controller among others). Interpretation and raster image processing of a PDL have much higher computational requirements compared to decoding and processing the intermediate output data of this invention that include rasterized output image or images. Implementing a conventional printer controller with, for example, PDL increases component cost (e.g. memories, storages, ICs, software and processors etc.) when compared to using the output controller included in the data output method of this present invention. Furthermore, an output data that includes PDL can create a large file size compared to an intermediate output data that includes rasterized output image. The data output method for this invention comparatively transmits a smaller output data from an information apparatus to an output device. Smaller output data size can speed up transmission, lower communication bandwidth, and reduce memory requirements. Finally, this invention can provide a convenient method to render content at an output device with or without connection to a static network. In conventional network printing, both information apparatus and output device must be connected to a static network. In this invention, through local communication and synchronization between an information apparatus and an output device, installation of hardware and software to maintain static network connectivity may not be necessary to enable the rendering of content to an output device. According to the several aspects of the present invention there is provided the subject matter defined in the appended independent claims. Additional objects and advantages of the present invention will be apparent from the detailed description of the preferred embodiment thereof, which proceeds with reference to the accompanying drawings. BRIEF DESCRIPTION OF THE DRAWINGS FIG. 1A is a flow diagram of a conventional data output method and its corresponding raster image process in accordance with prior art. FIG. 1B is a flow diagram of a second conventional data output method and its corresponding raster image process for an output device that includes a conventional printer controller in accordance with prior art. FIGS. 2A and 2B are block diagrams illustrating components of an operating environment that can implement the process and apparatus of the present invention. FIG. 3A is a schematic block diagram illustrating hardware/software components of an information apparatus implementation in accordance with the present invention. The information apparatus includes an operating system. FIG. 3B is a second schematic block diagram illustrating hardware/software components of an information apparatus implementation in accordance with the present invention. FIG. 4A is a block diagram of a conventional printing system or printer with a conventional printer controller. FIG. 4B is a block diagram of a second conventional output system or output device. FIG. 5A is a schematic block diagram of a printing system or printer with a conventional printer controller and an output controller in accordance with present invention. FIG. 5B is a schematic block diagram of a second output system or output device that includes an output controller in accordance with present invention. FIG. 6A is a schematic block diagram illustrating hardware/software components of an output controller in accordance with present invention. The output controller includes an operating system. FIG. 6B is a second schematic block diagram illustrating hardware/software components of an output controller in accordance with present invention. The output controller does not include an operating system. FIG. 6C is a third schematic block diagram illustrating hardware/software components of an output controller in accordance with present invention. The output controller combines the functionality of a printer controller and an output controller of present invention. FIGS. 7A-7F illustrate various configurations and implementations of output controller with respect to an output device such as a printer. FIG. 8A is a block diagram illustrating an exemplary implementation of hardware/software components of wireless communication unit. FIG. 8B is block diagram illustrating a second exemplary implementation of hardware/software components of wireless communication unit. FIG. 9 is a flow diagram of a universal data output method and its corresponding raster imaging process of the present invention. FIG. 10 is a block diagram of a universal data output method of the present invention with respect to the components, system and apparatus described with reference to FIG. 2. FIG. 11 is a flow diagram illustrating one way of implementing a discovery process optionally included in the output process of FIG. 10. FIGS. 12A and 12B are flow diagrams of exemplary client application process included in the output process of FIG. 10. FIGS. 13A and 13B are flow diagrams of exemplary output device or output system process included in the output process of FIG. 10. DETAILED DESCRIPTION OF PREFERRED EMBODIMENTS Sets forth below are definitions of terms that are used in describing implementations of the present invention. These definitions are provided to facilitate understanding and illustration of implementations of the present invention and should in no way be construed as limiting the scope of the invention to a particular example, class, or category. Output Device Profile (or Object) An output device profile (or object) includes software and data entity, which encapsulates within itself both data and attributes describing an output device and instructions for operating that data and attributes. An output device profile may reside in different hardware environments or platforms or applications, and may be transported in the form of a file, a message, a software object or component among other forms and techniques. For simplicity of discussion, a profile or object may also include, for example, the concept of software components that may have varying granularity and can consist of one class, a composite of classes, or an entire application. The term profile or object used herein is not limited to software or data as its media. Any entity containing information, descriptions, attributes, data, instructions etc. in any computer-readable form or medium such as hardware, software, files based on or including voice, text, graphics, image, or video information, etc., are all valid forms of profile and object definition. A profile or object may also contain in one of its fields or attributes a reference or pointer to another profile or object, or a reference or pointer to data and or content. A reference to a profile or object may include one or more, or a combination of pointers, identifiers, names, paths, addresses or any descriptions relating to a location where an object, profile, data, or content can be found. An output device profile may contain one or more attributes that may identify and describe, for example, the capabilities and functionalities of a particular output device such as a printer. An output device profile may be stored in the memory component of an output device, an information apparatus or in a network node. A network node includes any device, server or storage location that is connected to the network. As described below in greater detail, an information apparatus requesting output service may communicate with an output device. During such local service negotiation, at least a partial output device profile may be uploaded to the information apparatus from the output device. By obtaining the output device profile (or printer profile in the case of a printer), the information apparatus may learn about the capability, compatibility, identification, and service provided by the output device. As an example, an output device profile may contain one or more of the following fields and or attribute descriptions. Each of following fields may be optional, and furthermore, each of the following fields or attributes may or may not exist in a particular implementation (e.g., may be empty or NULL): Identification of an output device (e.g., brand, model, registration, IP address etc.) Services and feature sets provided by an output device (e.g., color or grayscale output, laser or inkjet, duplex, output quality, price per page, quality of service, etc.) Type of input languages, formats, output data and/or input requirements (e.g., PostScript, PCL, XML, RTL, etc.) supported by an output device. Device specific or dependent parameters and information (e.g., communication protocols, color space, color management methods and rendering intents, resolution, halftoning methods, dpi (dots-per-inch), bit depth, page size, printing speed, number of independent colors channels or ink etc.) Data and tables needed for image processing such as color table, halftone table, scale factor, encoding/decoding parameters and methods, compression and decompression parameters and method etc. Another profile which contain parameters and information about the output device and its service (e.g. color profiles, halftoning profiles, communication profiles, rasterization profiles, quality of service etc.). Payment information on a plurality of services provided by an output device. Information or security requirements and type of authentication an output device supports. Date and version of the output device profile, history of its modification and updates. Software components containing algorithms or instructions or data, which may be uploaded to run in an information apparatus. For example, a graphical user interface (GUI) software component may be uploaded to an information apparatus. The software component may be incorporated into or launched in the information apparatus by a client application of present invention to capture a user's preferences (e.g., print quality, page layout, number of copies, number of cards per page, etc.). In another example, software components may include methods, instructions or executables for compression/decompression, encoding/decoding, color matching or correction, segmentation, scaling, halftoning, encryption/decryption among others. Pointer or reference to one or more output device parameters, including one or more of the above described output device profile or object fields and or attribute descriptions. For example, a more up-to-date or original version of output device parameters may sometimes be stored in a network node (any device, server or storage location that is connected to the network), or within the information apparatus where it can be obtained by the client application. An output device profile may include pointer or pointers to these output device parameters. Content (or Data Content, Digital Content, Output Content) Content (or data content, digital content, output content) is the data intended for output, which may include texts, graphics, images, forms, videos, audio among other content types. Content may include the data itself or a reference to that data. Content may be in any format, language, encoding or combination, and it can be in a format, language or encoding that is partially or totally proprietary. A digital document is an example of content that may include attributes and fields that describe the digital document itself and or reference or references to the digital document or documents. Examples of a digital document may be any one or combination of file types: HTML, VHTML, PostScript, PCL, XML, PDF, MS Word, PowerPoint, JPEG, MPEG, GIF, PNG, WML, VWML, CHTML, HDML, ASCII, 2-byte international coded characters, etc. Content may be used interchangeably with the term data content, output content or digital content in the descriptions of present invention. Intermediate Output Data Output data (or print data in case of a printer) is the electronic data sent from an information apparatus to an output device. Output data is related to the content intended for output and may be encoded in a variety of formats and languages (e.g. postscript, PCL, XML), which may include compressed or encrypted data. Some output device manufacturers may also include in the output data (or print data) a combination of proprietary or non-proprietary languages, formats, encoding, compression, encryption etc. Intermediate output data is the output data of the present invention, and it includes the broader definition of an output file or data generated by an information apparatus, or a client application or device driver included in the information apparatus. An intermediate output data may contain text, vector graphics, images, video, audio, symbols, forms or combination and can be encoded with one or more of a page description language, a markup language, a graphics format, an imaging format, a metafile among others. An intermediate output data may also contain instructions (e.g. output preferences) and descriptions (e.g. data layout) among others. Part or all of an intermediate output data may be compressed, encrypted or tagged. In a preferred embodiment of this invention, intermediate output data contains rasterized image data. For example, vector graphics and text information or objects that are not in image form included in content can be rasterized or conformed into image data in an information apparatus and included in an intermediate output data. Device dependent image processing operations of a RIP such as digital halftoning and color space conversions can be implemented at an output device or an output system. The intermediate output data can be device dependent or device independent. In one implementation, the rasterized output image is device dependent if the rasterization parameters used, such as resolution, scale factor, bit depth, output size and or color space are device dependent. In another implementation of this invention, the rasterized image may be device independent if the rasterization parameters used are device independent. Rasterization parameter can become device independent when those parameters include a set of predetermined or predefined rasterization parameters based on a standard or a specification. With predefined or device independent rasterization parameters, a client application of present invention can rasterize at least a portion of the content and generate a device independent image or images included in the intermediate output data. By doing so, the intermediate output data may become device independent and therefore, become universally acceptable with output devices that have been pre-configured to accept the intermediate output data. One advantage of rasterizing or converting text and graphics information into image data at the information apparatus is that the output device or printer controller no longer needs to perform complex rasterization operation nor do they need to include multiple fonts. Therefore, employing the intermediate output data and the data output method described herein could potentially reduce the cost and complexity of an output controller, printer controller and or output device. One form of image data encoding is known as mixed raster content, or MRC. Typically, an image stored in MRC includes more than one image or bitmap layers. In MRC, an image can be segmented in different layers based on segmentation criteria such as background and foreground, luminance and chrominance among others. For example, an MRC may include three layers with a background layer, a foreground layer and a toggle or selector layer. The three layers are coextensive and may include different resolution, encoding and compression. The foreground and background layers may each contain additional layers, depending on the manner in which the respective part of the image is segmented based on the segmentation criteria, component or channels of a color model, image encoding representation (HLS, RGB, CMYK, YCC, LAB etc) among others. The toggle layer may designate, for each point, whether the foreground or background layer is effective. Each layer in a MRC can have different bit depths, resolution, color space, which allow, for example, the foreground layer to be compressed differently from the background layer. The MRC form of image data has previously been used to minimize storage requirements. Further, an MRC format has been proposed for use in color image fax transmission. In one embodiment of present invention, the intermediate output data includes one or more rasterized output images that employ MRC format, encoding and or related compression method. In this implementation, different layers in the output image can have different resolutions and may include different compression techniques. Different information such as chrominance and luminance and or foreground and background information in the original content (e.g. digital document) can be segmented and compressed with different compression or encoding techniques. Segmented elements or object information in the original content can also be stored in different image layers and with different resolution. Therefore, with MRC, there is opportunity to reduce output data file size, retain greater image information, increase compression ratio, and improve image quality when compared to other conventional image encoding and compression techniques. Implementations of rasterization, raster image processing and intermediate output data that include MRC encoding in the present invention are described in more detail below. Rasterization Rasterization is an operation by which graphics and text in a digital document are converted to image data. For image data included in the digital document, rasterization may include scaling and interpolation. The rasterization operation is characterized by rasterization parameters including, among others bit depth and resolution. A given rasterization operation may be characterized by several more rasterization parameters, including output size, color space, color channels etc. Values of one or more of the rasterization parameters employed in a rasterization operation may be specified by default; values of one or more of the rasterization parameters may be supplied to the information apparatus as components of a rasterization vector. In a given application, the rasterization vector may specify a value of only one rasterization parameter, default values being employed for other rasterization parameters used in the rasterization operation. In another application the rasterization vector may specify values of more than one, but less than all, rasterization parameters, default values being employed for at least one other rasterization parameter used in the rasterization operation. And in yet another application the rasterization vector may specify values of all the rasterization parameters used in the rasterization operation. FIGS. 2A and 2B are block diagrams illustrating components of an operating environment that can implement the process and apparatus of present invention. FIG. 2A shows an electronic system which includes an information apparatus 200 and an output device 220. The output device 220 includes an output controller 230. FIG. 2B illustrates a second implementation of an electronic system that includes an information apparatus 200 and an output system 250. The output system 250 includes an output device 220 and an output controller 230 which may be externally connected to, or otherwise associated with, the output device 220 in the output system 250. Information apparatus 200 is a computing device with processing capability. In one embodiment, information apparatus 200 may be a mobile computing device such as palmtop computer, handheld device, laptop computer, personal digital assistant (PDA), smart phone, screen phone, e-book, Internet pad, communication pad, Internet appliance, pager, digital camera, etc. It is possible that information apparatus 200 may also include a static computing device such as a desktop computer, workstation, server, etc. FIGS. 3A and 3B are block diagrams illustrating examples of hardware/software components included in an information apparatus 200 of present invention. Information apparatus 200 may contain components such as a processing unit 380, a memory unit 370, an optional storage unit 360 and an input/output control unit (e.g. communication manager 330). Information apparatus 200 may include an interface (not shown) for interaction with users. The interface may be implemented with software or hardware or a combination. Examples of such interfaces include, without limitation, one or more of a mouse, a keyboard, a touch-sensitive or non-touch-sensitive screen, push buttons, soft keys, a stylus, a speaker, a microphone, etc. Information apparatus 200 typically contains one or more network communication unit 350 that interfaces with other electronic devices such as network node (not shown), output device 220, and output system 230. The network communication unit may be implemented with hardware (e.g., silicon chipsets, antenna), software (e.g., protocol stacks, applications) or a combination. In one embodiment of the present invention, communication interface 240 between information apparatus 200 and output device 220 or output system 250 is a wireless communication interface such as a short-range radio interface including those implemented according to the Bluetooth or IEEE 802.11 standard. The communication interface may also be realized by other standards and/or means of wireless communication that may include radio, infrared, cellular, ultrasonic, hydrophonic among others for accessing one or more network node and/or devices. Wired line connections such as serial or parallel interface, USB interface and fire wire (IEEE 1394) interface, among others, may also be included. Connection to a local network such as an Ethernet or a token Ring network, among others, may also be implemented in the present invention for local communication between information apparatus 200 and output device 220. Examples of hardware/software components of communication units 350 that may be used to implement wireless interface between the information apparatus 200 and the output device 220 are described in more detail with reference to FIGS. 8A and 8B below. For simplicity, FIG. 3 illustrates one implementation where an information apparatus 200 includes one communication unit 350. However, it should be noted that an information apparatus 200 may contain more than one communication unit 350 in order to support different interfaces, protocols, and/or communication standards with different devices and/or network nodes. For example, information apparatus 200 may communicate with one output device 220 through a Bluetooth standard interface or through an IEEE 802.11 standard interface while communicating with another output device 220 through a parallel cable interface. The information apparatus 200 may also be coupled to a wired or wireless network (e.g. the Internet or corporate network) to send, receive and/or download information. Information apparatus 200 may be a dedicated device (e.g., email terminal, web terminal, digital camera, e-book, web pads, Internet appliances etc.) with functionalities that are pre-configured by manufacturers. Alternatively, information apparatus 200 may allow users to install additional hardware components and or application software 205 to expand its functionality. Information apparatus 200 may contain a plurality of applications 205 to implement its feature sets and functionalities. As an example, a document browsing or editing application may be implemented to help user view and perhaps edit, partially or entirely, digital documents written in certain format or language (e.g., page description language, markup language, etc.). Digital documents may be stored locally in the information apparatus 200 or in a network node (e.g., in content server). An example of a document browsing application is an Internet browser such as Internet Explorer, Netscape Navigator, or a WAP browser. Such browsers may retrieve and display content (e.g. digital content) written in mark-up languages such as HTML, WML, XML, CHTML, HDML, among others. Other examples of software applications in the information apparatus 200 may include a document editing software such as Microsoft Word™ which also allows users to view and or edit digital documents that have various file extensions (e.g., doc, rtf, html, XML etc.) whether stored locally in the information apparatus 200 or in a network node. Still, other example of software applications 205 may include image acquisition and editing software. As illustrated previously with reference to FIG. 1, there are many difficulties in providing output capability to an information apparatus 200 that has limited memory and processing capability. To address theses difficulties, information apparatus 200 includes a client application 210 that helps provide the universal data output capability of the present invention. Client application 210 may include software and data that can be executed by the processing unit 380 of information apparatus 200. Client application 210 may be implemented as a stand-alone software application or as a part of or feature of another software application, or in the form of a device driver, which may be invoked, shared and used by other application software 205 in the information apparatus 200. Client application 210 may also include components to invoke other applications 205 (e.g., a document browsing application, editing application, data and/or image acquisition application, a communication manager, a output manager etc.) to provide certain feature sets, as described below. FIG. 3 illustrates a configuration where the client application 210 is a separate application from the other application 205 such as the case when the client application is a device driver; however, it should be noted that the client application 210 can be combined or being part of the other application not shown in FIG. 3. Client application 210 may be variously implemented in an information apparatus 200 and may run on different operating systems or platforms. The client application 210 may also run in an environment with no operating system. For example, FIG. 3A illustrates an implementation where the information apparatus 200A includes an operating system 340A; while FIG. 3B illustrates an implementation where the information apparatus 200B does not include an operating system. Client application 210 includes a rasterization component 310 to conform content into one or more raster output images according to one or more rasterization parameters; an intermediate output data generator component 320 that generates and/or encodes intermediate output data that includes the one or more output images; and a communications manager 330 that manages the communication and interaction with an output device 220 or system 250 or output controller 230. Communications manager can be implemented as part of the client application 210 (shown in FIG. 3) or as a separate application (not shown). Components in a client application can be implemented in software, hardware or combination. As an example, client application 210 may include or utilize one or more of the following: Components or operations to obtain content (e.g. digital document) for output. The client application 210 may obtain a digital document from other applications 205 (e.g. document browsing application, content creation and editing application, etc.), or the client application 210 may provide its own capability for user to browse, edit and or select a digital document. Components or operations to rasterize content that includes text, graphics and images among others objects or elements into one or more raster images according to a set of rasterization parameters such as scale factor, output size, bit depth, color space and resolution. The rasterization parameters may be obtained in various ways, for example, from an output device profile uploaded from an output device 220, or stored locally in information apparatus 200, or manually inputted by a user. Alternatively, rasterization parameters may be based on a predefined standard or specification stored in the information apparatus 200 as a set of defaults, or hard-coded in the client application 210, or calculated by the client application 210 after communicating with an output device 220, output controller 230, and/or a user. Components or operations to generate intermediate output data that includes at least one rasterized output image corresponding to the content (e.g. digital document). This process may further include one or combination of compression, encoding, encryption and color correction among others. The intermediate output data may include, for example, images, instructions, documents and or format descriptions, color profiles among others. Components or operations to transmit the intermediate output data to an output device 220 or system 250 through wired or wireless communication link 240. The client application 210 may also optionally include or utilize one or more of the following components or operations: Components or operations to communicate with one or more output devices 220 to upload an output device profile. Components or operations to communicate directly or indirectly (such as through an operating system or component or object model, messages, file transfer etc.) with other applications 205 residing in the same information apparatus 200 to obtain objects, data, and or content needed, or related to the pervasive output process of present invention (e.g. obtain a digital document for printing). Components or operations to manage and utilize directly or indirectly functionalities provided by hardware components (e.g. communication unit 350) residing in its host information apparatus 200. Components or operations to provide a graphical user interface (GUI) in host information apparatus to interact with user. Components or operations to obtain user preferences. For example, a user may directly input his or her preferences through a GUI. A set of default values may also be employed. Default values may be pre-set or may be obtained by information apparatus 200 as result of communicating and negotiating with an output device 220 or output controller 230. The above functionalities and process of client application 210 of present invention are described in further detail in the client application process with reference to FIG. 12. Output device 220 is an electronic system capable of outputting digital content regardless of whether the output medium is substrate (e.g., paper), display, projection, or sound. A typical example of output device 220 is a printer, which outputs digital documents containing text, graphics, image or any combination onto a substrate. Output device 220 may also be a display device capable of displaying still images or video, such as, without limitation, televisions, monitors, and projectors. Output device 220 can also be a device capable of outputting sound. Any device capable of playing or reading digital content in audio (e.g., music) or data (e.g., text or document) formats is also a possible output device 220. A printer is frequently referred to herein as an example of an output device to simplify discussion or as the primary output device 220 in a particular implementation. However, it should be recognized that present invention applies also to other output devices 220 such as fax machines, digital copiers, display screens, monitors, televisions, projectors, voice output devices, among others. Rendering content with an output device 220 refers to outputting the content on a specific output medium (e.g., papers, display screens etc). For example, rendering content with a printer generates an image on a substrate; rendering content with a display device generates an image on a screen; and rendering content with an audio output device generates sound. A conventional printing system in general includes a raster image processor and a printer engine. A printer engine includes memory buffer, marking engine among other components. The raster image processor converts content into an image form suitable for printing; the memory buffer holds the rasterized image ready for printing; and the marking engine transfers colorant to substrate (e.g., paper). The raster image processor may be located within an output device (e.g. included in a printer controller 410) or externally implemented (in an information apparatus 200, external controller, servers etc). Raster image processor can be implemented as hardware, software, or a combination (not shown). As an example, raster image processor may be implemented in a software application or device driver in the information apparatus 200. Examples of raster image processing operations include image and graphics interpretation, rasterization, scaling, segmentation, color space transformation, image enhancement, color correction, halftoning, compression etc. FIG. 4A illustrates a block diagram of one conventional printing system or printer 400A that includes a printer controller 410 and a printer engine 420A. The printer controller 410 includes an interpreter 402 and a raster image processor 406, and the printer engine 420 includes memory buffer 424A and a marking engine 426A. Marking engine may use any of a variety of different technologies to transfer a rasterized image to paper or other media or, in other words, to transfer colorant to a substrate. The different marking or printing technologies that may be used include both impact and non-impact printing. Examples of impact printing may include dot matrix, teletype, daisywheel, etc. Non-impact printing technologies may include inkjet, laser, electrostatic, thermal, dye sublimation, etc. The marking engine 426 and memory buffer 424 of a printer form its printer engine 420, which may also include additional circuitry and components, such as firmware, software or chips or chipsets for decoding and signal conversion, etc. Input to a printer engine 420 is usually a final rasterized printer-engine print data generated by a raster image processor 406. Such input is usually device dependent and printer or printer engine specific. The printer engine 420 may take this device dependent input and generate or render output pages (e.g. with ink on a substrate). When a raster image processor is located inside an output device 220, it is usually included in a printer controller 410 (as shown in FIG. 4A). A printer controller 410 may interpret, rasterize, and convert input print data in the form of a page description language (e.g., PostScript, PCL), markup language (e.g., XML, HTML) or other special document format or language (e.g. PDF, EMF) into printer-engine print data which is a final format, language or instruction that printer engine 420A can understand. Print data sent to a printer with printer controller 410 is usually in a form (e.g. postscript) that requires further interpretation, processing or conversion. A printer controller 410 receives the print data, interprets, process, and converts the print data into a form that can be understood by the printer engine 420A. Regardless of the type of print data, conventionally, a user may need a device-specific driver in his or her information apparatus 200 in order to output the proper language, format, or file that can be accepted by a specific printer or output device 220. FIG. 4B illustrates another conventional output device 400B. Output device 400B may be a printing device, a display device, a projection device, or a sound device. In the case that the output device is a printing device or a printer, the printer with reference to FIG. 4B does not include a printer controller 410. As an example, printer 400B may be a low-cost printer such as a desktop inkjet printer. RIP operations in this example may be implemented in a software application or in a device driver included in an information apparatus 200. The information apparatus 200 generates device dependent output data (or print data in case of a printer) by rasterizing and converting a digital document into output data (e.g. into a compressed CMKY data with one or more bits per pixel) that can be understood by an output engine (or printer engine in case of a printer) 420B. Regardless of type or sophistication level, different output device 220 conventionally needs different printer drivers or output management applications in an information apparatus 200 to provide output capability. Some mobile devices with limited memory and processing power may have difficulty storing multiple device drivers or perform computational intensive RIP operations. It may also be infeasible to install a new device dependent or specific printer driver each time there is a need to print to a new printer. To overcome these difficulties, present invention provides several improvements to output device 220 or output system 250 as described in detail next. In present invention, output device 220 may include an output controller 230 to help managing communication and negotiation processes with an information apparatus 200 and to process output data. Output controller 230 may include dedicated hardware or software or combination of both for at least one output device 220. Output controller 230 may be internally installed, or externally connected to one or more output devices 220. The output controller 230 is sometimes referred to as a print server or output server. FIGS. 5A and 5B illustrate two exemplary internal implementations of the output controller 230 of present invention. FIG. 5A illustrates the implementation of an output controller 230 inside a conventional printer with reference to FIG. 4A, which includes a conventional printer controller 410(5A). The output controller 230(5A) includes an interpreter 510A component for decoding the intermediate output data of present invention; and a converter component 530A for converting one or more decoded output images into a printer-controller print data that is suitable for input to the printer controller 410(5A). An optional image processing component 520A may be included in the output controller 230(5A). FIG. 5B illustrates the implementation of an output controller 230 included internally in a conventional output device 220 with reference to FIG. 4B, which does not include a printer controller. The output controller 230(5B) includes an interpreter 510B component for decoding the intermediate output data of present invention; an image processor 520B component for performing one or more image processing operations such as color space conversion, color matching and digital halftoning; and an optional encoder 530B component to conform the processed output images into an output-engine output data that is suitable for input to the output engine 420B if the result of the image processing is not already in required form suitable for the output engine 420B. In one implementation, output device 220 may include a communication unit 550 or adapter to interface with information apparatus 200. Output device 220 may sometimes include more than one communication unit 550 in order to support different interfaces, protocols, or communication standards with different devices. For example, output device 220 may communicate with a first information apparatus 200 through a Bluetooth interface while communicating with a second information apparatus 200 through a parallel interface. Examples of hardware components of a wireless communication unit are described in greater detail below with reference to FIGS. 8A and 8B. In one embodiment, output controller 230 does not include a communication unit, but rather utilizes or manages a communication unit residing in the associated output device 220 such as the illustration in FIG. 5. In another embodiment, output controller 230 may include or provide a communication unit to output device 220 as shown in FIG. 6. For example, an output controller 230 with a wireless communication unit may be installed internally or connected externally to a legacy printer to provide it with wireless communication capability that was previously lacking. FIG. 6 includes three functional block diagrams illustrating the hardware/software components of output controller 230 in three different implementations. Each components of an output controller 230 may include software, hardware, or combination. For example, an output controller 230 may include components using one or more or combinations of an application-specific integrated circuit (ASIC), a digital signal processor (DSP), a field programmable gate array (FPGA), firmware, system on a chip, and various communication chip sets. Output controller 230 may also contain embedded processors 670 A with software components or embedded application software to implement its feature sets and functionalities. Output controller 230 may contain an embedded operating system 680. With an operating system, some or all functionalities and feature sets of the output controller 230 may be provided by application software managed by the operating system. Additional application software may be installed or upgraded to newer versions in order to, for example, provide additional functionalities or bug fixes. FIG. 6A and FIG. 6C illustrates examples of implementation with an operating system 680 while FIG. 6B illustrates an example without the operating system 680 or the optional embedded processor 670. Output controller 230 typically includes a memory unit 640, or may share a memory unit with, for example, printer controller 410. The memory unit and storage unit, such as ROM, RAM, flash memory and disk drive among others, may provide persistent or volatile storage. The memory unit or storage unit may store output device profiles, objects, codes, instructions or data (collectively referred to as software components) that implement the functionalities of the output controller 230. Part of the software components (e.g., output device profile) may be uploaded to information apparatus 200 during or before a data output operation. An output controller 230 may include a processor component 670A and 670C, a memory component 650, an optional storage component 640, and an optional operating system component 680. FIG. 6 shows one architecture or implementation where the memory 650, storage 640, processor 670, and operating system 680 components, if exist, can be share or accessed by other operational components in the output controller 230 such as the interpreter 610 and image processor 650. FIG. 6 shows two communication units 660A and 660B included in the output controller 230; however, the output controller 230 of present invention may include any number of communication units 660. It is also possible that the output controller does not contain any communication unit but rather utilizes the communication unit of an output device. The output controller 230 may be connected externally to an output device 220 or integrated internally into the output device 220. FIGS. 5A and 5B illustrate implementations of output controller 230 inside an output device 220. The output controller 230, however, may also be implemented as an external box or station that is wired or wirelessly connected to an output device 220. An output controller 230 implemented as an external box or station to an output device 220 may contain its own user interface. One example of such an implementation is a print server connected to an output device 220 in an output system 250. Another configuration and implementation is to integrate or combine the functionalities of an output controller 230 with an existing printer controller 410 (referred to as “combined controller”) if the output device 220 is a printer as shown with reference to FIG. 7C or 7F. A combined controller can also be internally integrated or externally connected to output device 220, and include functionalities of both printer controller 410 (e.g., input interpretation and or raster image processing) and output controller 230 of present invention. One advantage of this configuration is that the functionalities or components of output controller 230 and printer controller 410 may share the same resources, such as processing unit, memory unit, etc. FIG. 6C illustrates an example of a combined controller implementation or output controller 230 where the printer controller 410C, interpreter 610C and converter 630C shares the use of the processor 670C, memory 650C and storage 640C, managed by an operating system 680C. Various exemplary implementations and configurations of an output controller 230 with respect to an output device 220 or output system 250 are illustrated in further detail with reference to FIG. 7. Other possible implementations of output controller 230 may include, for example, a conventional personal computer (PC), a workstation, and an output server or print server. In these cases, the functionalities of output controller 230 may be implemented using application software installed in a computer (e.g., PC, server, or workstation), with the computer connected with a wired or wireless connection to an output device 220. Using a PC, server, workstation, or other computer to implement the feature sets of output controller 230 with application software is just another possible embodiment of the output controller 230 and in no way departs from the spirit, scope and process of the present invention. The difference between output controller 230 and printer controller 410 should be noted. Printer controller 410 and output controller 230 are both controllers and are both dedicated hardware and or software for at least one output device 220. Output controller 230 refers to a controller with feature sets, capabilities, and functionalities of the present invention. A printer controller 410 may contain functions such as interpreting an input page description language, raster image processing, and queuing, among others. An output controller 230 may include part or all of the features of a printer controller 410 in addition to the feature sets, functionalities, capabilities, and processes of present invention. Functionalities and components of output controller 230 for the purpose of providing universal data output may include or utilize: Components and operations to receive output data from a plurality of information apparatus 200; the output data may include an intermediate output data containing at least one rasterized image related to the data content intended for output. Components and operations to interpret and/or decode the intermediate output data. Components and operations to process the intermediate output data. Such components and operations may include image processing functions such as scaling, segmentation, color correction, color management, GCR, image enhancement, decompression, decryption, and or halftoning among others. Components and operations to generate an output-engine output data, the output-engine output data being in an output data format acceptable for input to an output engine. Components and operations to send the output-engine output data to the output engine. When associated with an output device 220 that includes a printer controller 410, the output controller of present invention may further include or utilize: Components and operations to convert the intermediate output data into a printer-controller print data (e.g. a PDL such as PostScript and PCL), the printer-controller print data being in a format acceptable to a printer controller. Components and operations to send printer-controller print data to one or more printer controllers. In addition to the above components and functionalities, output controller 230 may further include one or more of the following: Components and operations to communicate with one or more information apparatus 200 through a wired or wireless interface. Components and operations to communicate and or manage a communication unit included in the output controller 230 or output device 220. Components and operations to store at least part of an output device profile (a printer profile in case of a printer) in a memory component. Components and operations to respond to service request from an information apparatus 200 by transmitting at least part of an output device profile to the information apparatus requesting service. The output controller 230 may transmit the output device profiles or object in one or multiple sessions. Components and operations to broadcast or advertise the services provided by a host output device 220 to one or more information apparatus 200 that may request such services. Components and operations to implement payment processing and management functions by, for example, calculating and processing payments according to the services requested or rendered to a client (information apparatus 200). Components and operations to provide a user interface such as display screen, touch button, soft key, etc. Components and operations to implement job management functions such as queuing and spooling among others. Components and operations to implement security or authentication procedures. For example, the output controller 230 may store in its memory component (or shared memory component) an access control list, which specifies what device or user may obtain service from its host (or connected) output device 220. Therefore, an authorized information apparatus 200 may gain access after confirming with the control list. When output controller 230 is implemented as firmware, or an embedded application, the configuration and management of the functionalities of output controller 230 may be optionally accomplished by, for example, using controller management software in a host computer. A host computer may be a desktop personal computer (PC), workstation, or server. The host computer may be connected locally or through a network to the output device 220 or the controller 230. Communication between the host computer and the output controller 230 can be accomplished through wired or wireless communication. The management application software in the host computer can manage the settings, configurations, and feature sets of the output controller 230. Furthermore, host computer's configuration application may download and or install application software, software components and or data to the output controller 230 for the purpose of upgrading, updating, and or modifying the features and capabilities of the output controller 230. Output device 220 in one implementation includes or is connected to output controller 230 described above. Therefore, functionalities and feature sets provided by output controller 230 are automatically included in the functionalities of output device 220. The output device 220 may, however, implement or include other controllers and/or applications that provide at least partially the features and functionalities of the output controller 230. Therefore, the output device 220 may include some or all of the following functionalities: Components and operations to receive multiple service requests or queries (e.g., a service request, a data query, an object or component query etc.) from a plurality of information apparatus 200 and properly respond to them by returning components, which may contain data, software, instructions and/or objects. Components and operations to receive output data from a plurality of information apparatus 200; the output data may include an intermediate output data containing one or more rasterized image related to the content intended for output. Components and operations to interpret and/or decoding the intermediate output data. Components and operations to process and/or convert the intermediate output data into a form (e.g. output-engine print data) suitable for rendering at an output engine associated with the output device. Components and operations to render a representation or an image related to the content onto an output medium (e.g. substrate or a display screen). An output device 220 may further comprise optionally one or more of the following functionalities: Components and operations for establishing and managing a communication link with an information apparatus 200 requesting service; the communication link may include wired or wireless communication. Components and operations for storing at least part of an output device profile (e.g. printer profile) in a memory component. Components and operations to provide at least part of an output device profile (e.g., printer profile in case of a printer) to one or more information apparatus 200 requesting service. The output device 220 may transmit the output device profile in one or multiple sessions. Components and operations to advertise or broadcast services provided or available to one or more information apparatus 200. Components and operations to implement payment processing and management functions by, for example, calculating and processing payments according to the services requested by or rendered to a client (information apparatus 200). Components and operations to implement job management functionalities such as queuing and spooling among others. Components and operations to provide a user interface such as display screen touch button, soft key, power switch, etc. Components and operations to implement security or authentication procedures. For example, the output device 220 may store in its memory component (or a shared memory component) an access control list, which specifies what device or user may obtain service from it. Therefore, an authorized information apparatus 200 may gain access after confirming with the control list. FIGS. 7A-7F illustrate various alternative configurations and implementations of output controller 230 with respect to an output device 230. Printer is sometimes used as an exemplary output device 230 to demonstrate the various configurations. It should be understood, however, the output device 230 of present invention is not limited to printers. As described with reference to FIG. 4, a printer may or may not contain a printer controller 410. Printer 400A that includes a printer controller 410 typically has higher speed and is more expensive than printer 400B which does not include a printer controller 410. FIG. 7A shows that output controller 230 may be cascaded externally to one or more printers (only one shown). Information apparatus 200 communicates with output controller 230A, which then communicates with output device 220 such as a printer 220A. The communication link between the output controller 230A and the printer 220A may be a wired link or a wireless link, as described above. FIGS. 6A and 6B illustrates two examples of functional component design of the output controller that can implement the configuration illustrated in FIG. 7A. The Image processor 620 in this implementation is optional. FIG. 7B shows another implementation in which output controller 230B is installed as one or more circuit boards or cards internally inside printer 220B. The output controller 230B may co-exist with printer controller 410 and other components of the printer 220B. One example of this implementation is to connect output controller 230B sequentially with the printer controller 310. FIG. 5A shows as an example of an implementation. FIG. 7C shows another implementation in which the functionalities of output controller 230 and printer controller 410 are combined into a single controller (referred to as “combined controller”) 230C. In this implementation, it is possible to reduce the cost of material when compared to implementing two separate controllers as shown in FIG. 7B. As an example, the combined controller 230C may share the same processors, memories, and storages to run the applications and functionalities of the two types of controllers and therefore, may have lower component costs when compared to providing two separate controllers. FIG. 6C illustrates an example of a combined controller functional component implementation. Some printers do not include a raster image processor or printer controller 410, as illustrated in FIG. 4B. An example of this type of printer is a lower cost desktop inkjet printer. Input to an inkjet printer may consist of a compressed CMYK data (proprietary or published) with one or more bits per pixel input. To output to a printer that does not include a printer controller, a device specific software application or a printer driver is typically required in an information apparatus 200 to perform raster image processing operations. Accordingly, output controller 230 can be implemented into a variety of output devices 220 and/or output systems 250 including printers that do not have printer controllers for performing raster image processing operations. FIG. 7D and FIG. 7E illustrate two implementations of output controller 230 in an output device 220 or system 250. The output device 230 or system 250 may include a display device, a projection device, an audio output device or a printing device. In the case when the output device 220D or 220E is a printer, it does not include a printer controller. FIG. 7D illustrates an implementation of an output controller 230D installed as an external component or “box” to output device 220D. For example, the output controller 230 may be implemented as an application in a print server or as a standalone box or station. In this configuration, some or all of raster image processing operations may be implemented in the output controller 230D. Output controller 230D receives intermediate output data from an information apparatus 200 and generates output-engine output data that is acceptable to the output engine included in the output device 220D. The output controller 230D may send the output data to the output device 220D through a wired or wireless communication link or connection. FIGS. 6A and 6B illustrates two example of functional component design of the output controller that can implement the configurations for both FIGS. 7D and 7E. FIG. 7E shows a fifth implementation of output controller 230E in which the output controller 230E is incorporated within output device 220E as one or more circuit boards or cards and may contain software and applications running on an embedded processor. As with output device 220D (FIG. 7D), output device 220E does not include a printer controller 410. Accordingly, the output controller 230E implements the functionalities and capabilities of present invention that may include part of or complete raster imaging processing operation. FIG. 7F shows a sixth implementation, an external combined controller 230F that integrates the functionalities of a printer controller 310 and an output controller into a single external combined controller component or “box” 230F. The two controller functions may share a common processor as well as a common memory space to run applications of the two types of controllers. Under this configuration, either information apparatus 200 or the combined controller 230F could perform or share at least part of raster image processing functionality. FIG. 6C shows an example of functional components of a combined controller 230F. Another implementation of the combined controller 230F shown in FIG. 7F is to use an external computing device (PC, workstation, or server) running one or more applications that include the functionality of output controller 230 and printer controller 410. The above are examples of different implementations and configurations of output controller 230. Other implementations are also possible. For example, partial functionalities of output controller 230 may be implemented in an external box or station while the remaining functionalities may reside inside an output device 220 as a separate board or integrated with a printer controller 410. As another example, the functionalities of output controller 230 may be implemented into a plurality of external boxes or stations connected to the same output device 220. As a further example, the same output controller 230 may be connected to service a plurality of output devices 220 FIGS. 8A and 8B are block diagrams illustrating two possible configurations of hardware/software components of wireless communication units. These wireless communication units can be implemented and included in information apparatus 200, in output controller 230 and in output device 220. Referring to FIG. 8A, a radio adapter 800 may be implemented to enable data/voice transmission among devices (e.g., information apparatus 200 and output device 220) through radio links. An RF transceiver 814 coupled with antenna 816 is used to receive and transmit radio frequency signals. The RF transceiver 814 also converts radio signals into and from electronic signals. The RF transceiver 814 is connected to an RF link controller 810 by an interface 812. The interface 812 may perform functions such as analog-to-digital conversion, digital-to-analog conversion, modulation, demodulation, compression, decompression, encoding, decoding, and other data or format conversion functions. RF link controller 810 implements real-time lower layer (e.g., physical layer) protocol processing that enables the hosts (e.g., information apparatus 200, output controller 230, output device 220, etc.) to communicate over a radio link. Functions performed by the link controller 810 may include, without limitation, error detection/correction, power control, data packet processing, data encryption/decryption and other data processing functions. A variety of radio links may be utilized. A group of competing technologies operating in the 2.4 GHz unlicensed frequency band is of particular interest. This group currently includes Bluetooth, Home radio frequency (Home RF) and implementations based on IEEE 802.11 standard. Each of these technologies has a different set of protocols and they all provide solutions for wireless local area networks (LANs). Interference among these technologies could limit deployment of these protocols simultaneously. It is anticipated that new local area wireless technologies may emerge or that the existing ones may converge. Nevertheless, all these existing and future wireless technologies may be implemented in the present invention without limitation, and therefore, in no way depart from the scope of present invention. Among the currently available wireless technologies, Bluetooth may be advantageous because it requires relatively lower power consumption and Bluetooth-enabled devices operate in piconets, in which several devices are connected in a point-to-multipoint system. Referring to FIG. 8B, one or more infrared (IR) adapters 820 may be implemented to enable data transmission among devices through infrared transmission. The IR adapters 820 may be conveniently implemented in accordance with the Infrared Data Association (IrDA) standards and specifications. In general, the IrDA standard is used to provide wireless connectivity technologies for devices that would normally use cables for connection. The IrDA standard is a point-to-point (vs. point-to-multipoint as in Bluetooth), narrow angle, ad-hoc data transmission standard. Configuration of infrared adapters 820 may vary depending on the intended rate of data transfer. FIG. 8B illustrates one embodiment of infrared adapter 820. Transceiver 826 receives/emits IR signals and converts IR signals to/from electrical signals. A UART (universal asynchronous receiver/transmitter) 822 performs the function of serialization/deserialization, converting serial data stream to/from data bytes. The UART 822 is connected to the IR transceiver 826 by encoder/decoder (ENDEC) 824. This configuration is generally suitable for transferring data at relatively low rate. Other components (e.g., packet framer, phase-locked loop) may be needed for higher data transfer rates. FIGS. 8A and 8B illustrate exemplary hardware configurations of wireless communication units. Such hardware components may be included in devices (e.g., information apparatus 200, output controller 230, output device 220, etc.) to support various wireless communications standards. Wired links, however, such as parallel interface, USB, Firewire interface, Ethernet and token ring networks may also be implemented in the present invention by using appropriate adapters and configurations. FIG. 9 is a logic flow diagram of an exemplary raster imaging process (RIP) 902 that can implement the universal output method of present invention. Content (e.g. digital document) 900 may be obtained and/or generated by an application running in an information apparatus 200. For example, a document browsing application may allow a user to download and or open digital document 900 stored locally or in a network node. As another example, a document creating or editing application may allow a user to create or edit digital documents in his/her information apparatus 200. A client application 210 in the information apparatus may be in the form of a device driver, invoked by other applications residing in the information apparatus 200 to provide output service. Alternatively, the client application 210 of present invention may be an application that includes data output and management component, in addition of other functionalities such as content acquisitions, viewing, browsing, and or editing etc. For example, a client application 210 in an information apparatus 200 may itself include components and functions for a user to download, view and or edit digital document 900 in addition of the output management function described herein. Raster image process method 902 allows an information apparatus 200 such as a mobile device to pervasively and conveniently output content (e.g. a digital document) to an output device 220 or system 250 that includes an output controller 230. A client application 210 in an information apparatus 200 may perform part of raster image processing operations (e.g. rasterization operation). Other operations of raster image processing such as halftoning can be completed by the output device 220 or by the output controller 230. In conventional data output methods, raster image processing is either implemented entirely in an information apparatus (e.g. a printer that does not include a printer controller with reference to FIG. 1A) or in an output device (e.g. a printer that includes a printer controller with reference to FIG. 1B). Present invention provides a more balanced approach where raster image process operations are shared between an information apparatus 200 and an output device 220 or system 250. For example, content 600 may be processed (e.g. raster image processed) by different components or parts of an overall output system from a client application 210 to an output controller 230 before being sent to an output engine or a printer engine for final output in step 960. Because the raster image processing operations are not completely implemented in the information apparatus 200, there is less processing demand on the information apparatus 200. Therefore, present RIP process may enable additional mobile devices with less memory and processing capability to have data output capability. In step 910, rasterization operation, a content (e.g. digital document), which may include text, graphics, and image objects, is conformed or rasterized to image form according to one or more rasterization parameters such as output size, bit depth, color space, resolution, number of color channels etc. During the rasterization operation, text and vector graphics information in the content are rasterized or converted into image or bitmap information according to a given set of rasterization parameters. Image information in the content or digital document may be scaled and or interpolated to fit a particular output size, resolution and bit depth etc. The rasterization parameters are in general device dependent, and therefore may vary according to different requirements and attributes of an output device 220 and its output engine. There are many ways to obtain device dependent rasterization parameters, as described in more detail below with reference to FIG. 12A. Device dependent rasterization parameters, in one example, may be obtained from an output device profile stored in an information apparatus 200, an output device 220 or an output controller 230. In an alternative implementation, rasterization parameters may be predetermined by a standard or specification. In this implementation, in step 910 the content 900 is rasterized to fit or match this predefined or standard rasterization parameters. Therefore, the rasterized output image becomes device independent. One advantage of being device independent is that the rasterized output image is acceptable with controllers, devices and/or output devices implemented or created with the knowledge of such standard or specification. A rasterized image with predefined or standardized attributes is usually more portable. For example, both the client application 210 and output device 220 or its output controller 230 may be preprogrammed to receive, interpret, and or output raster images based on a predefined standard and/or specification. Occasionally, a predefined standard or specification for rasterization parameters may require change or update. One possible implementation for providing an easy update or upgrade is to store information and related rasterization parameters in a file or a profile instead of hard coding these parameters into programs, components or applications. Client application 210, output controller 230, and/or the output device 220 can read a file or a profile to obtain information related to rasterization parameters. To upgrade or update the standard specification or defaults requires only replacing or editing the file or the profile instead of replacing a software application or component such as the client application 210. In step 920 the rasterized content in image form is encoded into an intermediate output data. The intermediate output data, which describes the output content, may include image information, instructions, descriptions, and data (e.g. color profile). The rasterized output image may require further processing including one or more of compression, encoding, encryption, smoothing, image enhancement, segmentation, color correction among others before being stored into the intermediate output data. The output image in the intermediate output data may be encoded in any image format and with any compression technique such as JPEG, BMP, TIFF, JBIG etc. In one preferred embodiment, a mixed raster content (MRC) format and its related encoding and/or compression methods are used to generate the output image. The advantages of using MRC over other image formats and techniques may include, for example, better compression ratio, better data information retention, smaller file size, and or relatively better image quality among others. In step 930, the intermediate output data is transmitted to the output device 220 or output system 250 for further processing and final output. The transmission of the intermediate output data may be accomplished through wireless or wired communication links between the information apparatus 200 and the output device 220 and can be accomplished through one or multiple sessions. In step 940, the output device 220 or output system 250 receives the transmitted intermediate output data. The output device 220 or output system 250 may include an output controller 230 to assist communicating with the information apparatus 200 and/or processing the intermediate output data. Output controller 230 may have a variety of configurations and implementations with respect to output device 220 as shown in FIG. 7A-7F. Interpretation process 940 may include one or more of parsing, decoding, decompression, decryption, image space conversion among other operations if the received intermediate output data requires such processing. An output image is decoded or retrieved from the intermediate output data and may be temporarily stored in a buffer or memory included in the output device/output system (220/250) or output controller 230 for further processing. If the intermediate output data includes components with MRC format or encoding techniques, it may contain additional segmented information (e.g. foreground and background), which can be used to enhance image quality. For example, different techniques or algorithms in scaling, color correction, color matching, image enhancement, anti-aliasing and or digital halftoning among others may be applied to different segments or layers of the image information to improve output quality or maximize retention or recovery of image information. Multiple layers may later be combined or mapped into a single layer. These image processing and conversion components and/or operations can be included in the output controller 230 of present invention. In step 950, the decoded or retrieved output image from the intermediate output data may require further processing or conversion. This may include one or more of scaling, segmentation, interpolation, color correction, GCR, black generation, color matching, color space transformation, anti-aliasing, image enhancement, image smoothing and or digital halftoning operations among others. In an embodiment where the output device 220 does not include a printer controller, an output controller 230 or an output device 220 that includes output controller, after performing the remaining portion of RIP operations (e.g. color space conversion and halftoning) on the output image, may further convert the output data in step 950 into a form that is acceptable for input to a printer engine for rendering. In an alternative embodiment where the output device 220 or the output system 250 includes a conventional printer controller, the output controller may simply decodes and or converts the intermediate output data (print data in this example) into format or language acceptable to the printer controller. For example, a printer controller may require as input a page description language (e.g. PostScript, PCL, PDF, etc.), a markup language (HTML, XML etc) or other graphics or document format. In these cases, the output controller 230 may interpret, decompress and convert the intermediate print data into an output image that has optimal output resolution, bit depth, color space, and output size related to the printer controller input requirements. The output image is then encoded or embedded into a printer-controller print data (e.g. a page description language) and sent to the printer controller. A printer-controller print data is a print data that is acceptable or compatible for input to the printer controller. After the printer controller receives the printer-controller print data, the printer controller may further perform operations such as parsing, rasterization, scaling, color correction, image enhancement, halftoning etc on the output image and generate an appropriate printer-engine print data suitable for input to the printer engine. In step 960, the output-engine output data or printer-engine print data generated by the output controller 230 or the printer controller in step 950 is sent to the output engine or printer engine of the output device for final output. FIG. 10 illustrates a flow diagram of a universal data output process of the present invention that includes the raster image processing illustrated with reference to FIG. 9. A universal data output process allows an information apparatus 200 to pervasively output content or digital document to an output device. The data output process may include or utilize: A user interface component and operation where a user initiates an output process and provides an indication of the selected output content (e.g. digital document) for output. A client application component or operation that processes the content indicated for output, and generates an intermediate output data. The intermediate output data may include at least partly a raster output image description related to the content. An information apparatus component or operation that transmits the intermediate output data to one or more selected output device 220. An output device component (e.g. output controller) or operation that interprets the intermediate output data and may further process or convert the output data into a form more acceptable to an output engine for rendering of the content. With reference to FIG. 10, a user in step 1000 may initiate the universal output method or process 1002. Typically, a user initiates the output process by invoking a client application 210 in his/her information apparatus 200. The client application 210 may be launched as an independent application or it may be launched from other applications 205 (such as from a document browsing, creating or editing application) or as part of or component of or a feature of another application 205 residing in the same information apparatus 200. When launched from another application 205, such as the case when the client application is a device driver or helper application, the client application 210 may obtain information, such as the content (e.g. digital document) from that other application 205. This can be accomplished, for example, by one or combinations of messages or facilitated through an operating system or a particular object or component model etc. During output process 1002, a user may need to select one or more output devices 220 for output service. An optional discovery process step 1020 may be implemented to help the user select an output device 220. During the discovery process step 1020, a user's information apparatus 200 may (1) search for available output devices 220; (2) provide the user with a list of available output devices 220; and (3) provide means for the user to choose one or more output devices 220 to take the output job. An example of a discovery process 1020 is described below in greater detail with reference to FIG. 11. The optional discovery process 1020 may sometimes be unnecessary. For example, a user may skip the discovery process 1020 if he or she already knows the output device (e.g., printer) 220 to which the output is to be directed. In this case, the user may simply connect the information apparatus 200 to that output device 220 by wired connections or directly point to that output device 220 in a close proximity such as in the case of infrared connectivity. As another example, a user may pre-select or set the output device or devices 220 that are used frequently as preferred defaults. As a result, the discovery process 1020 may be partially or completely skipped if the default output device 220 or printer is found to be available. In stage 1030, the client application may interact with output device 220, the user, and/or other applications 205 residing in the same information apparatus 200 to (1) obtain necessary output device profile and/or user preferences, (2) perform functions or part of raster image processing operations such as rasterization, scaling and color correction, and/or (3) convert or encode at least partially the rasterized content (e.g. digital document) into an intermediate output data. The processing and generation of the intermediate output data may reflect in part a relationship to an output device profile and/or user preferences obtained, if any. The intermediate output data generated by the client application 210 is then transmitted through wired or wireless local communication link(s) 240 to the output controller 230 included or associated with the selected output device 220 or output system 250. An exemplary client application process is described in greater detail with reference to FIG. 12. In step 1040, the output controller 230 of present invention receives the intermediate output data. In the case where the selected output device 230 does not include a printer controller, the output controller 230 of present invention may further perform processing functions such as parsing, interpreting, decompressing, decoding, color correction, image enhancement, GCR, black generation and halftoning among others. In addition, the output controller 230 may further convert or conform the intermediate output data into a form or format suitable for the output engine (e.g. printer engine in the case of a printer). The generated output-engine output data from the output controller is therefore, in general, device dependent and acceptable for final output with the output engine (or the printer engine in case of a printer) included in the selected output device 220 or output system 250. In the case where the selected output device 220 is a printer, and when the printer includes or is connected to a printer controller, the output controller 230 may generate the proper language or input format required to interface with the printer controller (referred to as printer-controller print data). The printer controller may for example require a specific input such as a page description language (PDL), markup language, or a special image or graphics format. In these cases, the output controller 230 in step 1040 may interpret and decode the intermediate output data, and then convert the intermediate output data into the required printer-controller print data (e.g. PDL such as PostScript or PCL). The printer-controller print data generated by the output controller is then sent to the printer controller for further processing. The printer controller may perform interpretation and raster image processing operations among other operations. After processing, the printer controller generates a printer-engine print data suitable for rendering at the printer engine. In either case, the output controller 230 or printer controller generates an output-engine output data that is suitable for sending to or interfacing with the output engine or the printer engine included in the output device for rendering. The output data may be temporarily buffered in components of the output device 220. An implementation of the output device process 1040 is described in greater detail with reference to FIG. 13. The steps included in the universal pervasive output process 1002 may proceed automatically when a user requests output service. Alternatively, a user may be provided with options to proceed, cancel, or input information at each and every step. For example, a user may cancel the output service at any time by, for example, indicating a cancellation signal or command or by terminating the client application 210 or by shutting down the information apparatus 200 etc FIG. 11 is a flow diagram of an example of a discovery process 720, which may be an optional step to help a user locate one or more output devices 220 for an output job. The discovery process 1020 may, however, be skipped partially or entirely. Implementation of discovery process 1020 may require compatible hardware and software components residing in both the information apparatus 200 and the output device 220. The information apparatus 200 may utilize the client application 210 or other application 205 in this process. The discovery process 1020 may include: An information apparatus 200 communicating with available output devices 220 to obtain information and attributes relating to the output device 220 and or its services such as output device capability, feature sets, service availability, quality of service, condition. An Information apparatus 200 provides the user information on each available and or compatible output devices 220. A user selects or the client application 210 (automatically or not) selects one or more output devices 220 for the output service from the available or compatible output devices 220. Various protocols and or standards may be used during discovery process 1020. Wireless communication protocols are preferred. Wired communication, on the other hand, may also be implemented. Examples of applicable protocols or standards may include, without limitation, Bluetooth, HAVi, Jini, Salutation, Service Location Protocol, and Universal Plug-and-play among others. Both standard and proprietary protocols or combination may be implemented in the discovery process 1020. However, these different protocols, standards, or combination shall not depart from the spirit and scope of present invention. In one implementation an application (referred here for simplicity of discussion as a “communication manager,” not shown) residing in the information apparatus 200 helps communicate with output device 220 and manages service requests and the discovery process 1020. The communication manager may be a part of or a feature of the client application 210. Alternatively or in combination, the communication manager may also be a separate application. When the communication manager is a separate application, the client application 210 may have the ability to communicate, manage or access functionalities of the communication manager. The discovery process 1020 may be initiated manually by a user or automatically by a communication manager when the user requests an output service with information apparatus 200. In the optional step 1100, a user may specify searching or matching criteria. For example, a user may indicate to search for color printers and or printers that provide free service. The user may manually specify such criteria each time for the discovery process 1020. Alternatively or in combination, a user may set default preferences that can be applied to a plurality of discovery processes 1020. Sometimes, however, no searching criteria are required: the information apparatus 200 may simply search for all available output devices 220 that can provide output service. In step 1101, information apparatus 200 searches for available output devices 220. The searching process may be implemented by, for example, an information apparatus 200 (e.g. with the assistance of a communication manager) multi-casting or broadcasting or advertising its service requests and waiting for available output devices 220 to respond. Alternatively or in combination, an information apparatus 200 may “listen to” service broadcasts from one or more output devices 220 and then identify the one or more output devices 220 that are needed or acceptable. It is also possible that multiple output devices 220 of the same network (e.g., LAN) register their services with a control point (not shown). A control point is a computing system (e.g., a server) that maintains records on all service devices within the same network. An information apparatus 200 may contact the control point and search or query for the needed service In step 1102, if no available output device 220 is found, the communication manager or the client application 210 may provide the user with alternatives 1104. Such alternatives may include, for example, aborting the discovery process 1020, trying discovery process 1020 again, temporarily halting the discovery process 1020, or being notified when an available output device 220 is found. As an example, the discovery process 1020 may not detect any available output device 220 in the current wired/wireless network. The specified searching criteria (if any) are then saved or registered in the communication manager. When the user enters a new network having available output devices 220, or when new compatible output devices 220 are added to the current network, or when an output device 220 becomes available for any reason, the communication manager may notify the user of such availability. In step 1106, if available output devices 220 are discovered, the communication manager may obtain some basic information, or part of or the entire output device profile, from each discovered output device 220. Examples of such information may include, but not limited to, device identity, service charge, subscription, service feature, device capability, operating instructions, etc. Such information is preferably provided to the user through the user interface (e.g., display screen, speaker, etc.) of information apparatus 200. In step 1108, the user may select one or more output devices 220 based on information provided, if any, to take the output job. If the user is not satisfied with any of the available output device 220, the user may decline the service. In this case, the user may be provided with alternatives such as to try again in step 1110 with some changes made to the searching criteria. The user may choose to terminate the service request at any time. In step 1112, with one or more output devices 220 selected or determined, the communication link between information apparatus 200 and the selected output device or devices 220 may be “locked”. Other output devices 220 that are not selected may be dropped. The output process 1020 may then proceed to the client application process of step 1030 of FIG. 10. FIG. 12A is a flow diagram of an exemplary client application process with reference to step 1030 of FIG. 10. A client application process 1202 for universal output may include or utilize: A client application 210 that obtains content (e.g. digital document) intended for output. A client application 210 that obtains output device parameters (e.g. rasterization parameters, output job parameters). One example of implementation is to obtain the output device parameters from an output device profile (e.g. printer profile), which includes device dependent parameters. Such profile may be stored in an output controller 230, output device 220 or information apparatus 200. A client application 210 that may optionally obtain user preferences through (1) user's input (automatic or manual) or selections or (2) based on preset preference or pre-defined defaults or (3) combination of the above. A client application 210 that rasterizes at least part of the content intended for output (e.g. a digital document) according to one or more rasterization parameters obtained from previous steps such as through output device profile, user selection, predefined user preferences, predefined default or standard etc. A client application 210 that generates an intermediate output data containing at least part of the rasterized image related at least partly to the content intended for output. A client application that transmits the intermediate output data to an output device 220 or output controller 230 for further processing and or final output. A client application 210 may obtain content (e.g. digital document) 900 or a pointer or reference to the content in many ways. In a preferred embodiment, the client application 210 is in the form of a device driver or an independent application, and the content or its reference can be obtained by the client application 210 from other applications 205 in the same information apparatus 200. To illustrate an example, a user may first view or download or create a digital document by using a document browsing, viewing and or editing application 205 in his/her information apparatus 200, and then request output service by launching the client application 210 as a device driver or helper application. The client application 210 communicates with the document browsing or editing application to obtain the digital document or reference to the digital document. As another example, the client application 210 is an independent application and it launches another application to help locate and obtain the digital document for output. In this case, a user may first launch the client application 210, and then invoke another application 205 (e.g. document editing and or browsing application) residing in the same information apparatus 200 to view or download a digital document. The client application 210 then communicates with the document browsing or editing application to obtain the digital document for output. In another embodiment, the client application 210 itself provides multiple functionalities or feature sets including the ability for a user to select the content (e.g. digital document) for output. For example, the client application 210 of present invention may provide a GUI where a user can directly input or select the reference or path of a digital document that the user wants to output. In order to perform rasterization operation on content (e.g. digital document) 900, the client application 210 in step 1210 needs to obtain device dependent parameters of an output device 220 such as the rasterization parameters. Device dependent parameters may be included in an output device profile. A client application 210 may obtain an output device profile or rasterization parameters in various ways. As an example, an output device profile or rasterization parameters can be obtained with one or combination of the following: The client application communicates with an output device 220 to upload output device profile or information related to one or more rasterization parameters. The client application 210 obtains the output device profile from a network node (e.g. server). A user selects an output device profile stored in the user's information apparatus 200. The client application 210 automatically retrieves or uses a default profile, predefined standard values or default values among others. The client application 210 obtains output device parameters by calculating, which may include approximation, based at least partly on the information it has obtained from one or combination of an output device 220, a user, default values, and a network node. It is important to note that step 1210 is an optional step. In some instance, part of or the entire output device profile or related device dependent information may have been already obtained by the client application 210 during the prior optional discovery process (step 1020 in FIG. 10). In this case, step 1210 may be partially or entirely skipped. In one implementation, the client application 210 communicates with one or more output devices 220 to upload output device profiles stored in the memory or storage components of those one or more output devices 220 or their associated one or more output controllers 230. In some instance, the uploaded output device profile may contain partially or entirely references or pointers to device parameters instead of the device parameters themselves. The actual output device parameters may be stored in a network node or in the information apparatus 200, where they can be retrieved by the client application 210 or by other applications 205 using the references or pointers. It should be noted that a plurality of information apparatuses 200 may request to obtain output device profile or profiles from the same output device 220 at the same time or at least during overlapping periods. The output device 220 or its associated output controller 230 may have components or systems to manage multiple communication links and provide the output device profile or profiles concurrently or in an alternating manner to multiple information apparatuses 200. Alternatively, an output device 220 may provide components or systems to queue the requests from different information apparatuses 200 and serve them in a sequential fashion according to a scheme such as first come first served, quality of service, etc. Multi-user communication and service management capability with or without queuing or spooling functions may be implemented by, for example, the output controller 230 as optional feature sets. In another implementation, one or more output device profiles may be stored locally in the information apparatus 200. The client application 210 may provide a GUI where a user can select a profile from a list of pre-stored profiles. As an example, the GUI may provide the user with a list of output device names (e.g. makes and models), each corresponding to an output device profile stored locally. When the user selects an output device 220, the client application 210 can then retrieve the output device profile corresponding to the name selected by the user. In certain cases, during a discovery or communication process described earlier, the client application 210 may have already obtained the output device ID, name, or reference or other information in a variety of ways described previously. In this case, the client application 210 may automatically activate or retrieve an output device profile stored in the information apparatus 200 based on the output device ID, name, or reference obtained without user intervention. In yet another implementation, the client application 210 may use a set of pre-defined default values stored locally in a user's information apparatus 200. Such defaults can be stored in one or more files or tables. The client application 210 may access a file or table to obtain these default values. The client application 210 may also create or calculate certain default values based on the information it has obtained during previous steps (e.g. in optional discovery process, based on partial or incomplete printer profile information obtained, etc). A user may or may not have an opportunity to change or overwrite some or all defaults. Finally, if, for any reason, no device dependent information is available, the client application 210 may use standard output and rasterization parameters or pre-defined default parameters. The above illustrates many examples and variations of implementation, these and other possible variations in implementation do not depart from the scope of the present invention. In step 1220, the client application 210 may optionally obtain user preferences. In one exemplary implementation, the client application 210 may obtain user preferences with a GUI (graphical user interface). For simplicity, a standard GUI form can be presented to the user independent of the make and model of the output device 220 involved in the output process. Through such an interface, the user may specify some device independent output parameters such as page range, number of cards per page, number of copies, etc. Alternatively or in combination, the client application 210 may also incorporate output device-dependent features and preferences into the GUI presented to the user. The device-dependent portion of the GUI may be supported partly or entirely by information contained in the output device profile obtained through components and processes described in previous steps. To illustrate, device dependent features and capabilities may include print quality, color or grayscale, duplex or single sided, output page size among others. It is preferred that some or all components, attributes or fields of user preferences have default values. Part or all default values may be hard-coded in software program in client application 210 or in hardware components. Alternatively, the client application 210 may also access a file to obtain default values, or it may calculate certain default values based on the information it has obtained during previous steps or components (e.g. from an output device profile). A user may or may not have the ability to pre-configure, or change or overwrite some or all defaults. The client application 210 may obtain and use some or all defaults with or without user intervention or knowledge. In step 1230, the client application 210 of present invention performs rasterization operation to conform a content (e.g. a digital document), which may includes objects and information in vector graphics, text, and images, into one or more output images in accordance with the rasterization parameters obtained in previous steps. During rasterization process, text and vector graphics object or information in the content is rasterized or converted into image or bitmap form according to the given set of rasterization parameters. Image information in the content may require scaling and interpolation operations to conform the rasterization parameters. Rasterization process may further include operations such as scaling, interpolation, segmentation, image transformation, image encoding, color space transformation etc. to fit or conform the one or more output images to the given set of rasterization parameters such as target output size, resolution, bit depth, color space and image format etc. In step 1240, the client application 210 generates an intermediate output data that includes the rasterized one or more output images. The intermediate output data of the present invention may contain image information, instructions, descriptions, and data such as color profile among others. Creating and generating intermediate output data may further include operations such as compression, encoding, encryption, smoothing, segmentation, scaling and or color correction, among others. The image or images contained in an intermediate output data may be variously encoded and/or implemented with different image formats and/or compression methods (e.g. JPEG, BMP, TIFF, JBIG etc or combination). One preferred implementation is to generate or encode the output image in the intermediate output data with mixed raster content (MRC) description. The use of MRC in the data output process of present invention provides opportunities to improve the compression ratio by applying different compression techniques to segmented elements in the content. In addition, MRC provides opportunities to maintain more original content information during the encoding process of the output image and, therefore, potentially improve output quality. In step 1250, the client application 210 transmits intermediate output data to an output device 220 through local communication link 240. The communication link may be implemented with wired or wireless technologies and the transmission may include one or multiple sessions. It should be recognized that FIG. 12A illustrates one example of a client application process 1030 in the data output method 1002 of present invention. Other implementations with more or less steps are possible, and several additional optional processes not shown in FIG. 12 may also be included in the client application process 1030. Use of these different variations, however, does not result in a departure from the scope of the present invention. As an example, an optional authentication step may be included when the selected output device 220 provides service to a restricted group of users. Various authentication procedures may be added in step 1210 when client application 210 obtains output device profile by communicating with an output device or an output controller. As another example, authentication procedures may also be implemented in step 1250 when the client application transmits intermediate output data to one or more output devices 220 or output controllers 230. A simple authentication may be implemented by, for example, comparing the identity of an information apparatus 200 with an approved control list of identities stored in the output device 220 or output controller 230. Other more complex authentication and encryption schemes may also be used. Information such as user name, password, ID number, signatures, security keys (physical or digital), biometrics, fingerprints, voice among others, may be used separately or in combination as authentication means. Such identification and or authentication information may be manually provided by user or automatically detected by the selected output device or devices 220 or output controller 230. With successful authentication, a user may gain access to all or part of the services provided by the output device 220. The output device profile that the client application 210 obtains may vary according to the type or quality of service requested or determined. If authentication fails, it is possible that a user may be denied partially or completely access to the service. In this case, the user may be provided with alternatives such as selecting another output device 220 or alternative services. Another optional process is that a user may be asked to provide payment or deposit or escrow before, during or after output service such as step 1210 or 1250 with reference to FIG. 12. Examples of payment or deposit may include cash, credit card, bankcard, charge card, smart card, electronic cash, among others. The output controller 220 may provide payment calculation or transaction processing as optional feature sets of present invention. FIG. 12B illustrates another exemplary client application output process 1030 with which an information apparatus 200 can pervasively and universally output content to one or more output devices 220 associated with or equipped with an output controller 230 of present invention. The process illustrated in FIG. 12B is similar to the process described in FIG. 12A except that step 1210, obtaining output device profile, is skipped. In this embodiment, the client application 210 utilizes a set of hard-coded, standard or predefined output device parameters including rasterization parameters with which the client application 210 can perform rasterization operation and other required image processing functions. Users may be provided with the option of changing these parameters or inputting alternative parameters. Rasterization parameters include output size, output resolution, bit depth, color space, color channels, scale factors etc. These pre-defined parameters typically comply with a specification or a standard. The same specification and standard may also defined or describe at least partly the intermediate output data. Predefined standard parameters can be stored in a file or profile in an information apparatus 200, an output controller 230, and/or in an output device 220 for easy update or upgrade. In client output process 1204, since the rasterization parameters are predefined, the client application 210 may not need to upload printer profiles from the selected output device 230. Consequently, no two-way communication between the information apparatus 200 and the output device or devices 220 is necessary in this process 1204 when compared with process 1202 illustrated in FIG. 12A. The client application 210 performs rasterization operation 1225 based on standard and/or predefined parameters and generates a rasterized output image with predefined or standard properties of those rasterization parameters. The resulting intermediate output data, which includes at least one rasterized output image, is transmitted from the information apparatus 200 to an output device 220 in step 1250 or to its associated output controller 230 for rendering or output. The intermediate output data generated in process 1202 in general is less device dependent compared to the intermediate output data generated in the process 1202 shown in FIG. 12A. The output controller 230 included or associated with the output device 220 may be preprogrammed to interpret the raster output image, which includes properties or attributes that correspond to those standard or predefined parameters. The standard or predefined rasterization parameters may be hard coded or programmed into the client application 210 and/or the output controller 230. However, instead of hard coding those parameters, one technique to facilitate updates or changes is to store those standard parameters in a default file or profile. The standard or predefined parameters contained in the file or profile can be retrieved and utilized by applications in an information apparatus 200 (e.g. client application 210) and/or by applications or components in an output device 220 or the output controller 230. In this way, any necessary updates, upgrades or required changes to those predefined or standard parameters can be easily accomplished by replacing or modifying the file or profile instead of modifying or updating the program, application or components in the information apparatus 200, output device 220 and/or output controller 230. A client application process 1204 providing universal output capability to information apparatus 200 may include or utilize: A client application 210 that obtains content (e.g. digital document) intended for output. A client application 210 that optionally obtains user preferences (in step 1220) through (1) user's input (automatic or manual) or selections or (2) based on preset preference or predefined defaults or (3) combination of the above. A client application 210 that rasterizes content (in step 1230 or 1225) according to pre-defined or standard rasterization parameters. A client application 210 that generates intermediate output data (in step 1240) for rendering or output at an output device 220; the intermediate output data containing at least partially a rasterized image related to the content intended for output. A client application 210 that transmits the intermediate output data to an output device 220 (in step 1250) for further processing and final output. One advantage of the client output process 1204 of FIG. 12B compared to the process 1202 illustrated in FIG. 12A is that the generated intermediate output data is in general less device dependent. The device independent attribute allows the intermediate output data to be more portable and acceptable to more output devices equipped or associated with output controllers. Both data output processes (1202 and 1204) enable universal output; allowing a user to install a single client application 210 or components in an information apparatus 200 to provide output capability to more than one output device 220. FIG. 13A illustrates one example of an output device process 1302 and its associated raster imaging method of present invention. In this output device process 1302, an output device 220 is capable of receiving an intermediate output data from an information apparatus 200. The output device process 1302 and its operations may include or utilize: An output device/system or output controller that receives intermediate output data (in step 1300). The intermediate output data includes at least partially a raster output image describing at least part of the content for rendering at the output device 220 or system 250. An output device/system or output controller that interprets (in step 1310) the intermediate output data; in one preferred embodiment, the intermediate output data includes an output image utilizing one or more MRC formats or components. An output device/system or output controller that performs image processing operation (in step 1320) on the raster image. The image processing operation may include but not limited to image decompression, scaling, halftoning, color matching, among others. An output device/system or output controller that converts and or generates (in step 1330) output-engine output data that is in a format or description suitable for input to an output engine (e.g. printer engine in case of a printer) included in an output device 220. An output engine in an output device 220 that renders or generates a final output (e.g. the output-engine output data) in step 1370. The output device 220 or output system 250 may include an output controller 230 internally or externally to assist the management and operation of the output process 1302. As shown in FIG. 7, there are many possible configurations and implementations of an output controller 230 associated to an output device 220 Herein and after, output controller 230 is regarded as an integral part of the output device to which it is attached. Hence, the following described output device operations may be partially or completely performed by the output controller associated with it. In step 1300, output device process 1302 is initiated by client application 210 transmitting an intermediate output data to output device 220 or output system 250. In step 1310, the output device 220 reads and interprets the intermediate output data, containing at least one raster output image relating to the content intended for output. During the reading and interpretation process 1310, the output device 220 may include components that parse the intermediate output data and perform operations such as decompression, decoding, and decryption among others. The output image may be variously encoded and may include one or more compression methods. In the event that the method of image encoding includes MRC format, then, in one example implementation, during decoding and mapping of the output image in step 1310, the lower resolution layer and information in an image that includes MRC may be mapped, scaled or interpolated to a higher-resolution output image to produce a better image quality. Therefore, step 1310, in the event that the intermediate output data includes MRC component, each layer in an MRC image can be decompressed, processed, mapped and combined into a single combined output image layer. Step 1310 may also include scaling, color space transformation, and/or interpolation among others. In addition to the possibility of mapping methods using different scaling and interpolation ratio with different layers, another advantage of using MRC is that segmentation information contained in MRC can be utilized to apply different image processing and enhancement techniques to data in different layers of an MRC image in step 1320. In step 1320, the output device 220 may further perform image processing operations on the decoded output image. These image processing operations may include, for example, color correction, color matching, image segmentation, image enhancement, anti-aliasing, image smoothing, digital watermarking, scaling, interpolation, and halftoning among others. The image processing operations 1320 may be combined or operated concurrently with step 1310. For example, while each row, pixel, or portion of the image is being decoded and or decompressed, image processing operations 1320 is applied. In another implementation, the image processing 1320 may occur after the entire output image or a large portion of the image has been decoded or decompressed. If the intermediate output data includes MRC component, then in step 1320, there are additional opportunities to improve image quality. An image encoded in MRC contains segmented information that a traditional single layer image format does not usually have. As an example, foreground can be in one layer, and background in another. As another example, chrominance information may be in one layer and luminance may be in another. This segmented information in MRC may be used to apply different or selective image processing methods and algorithms to different layers or segments to enhance image quality or retain or recover image information. Different image processing techniques or algorithms may include color matching, color correction, black generation, halftoning, scaling, interpolation, anti-aliasing, smoothing, digital watermarking etc. For example, one can apply calorimetric color matching to foreground information and perceptual color matching to background information or vice versa. As another example, error diffusion halftoning can be applied to foreground and stochastic halftoning can be applied to background or vice versa. As yet another example, bi-cubic interpolation can be applied to a layer and bi-linear or minimum distance interpolation can be applied to a different layer. In step 1330, the output device 220 or the output controller 230 may convert the processed image (e.g. halftoned) into a form acceptable to the output engine of output device 220. This conversion step is optional, depending on the type, format and input requirement of a particular output device engine (e.g. printer engine in case of a printer). Different output engines may have different input raster image input requirements. As an example different output engines may require different input image formats, number of bits or bytes per pixel, compression or uncompressed form, or different color spaces (e.g. such as RGB, CMY, CMYK, or any combination of Hi-Fi color such as green, orange, purple, red etc). Incoming raster image data can be encoded in a row, in a column, in multiple rows, in multiple columns, in a chunk, in a segment, or a combination at a time for sending the raster data to the output engine. In some cases, step 1330 may be skipped if the result of step 1320 is already in a form acceptable to the output device engine. In other cases, however, further conversion and or processing may be required to satisfy the specific input requirement of a particular output device engine. It is important to note that the above described processing from step 1310 to step 1330 may require one or more memory buffers to temporarily store processed results. The memory buffer can store or hold a row, a column, a portion, or a chunk, of the output image in any of the steps described above. Storing and retrieving information into and from the memory buffer may be done sequentially, in an alternating fashion, or in an interlaced or interleaved fashion among other possible combinations. Step 1310 to step 1330 operations can be partially or completely implemented with the output controller 230. In step 1370, the output device engine included in the output device 220 or output system 250 receives the output-engine output data generated in step 1330 or step 1320. The output-engine output data is in a form that satisfies the input requirements and attributes of the output engine, such as color space, color channel, bit depth, output size, resolution, etc. The output engine then takes this output-engine output data and outputs or renders the data content through its marking engine or display engine. One advantage of data output method 1002 that includes output device process 1302 is that it has less processing requirements on an information apparatus 200 compared to conventional process with reference to FIG. 1A, and therefore, enables more information apparatus 200 with relatively lower processing power and memory space to have output capability. For example, some image processing functions, such as halftoning (e.g. error diffusion) may require substantial processing and computing power. In data output process 1002 that includes output device process 1302, halftoning is performed in step 1320 by an output device component (e.g. the output controller 230) included in the output device 220 or the output system 250, not in the information apparatus 200; therefore reducing the computational requirements for the information apparatus 200. Another advantage of data output 1302 is that the intermediate output data is less device dependent than the output data generated by conventional output method 102 with reference to FIG. 1A. The device independence provides opportunity to allow a single driver or application in an information apparatus 200 to output intermediate output data to a plurality of output devices 220 that include output controllers 230. Some output devices 220 may contain a printer controller 410. An example of this type of output device or printer is a PostScript printer or PCL printer among others. FIG. 13B illustrates an example of an output device process 1304 with a printer that includes a printer controller 410. As discussed in FIG. 1, a printer with a printer controller requires input such as page description language (e.g. PostScript, PCL etc.), markup language (HTML, XML etc), special image format, special graphics format, or a combination, depending on the type of the printer controller. There are many printing system configurations for providing the data output capability and process to a printer or a printing system that includes a printer controller. In one example, the existing printer controller in the output device 220 may incorporate the feature sets provided by the output controller to form a “combined controller” as described previously with reference to FIGS. 7C and 7F. In another example, the output controller 230 of present invention may be connected sequentially or cascaded to an existing printer controller; the output controller 230 can be internally installed (with reference to FIG. 7B) or externally connected (with reference to FIG. 7A) to the output device 220. For output device 220 that includes a printer controller, the output controller 230 may simply decode the intermediate output data in step 1310 and then convert it into a form acceptable for input to the printer controller in step 1350. An output device process 1304 and operations for an output device 220 or system 250 that includes a printer controller 410 may include or utilize: An output controller 230 or components in an output device 220 or system 250 that receives an intermediate print data or output data (with reference to step 1300), the intermediate print data includes at least a raster image related at least in part to the content for rendering at the output device 220. An output controller 230 or components in an output device 220 or system 250 that interprets the intermediate output data (with reference to step 1310); in one preferred embodiment, the intermediate output data includes an output image utilizing one or more MRC format or components. An output controller 230 or components in an output device 220 or system 250 that converts the intermediate output data into a printer-controller print data (with reference to step 1350); the printer-controller print data includes a format or language (e.g. PDL, PDF, HTML, XML etc.) that is acceptable or compatible to the input requirement of a printer controller. A printer controller or components in an output device 220 or system 250 that receives a printer controller print data; the printer controller may parse, interpret and further process (e.g. rasterization, scaling, image enhancement, color correction, color matching, halftoning etc.) and convert the printer-controller print data into a printer-engine print data (with reference to step 1360); the printer-engine print data comprising of a format or description acceptable for input to a printer engine in the output device 220 or the output system 250. A printer engine or components in an output device 220 or system 250 that renders or generates a final output (with reference to step 1370) with the input printer engine print data. In output device process 1304, step 1300 (receiving intermediate output data) and step 1310 (interpret intermediate output data) are identical to step 1300 and step 1310 in output device process 1302, which have been described in previous sections with reference to FIG. 13A. In step 1350, the output controller 230 converts the intermediate print data into a printer-controller print data that is in a form compatible or acceptable for input to a printer controller. For example, a printer controller may require as input a specific page description language (PDL) such as PostScript. The output controller 230 then creates a PostScript file and embeds the output image generated or retrieved in step 1310 into the PostScript file. The output controller 230 can also create and embed the output image from step 1310 into other printer controller print data formats, instructions or languages. In step 1360, the printer controller receives printer-controller print data generated in step 1350 that includes an acceptable input language or format to the printer controller. The printer controller may parse, interpret, and decode the input printer-controller print data. The printer controller may further perform raster image processing operations such as rasterization, color correction, black generation, GCR, anti-aliasing, scaling, image enhancement, and halftoning among others on the output image. The printer controller may then generate a printer-engine print data that is suitable for input to the printer engine. The type and or format of printer-engine print data may vary according to the requirement of a particular printer engine. It is important to note that the above described process from step 1310 to step 1360 may require one or more memory buffer to temporarily store processed results. The memory buffer can store or hold a row, a column, a portion, or a chunk, of the output image in any of the steps described above. Storing and retrieving information into and from the memory buffer may be done sequentially, alternated, or in an interlaced or interleaved fashion among other possible combinations. Process and operations of step 1310 to step 1360 can be implemented with output controller 230. In step 1370, the printer engine included in the output device 220 or output system 250 generates or renders the final output based on the printer-engine print data generated in step 1360. For example, the printer-engine print data may be in CMY, CMYK, and RGB etc, and this may be in one or more bits per pixel format, satisfying the size and resolution requirement of the printer engine. The printer engine included the output device 220 may take this print data and generate or render an output page through its marking engine. Having described and illustrated the principles of our invention with reference to an illustrated embodiment, it will be recognized that the illustrated embodiment can be modified in arrangement and detail without departing from such principles. In view of the many possible embodiments to which the principles of our invention may be applied, it should be recognized that the detailed embodiments are illustrative only and should not be taken as limiting the scope of our invention. Rather, I claim as my invention all such embodiments as may come within the scope of the following claims and equivalents thereto. Unless the context indicates otherwise, a reference in a claim to the number of instances of an element, be it a reference to one instance or more than one instance, requires at least the stated number of instances of the element but is not intended to exclude from the scope of the claim a structure or method having more instances of that element than stated. Specifically, but without limitation, a reference in a claim to an or one output device or system, to an or one image, or to a or one rasterization parameter is not intended to exclude from the scope of the claim a structure or method having, including, employing or supplying two or more output devices or system, images or rasterization parameters."},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE DISCLOSURE <EOH>The present invention relates to universal data output and, in particular, to providing a new data output method and a new raster image process for information apparatuses and output devices. As described herein, information apparatuses refer generally to computing devices, which include both stationary computers and mobile computing devices (pervasive devices). Examples of such information apparatuses include, without limitation, desktop computers, laptop computers, networked computers, palmtop computers (hand-held computers), personal digital assistants (PDAs), Internet enabled mobile phones, smart phones, pagers, digital capturing devices (e.g., digital cameras and video cameras), Internet appliances, e-books, information pads, and digital or web pads. Output devices may include, without limitation, fax machines, printers, copiers, image and/or video display devices (e.g., televisions, monitors and projectors), and audio output devices. For simplicity and convenience, hereafter, the following descriptions may refer to an output device as a printer and an output process as printing. However, it should be understood that the term printer and printing used in the discussion of present invention refer to one embodiment used as a specific example to simplify the description of the invention. The references to printer and printing used here are intended to be applied or extended to the larger scope and definition of output devices and should not be construed as restricting the scope and practice of present invention. Fueled by an ever-increasing bandwidth, processing power, wireless mobile devices, and wireless software applications, millions of users are or will be creating, downloading, and transmitting content and information using their pervasive or mobile computing devices. As a result, there is a need to allow users to conveniently output content and information from their pervasive computing devices to any output device. As an example, people need to directly and conveniently output from their pervasive information apparatus, without depending on synchronizing with a stationary computer (e.g., desktop personal computer) for printing. To illustrate, a mobile worker at an airport receiving e-mail in his hand-held computer may want to walk up to a nearby printer or fax machine to have his e-mail printed. In addition, the mobile worker may also want to print a copy of his to-do list, appointment book, business card, and his flight schedule from his mobile device. As another example, a user visiting an e-commerce site using his mobile device may want to print out transaction confirmation. In still another example, a user who takes a picture with a digital camera may want to easily print it out to a nearby printer. In any of the above cases, the mobile user may want to simply walk up to a printer and conveniently print a file (word processing document, PDF, HTML etc) that is stored on the mobile device or downloaded from a network (e.g., Internet, corporate network). Conventionally, an output device (e.g., a printer) is connected to an information apparatus via a wired connection such as a cable line. A wireless connection is also possible by using, for example, radio communication or infrared communication. Regardless of wired or wireless connection, a user must first install in the information apparatus an output device driver (e.g., printer driver in the case the output device is a printer) corresponding to a particular output device model and make. Using a device-dependent or specific driver, the information apparatus may process output content or digital document into a specific output device's input requirements (e.g., printer input requirements). The output device's input requirements correspond to the type of input that the output device (e.g., a printer) understands. For example, a printer's input requirement may include printer specific input format (e.g., one or more of an image, graphics or text format or language). Therefore, an output data (or print data in the case the output device is a printer) herein refers to data that is acceptable for input to an associated output device. Examples of input requirements may include, without limitation, audio format, video format, file format, data format, encoding, language (e.g., page description language, markup language etc), instructions, protocols or data that can be understood or used by a particular output device make and model. Input requirements may be based on proprietary or published standards or a combination of the two. An output device's input requirements are, therefore, in general, device dependent. Different output device models may have their own input requirements specified, designed or adopted by the output device manufacturer (e.g., the printer manufacturer) according to a specification for optimal operation. Consequently, different output devices usually require use of specific output device drivers (e.g., printer drivers) for accurate output (e.g., printing). Sometimes, instead of using a device driver (e.g., printer driver), the device driving feature may be included as part of an application software. Installation of a device driver (e.g., printer driver) or application may be accomplished by, for example, manual installation using a CD or floppy disk supplied by the printer manufacturer. Or alternatively, a user may be able to download a particular driver or application from a network. For a home or office user, this installation process may take anywhere from several minutes to several hours depending on the type of driver and user's sophistication level with computing devices and networks. Even with plug-and-play driver installation, the user is still required to execute a multi-step process for each printer or output device. This installation and configuration process adds a degree of complexity and work to end-users who may otherwise spend their time doing other productive or enjoyable work. Moreover, many unsophisticated users may be discouraged from adding new peripherals (e.g., printers, scanners, etc.) to their home computers or networks to avoid the inconvenience of installation and configuration. It is therefore desirable that an information apparatus can output to more than one output device without the inconvenience of installing multiple dedicated device dependent drivers. In addition, conventional output or printing methods may pose significantly higher challenges and difficulties for mobile device users than for home and office users. The requirement for pre-installation of a device-dependent driver diminishes the benefit and concept of mobile (pervasive) computing and output. For example, a mobile user may want to print or output e-mail, PowerPoint® presentation documents, web pages, or other documents at an airport, gas station, convenience store, kiosk, hotel, conference room, office, home, etc. It is highly unlikely that the user would find at any of these locations a printer of the same make and model as is at the user's base station. As a consequence, under the conventional printing method, the user would have to install and configure a printer driver each time at each such remote location before printing. It is usually not a viable option given the hundreds, or even thousands of printer models in use, and the limited storage, memory space, and processing power of the information apparatus. Moreover, the user may not want to be bothered with looking for a driver or downloading it and installing it just to print out or display one page of email at the airport. This is certainly an undesirable and discouraging process to promote pervasive or mobile computing. Therefore, a more convenient printing method is needed in support of the pervasive computing paradigm where a user can simply walk up to an output device (e.g., printer or display device) and easily output a digital document without having to install or pre-install a particular output device driver (e.g., printer driver). Another challenge for mobile users is that many mobile information apparatuses have limited memory space, processing capacity and power. These limitations are more apparent for small and low-cost mobile devices including, for example, PDAs, mobile phones, screen phones, pagers, e-books, Internet Pads, Internet appliances etc. Limited memory space poses difficulties in installing and running large or complex printer or device drivers, not to mention multiple drivers for a variety of printers and output devices. Slow processing speed and limited power supply create difficulties driving an output device. For example, processing or converting a digital document into output data by a small mobile information apparatus may be so slow that it is not suitable for productive output. Intensive processing may also drain or consume power or battery resources. Therefore, a method is needed so that a small mobile device, with limited processing capabilities, can still reasonably output content to various output devices. To output or render content (e.g. digital document) to an output device, a raster image processing (RIP) operation on the content is usually required. RIP operation can be computationally intensive and may include (1) a rasterization operation, (2) a color space conversion, and (3) a halftoning operation. RIP may also include other operations such as scaling, segmentation, color matching, color correction, GCR (Grey component replacement), Black generation, image enhancement compression/decompression, encoding/decoding, encryption/decryption GCR, image enhancement among others. Rasterization operation in RIP involves converting objects and descriptions (e.g. graphics, text etc) included in the content into an image form suitable for output. Rasterization may include additional operations such as scaling and interpolation operations for matching a specific output size and resolution. Color space conversion in RIP includes converting an input color space description into a suitable color space required for rendering at an output device (e.g. RGB to CMYK conversion). Digital halftoning is an imaging technique for rendering continuous tone images using fewer luminance and chrominance levels. Halftoning operations such as error diffusion can be computationally intensive and are included when the output device's bit depth (e.g. bits per pixel) is smaller than the input raster image bit depth. Conventionally, RIP operations are included either in an information apparatus, or as part of an output device or output system (e.g. in a printer controller). FIG. 1A illustrates a flow diagram of a conventional data output method 102 in which RIP 110 is implemented in the information apparatus. Output devices that do not include a printer controller to perform complex RIP operations, such as a lower-cost, lower speed inkjet printer, normally employ data output method 102 . In data output method 102 , an information apparatus obtains content (e.g. a digital document) in step 100 for rendering or output at an output device. The information apparatus may includes an application (e.g. device driver), which implements RIP operation 110 . The information apparatus generates an output data in step 120 and transmits the output data to the output device in step 130 for rendering. The output data relating to the content is in an acceptable form (e.g. in an appropriate output size and resolution) to the output engine (e.g. display engine, printer engine etc.) included in the output device. The output data in a conventional output method 102 is usually device dependent. One drawback for the data output method 102 of FIG. 1A is that the information apparatus performs most if not the entire raster image processing operations 110 required for output. The RIP operations may require intensive computation. Many information apparatus such as mobile information device might have insufficient computing power and/or memory to carry out at an acceptable speed the RIP operations 110 required in an output process. Another drawback for the conventional data output method 102 of FIG. 1A is that the generated output data is device dependent and therefore is typically not very portable to other output devices. As a result, the information apparatus may need to install multiple applications or device drivers for multiple output devices, which may further complicate its feasibility for use in information apparatuses with limited memory, storage and processing power. FIG. 1B illustrates a flow diagram of another conventional data output method 104 in which the RIP is implemented in an output device. An example of an output device that implements process 104 is a high-speed laser printer which includes a printer controller for performing RIP operations and an output engine (e.g. printer engine) for rendering content. Printer controller may be internally installed or externally connected to an output device (printer in this example). In data output method 104 , an information apparatus obtains content for output in step 100 and generates in step 160 an output data or print data for transmitting to the output device in step 170 . Print data includes information related to the content and is usually encoded in a page description language (PDL) such as PostScript and PCL etc. In step 180 , the printer receives the output data or print data (in a PDL). In step 190 , a printer controller included in the printer interprets the PDL, performs RIP operations, and generates a printer-engine print data that is in a form acceptable to the printer engine (e.g. a raster image in an appropriate output size, bit depth, color space and resolution). In step 150 the printer engine renders the content with the printer-engine print data. It will be understood that a reference to print data or output data including a language, such as PDL, should be interpreted as meaning that the print data or output data is encoded using that language. Correspondingly, a reference to a data output process generating a language, such as PDL, should be interpreted as meaning that the data output process encodes data using that language. There are many drawbacks in the conventional data output method 104 shown in FIG. 1B . These drawbacks are especially apparent for mobile computing devices with limited processing power and memory. One such drawback is that the output data or print data, which include a page description language (PDL) such as PostScript or PCL, can be very complex. Generating complex PDL may increase memory and processing requirements for an information apparatus. Furthermore, interpreting, decoding and then raster image processing complex PDL can increase computation, decrease printing speed, and increase the cost of the output device or its printer controller. Another drawback is that the output data that includes PDL can creates a very large file size that would increase memory and storage requirements for the information apparatus, the output device and/or the printer controller etc. Large file size may also increase the bandwidth required in the communication link between the information apparatus and the output device. Finally, to rasterize text in an output device, a printer controller may need to include multiple fonts. When a special font or international characters is not included or missing in the printer controller, the rendering or output can potentially become inaccurate or inconsistent."},"summary":{"kind":"string","value":"<SOH> SUMMARY OF THE INVENTION <EOH>Accordingly, this invention provides a convenient universal data output method in which an information apparatus and an output device or system share the raster image processing operations. Moreover, the new data output method eliminates the need to install a plurality of device-dependent dedicated drivers or applications in the information apparatus in order to output to a plurality of output devices. In accordance with present invention, an electronic system and method of pervasive and universal output allow an information apparatus to output content conveniently to virtually any output device. The information apparatus may be equipped with a central processing unit, input/output control unit, storage unit, memory unit, and wired or wireless communication unit or adapters. The information apparatus preferably includes a client application that may be implemented as a software application, a helper application, or a device driver (a printer driver in case of a printer). The client application may include management and control capabilities with hardware and software components including, for example, one or more communication chipsets residing in its host information apparatus. The client application in the information apparatus may be capable of communicating with, managing and synchronizing data or software components with an output device equipped with an output controller of present invention. Rendering content in an output device refers to printing an image of the content onto an substrate in the case of a printing device; displaying an image of the content in the case of a displaying device; playing an audio representation of the content in a voice or sound output device or system. An output controller may be a circuit board, card or software components residing in an output device. Alternatively, the output controller may be connected externally to an output device as an external component or “box.” The output controller may be implemented with one or more combinations of embedded processor, software, firmware, ASIC, DSP, FPGA, system on a chip, special chipsets, among others. In another embodiment, the functionality of the output controller may be provided by application software running on a PC, workstation or server connected externally to an output device. In conventional data output method 102 as described with reference to FIG. 1A , an information apparatus transmits output data to an output device for rendering. Output data corresponds to content intended for output and is mostly raster image processed (RIPed) and therefore is device dependent because raster image processing is a typical device dependent operation. Output data may be encoded or compressed with one or more compression or encoding techniques. In present invention, an information apparatus generates an intermediate output data for transmitting to an output device. The intermediate output data includes a rasterized image corresponding to the content; however, device dependent image processing operations of a RIP (e.g. color matching and halftoning) have not been performed. As a result, an intermediate output data is more device independent and is more portable than the output data generated by output method with reference to FIG. 1A . In one implementation of this invention, the intermediate output data includes MRC (Mixed raster content) format, encoding and compression techniques, which further provides improved image quality and compression ratio compared to conventional image encoding and compression techniques. In an example of raster image process and data output method of the present invention, a client application such as a printer driver is included in an information apparatus and performs part of raster image processing operation such as rasterization on the content. The information apparatus generates an intermediate output data that includes an output image corresponding to the content and sends the intermediate output data to an output device or an output system for rendering. An output controller application or component included in the output device or output system implements the remaining part of the raster image processing operations such as digital halftoning, color correction among others. Unlike conventional raster image processing methods, this invention provides a more balanced distribution of the raster image processing computational load between the Information apparatus and the output device or the output system. Computational intensive image processing operations such as digital halftoning and color space conversions can be implemented in the output device or output system. Consequently, this new raster image processing method reduces the processing and memory requirements for the information apparatus when compared to conventional data output methods described with reference to FIG. 1A in which the entire raster image process is implemented in the information apparatus. Additionally, in this invention, a client application or device driver included in the information apparatus, which performs part of the raster image processing operation, can have a smaller size compared to a conventional output application included in the information apparatus, which performs raster image processing operation. In another implementation, the present invention provides an information apparatus with output capability that is more universally accepted by a plurality of output devices. The information apparatus, which includes a client application, generates an intermediate output data that may include device independent attributes. An output controller includes components to interpret and process the intermediate output data. The information apparatus can output content to different output devices or output systems that include the output controller even when those output devices are of different brand, make, model and with different output engine and input data requirements. Unlike conventional output methods, a user does not need to preinstall in the information apparatus multiple dedicated device dependent drivers or applications for each output device. The combination of a smaller-sized client application, a reduced computational requirement in the information apparatus, and a more universal data output method acceptable for rendering at a plurality of output devices enable mobile devices with less memory space and processing capabilities to implement data output functions which otherwise would be difficulty to implement with conventional output methods. In addition, this invention can reduce the cost of an output device or an output system compared to conventional output methods 104 that include a page description language (PDL) printer controller. In the present invention, an information apparatus generates and sends an intermediate output data to an output device or system. The intermediate output data in one preferred embodiment includes a rasterized output image corresponding to the content intended for output. An output controller included in an output device or an output system decodes and processes the intermediate output data for output, without performing complex interpretation and rasterization compared to conventional methods described in process 104 . In comparison, the conventional data output process 104 generates complex PDL and sends this PDL from an information apparatus to an output device that includes a printer controller (e.g. a PostScript controller or a PCL5 controller among others). Interpretation and raster image processing of a PDL have much higher computational requirements compared to decoding and processing the intermediate output data of this invention that include rasterized output image or images. Implementing a conventional printer controller with, for example, PDL increases component cost (e.g. memories, storages, ICs, software and processors etc.) when compared to using the output controller included in the data output method of this present invention. Furthermore, an output data that includes PDL can create a large file size compared to an intermediate output data that includes rasterized output image. The data output method for this invention comparatively transmits a smaller output data from an information apparatus to an output device. Smaller output data size can speed up transmission, lower communication bandwidth, and reduce memory requirements. Finally, this invention can provide a convenient method to render content at an output device with or without connection to a static network. In conventional network printing, both information apparatus and output device must be connected to a static network. In this invention, through local communication and synchronization between an information apparatus and an output device, installation of hardware and software to maintain static network connectivity may not be necessary to enable the rendering of content to an output device. According to the several aspects of the present invention there is provided the subject matter defined in the appended independent claims. Additional objects and advantages of the present invention will be apparent from the detailed description of the preferred embodiment thereof, which proceeds with reference to the accompanying drawings."},"cpc_label":{"kind":"string","value":"G06F31236"},"filing_date":{"kind":"string","value":"20171006"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180208"},"examiner_id":{"kind":"string","value":"66411.0"},"ipc_label":{"kind":"string","value":"G06F312"},"npe_litigated_count":{"kind":"number","value":6,"string":"6"},"examiner_full_name":{"kind":"string","value":"RILEY, MARCUS T"},"invention_title":{"kind":"string","value":"WIRELESS PRINTING DEVICES THAT PROVIDE PRINTING SERVICES OVER A NETWORK WITHOUT A NEED FOR A CLIENT DEVICE OF THE PRINTING DEVICE TO USE, AT THE CLIENT DEVICE, A PRINTER SPECIFIC PRINTER DRIVER"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":1,"string":"1"},"decision_as_of_2020":{"kind":"string","value":"CONT-ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"G06F"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}},{"rowIdx":32899,"cells":{"application_number":{"kind":"number","value":15726901,"string":"15,726,901"},"decision":{"kind":"string","value":"PENDING"},"title":{"kind":"string","value":"AMLODIPINE FORMULATIONS"},"abstract":{"kind":"string","value":"Provided herein are stable amlodipine oral liquid formulations. Also provided herein are methods of using amlodipine oral liquid formulations for the treatment of certain diseases including hypertension and Coronary Artery Disease (CAD)."},"claims":{"kind":"string","value":"1. An oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. 2. The formulation of claim 1, wherein the amlodipine benzoate is formed in situ. 3. The formulation of claim 2, wherein the amlodipine benzoate is formed by a reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate with a molar excess of sodium benzoate. 4. The formulation of claim 3, wherein the salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate is selected from amlodipine besylate, amlodipine tosylate, amlodipine mesylate, amlodipine succinate, amlodipine salicylate, amlodipine maleate, amlodipine acetate, and amlodipine hydrochloride. 5. The formulation of claim 2, wherein the amlodipine benzoate is formed by the reaction of amlodipine besylate with a molar excess of sodium benzoate. 6. The formulation of claim 1, wherein the formulation further comprises a flavoring agent. 7. The formulation of claim 1, wherein the formulation further comprises a sweetener. 8. The formulation of claim 7, wherein the sweetener is sucralose. 9. The formulation of claim 1, wherein the formulation is in the form of a suspension. 10. The formulation of claim 1, wherein the pH of the formulation is between about 3 and about 8. 11. The formulation of claim 10, wherein the pH is between about 4 and about 5. 12. The formulation of claim 10, wherein the pH is between about 5 and about 6. 13. The formulation of claim 1, wherein the formulation is stable at about 25±5° C. for at least 12 months. 14. The formulation of claim 1, wherein the formulation is stable at about 5±5° C. for at least 12 months. 15. The formulation of claim 1, wherein the formulation is stable at about 25±5° C. for at least 24 months. 16. The formulation of claim 1, wherein the formulation is stable at about 5±5° C. for at least 24 months."},"description":{"kind":"string","value":"CROSS-REFERENCE This application claims the benefit of U.S. Application Ser. No. 62/405,455 filed Oct. 7, 2016, which is hereby incorporated by reference in its entirety. BACKGROUND OF THE INVENTION Hypertension, or high blood pressure, is a serious health issue in many countries. According to the National Heart Blood and Lung Institute, it is thought that about 1 in 3 adults in the United States alone have hypertension. Left unchecked, hypertension is considered a substantial risk factor for cardiovascular and other diseases including coronary heart disease, myocardial infarction, congestive heart failure, stroke and kidney failure. Hypertension is classified as primary (essential) hypertension or secondary hypertension. Primary hypertension has no known cause and may be related to a number of environmental, lifestyle and genetic factors such as stress, obesity, smoking, inactivity and sodium intake. Secondary hypertension can be caused by drug or surgical interventions or by abnormalities in the renal, cardiovascular or endocrine system. A number of antihypertensive drugs are available for treating hypertension. Various therapeutic classes of antihypertensive drugs include alpha-adrenergic blockers, beta-adrenergic blockers, calcium-channel blockers, hypotensives, mineralcorticoid antagonists, central alpha-agonists, diuretics and rennin-angiotensin-aldosterone inhibitors which include angiotensin II receptor antagonists (ARB) and angiotensin-converting enzyme (ACE) inhibitors. Angiotensin-converting enzyme (ACE) inhibitors inhibit angiotensin-converting enzyme (ACE), a peptidyl dipeptidase that catalyzes angiotension I to angiotension II, a potent vasoconstrictor involved in regulating blood pressure. Amlodipine is a calcium channel blocker. It affects the movement of calcium into the cells of the heart and blood vessels. As a result, amlodipine relaxes blood vessels and increases the supply of blood and oxygen to the heart while reducing its workload. The structural formula of amlodipine is as follows: Amlodipine is currently administered in the form of oral tablets, (e.g., Norvasc) or in the form of a refrigerated liquid formulation. In addition to the treatment of hypertension, amlodipine tablets have been used for coronary artery disease (CAD) such as chronic stable angina, vasospastic angina, or angiographically documented coronary artery disease in patients without heart failure or an ejection fraction <40%. SUMMARY OF THE INVENTION Disclosed herein is an oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the amlodipine benzoate is formed in situ. In some embodiments of an oral liquid formulation, the amlodipine benzoate is formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate with a molar excess of sodium benzoate. In some embodiments of an oral liquid formulation, the salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate is selected from amlodipine besylate, amlodipine tosylate, amlodipine mesylate, amlodipine succinate, amlodipine salicylate, amlodipine maleate, amlodipine acetate, and amlodipine hydrochloride. In some embodiments of an oral liquid formulation, the amlodipine benzoate is formed by the reaction of amlodipine besylate with a molar excess of sodium benzoate. In some embodiments of an oral liquid formulation, the formulation further comprises a flavoring agent. In some embodiments of an oral liquid formulation, the formulation further comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of an oral liquid formulation, the formulation is in the form of a suspension. In some embodiments of an oral liquid formulation, the pH of the formulation is between about 3 and about 8. In some embodiments of an oral liquid formulation, the pH is between about 4 and about 5. In some embodiments of an oral liquid formulation, the pH is between about 5 and about 6. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 24 months. Also disclosed herein is a method of treating hypertension in a subject comprising administering to that subject an oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of a method of treating hypertension, the amlodipine benzoate is formed in situ. In some embodiments of a method of treating hypertension, the amlodipine benzoate is formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate with a molar excess of sodium benzoate. In some embodiments of a method of treating hypertension, the salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate is selected from amlodipine besylate, amlodipine tosylate, amlodipine mesylate, amlodipine succinate, amlodipine salicylate, amlodipine maleate, amlodipine acetate, and amlodipine hydrochloride. In some embodiments of a method of treating hypertension, the amlodipine benzoate is formed by the reaction of amlodipine besylate with a molar excess of sodium benzoate. In some embodiments of a method of treating hypertension, the formulation further comprises a flavoring agent. In some embodiments of a method of treating hypertension, the formulation further comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of a method of treating hypertension, the formulation is in the form of a suspension. In some embodiments of a method of treating hypertension, the pH of the formulation is between about 3 and about 8. In some embodiments of a method of treating hypertension, the pH is between about 4 and about 5. In some embodiments of a method of treating hypertension, the pH is between about 5 and about 6. In some embodiments of a method of treating hypertension, the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of a method of treating hypertension, the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of a method of treating hypertension, the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of a method of treating hypertension, the formulation is stable at about 5±5° C. for at least 24 months. In some embodiments of a method of treating hypertension, the hypertension is primary (essential) hypertension. In some embodiments of a method of treating hypertension, the hypertension is secondary hypertension. In some embodiments of a method of treating hypertension, the subject has blood pressure values greater than or equal to 140/90 mmm Hg. In some embodiments of a method of treating hypertension, the subject is an adult. In some embodiments of a method of treating hypertension, the subject is elderly. In some embodiments of a method of treating hypertension, the subject is a child. In some embodiments of a method of treating hypertension, the formulation is administered to the subject in a fasted state. In some embodiments of a method of treating hypertension, the formulation is administered to the subject in a fed state. In some embodiments of a method of treating hypertension, the formulation is further administered in combination with an agent selected from the group consisting of diuretics, beta blockers, alpha blockers, mixed alpha and beta blockers, calcium channel blockers, angiotensin II receptor antagonists, ACE inhibitors, aldosterone antagonists, and alpha-2 agonists. Also disclosed herein is a method of treating Coronary Artery Disease (CAD) in a subject comprising administering to that subject an oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the amlodipine benzoate is formed in situ. In some embodiments of a method of treating Coronary Artery Disease (CAD), the amlodipine benzoate is formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate with a molar excess of sodium benzoate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate is selected from amlodipine besylate, amlodipine tosylate, amlodipine mesylate, amlodipine succinate, amlodipine salicylate, amlodipine maleate, amlodipine acetate, and amlodipine hydrochloride. In some embodiments of a method of treating Coronary Artery Disease (CAD), the amlodipine benzoate is formed by the reaction of amlodipine besylate with a molar excess of sodium benzoate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation further comprises a flavoring agent. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation further comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is in the form of a suspension. In some embodiments of a method of treating Coronary Artery Disease (CAD), the pH of the formulation is between about 3 and about 8. In some embodiments of a method of treating Coronary Artery Disease (CAD), the pH is between about 4 and about 5. In some embodiments of a method of treating Coronary Artery Disease (CAD), the pH is between about 5 and about 6. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is stable at about 5±5° C. for at least 24 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the Coronary Artery Disease (CAD) is chronic stable angina, vasospastic angina, or angiographically documented coronary artery disease. In some embodiments of a method of treating Coronary Artery Disease (CAD), the angiographically documented coronary artery disease is in patients without heart failure or an ejection fraction <40%. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is further administered in combination with an additional anti-anginal agent. Disclosed herein is an oral liquid formulation, comprising: (i) a pharmaceutically acceptable salt of amlodipine; (ii) a buffer; (iii) water; and (iv) optionally one or more agents selected from the group consisting of preservatives, flavoring agents, sweetening agents, surfactants, suspensions aids, and antifoaming agents; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments of an oral liquid formulation, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments of an oral liquid formulation, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate or amlodipine naphthalene sulfonate with a molar excess of a salt forming agent. In some embodiments of an oral liquid formulation, the pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate or amlodipine naphthalene sulfonate is amlodipine besylate. In some embodiments of an oral liquid formulation, the salt forming agent is sodium benzoate. In some embodiments of an oral liquid formulation, the amount of sodium benzoate as the salt forming agent is about 1.0 mg/ml to about 10.0 mg/ml. In some embodiments of an oral liquid formulation, the salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments of an oral liquid formulation, the amount of sodium naphthalene-2-sulfonate as the salt forming agent is about 0.5 mg/ml to about 2.5 mg/ml. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises a surfactant. In some embodiments of an oral liquid formulation, the surfactant is polysorbate 80. In some embodiments of an oral liquid formulation, the amount of the surfactant is about 0.1 mg/ml to about 2.5 mg/ml. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises a preservative. In some embodiments of an oral liquid formulation, the preservative is selected from the group consisting of sodium benzoate, a paraben or paraben salt, and combinations thereof. In some embodiments of an oral liquid formulation, the amount of preservative is about 0.1 mg/ml to about 2.0 mg/ml. In some embodiments of an oral liquid formulation, the buffer comprises a citrate buffer. In some embodiments of an oral liquid formulation, the citrate buffer concentration is about 3 mM. In some embodiments of an oral liquid formulation, the buffer comprises a phosphate buffer. In some embodiments of an oral liquid formulation, the phosphate buffer concentration is about 3 mM. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises a suspension aid. In some embodiments of an oral liquid formulation, the suspension aid comprises silicon dioxide, hydroxypropyl methylcellulose, methylcellulose, microcrystalline cellulose, carboxymethylcellulose sodium, polyvinylpyrrolidone, or combinations thereof. In some embodiments of an oral liquid formulation, the suspension aid is silicon dioxide. In some embodiments of an oral liquid formulation, the amount of silicon dioxide is about 0.1 mg/ml to about 1.0 mg/ml. In some embodiments of an oral liquid formulation, the suspension aid is hydroxypropyl methylcellulose. In some embodiments of an oral liquid formulation, the amount of hydroxypropyl methylcellulose is about 3 mg/ml to about 10 mg/ml. In some embodiments of an oral liquid formulation, the suspension aid is a combination of silicon dioxide and hydroxypropyl methylcellulose. In some embodiments of an oral liquid formulation, the amount of silicon dioxide is about 0.1 mg/ml to about 1.0 mg/ml and the amount of hydroxypropyl methylcellulose is about 3 mg/ml to about 10 mg/ml. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises an antifoaming agent. In some embodiments of an oral liquid formulation, the antifoaming agent is simethicone. In some embodiments of an oral liquid formulation, the amount of the antifoaming agent is about 0.05 mg/ml to about 1.0 mg/ml. In some embodiments of an oral liquid formulation, the formulation comprises a flavoring agent. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of an oral liquid formulation, the oral liquid formulation further comprises unreacted salt forming agent. In some embodiments of an oral liquid formulation, the oral liquid formulation is in the form of a suspension. In some embodiments of an oral liquid formulation, the pH of the oral liquid formulation is between about 3 and about 8. In some embodiments of an oral liquid formulation, the pH is between about 4 and about 5. In some embodiments of an oral liquid formulation, the pH is between about 5 and about 6. In some embodiments of an oral liquid formulation, the amount of the pharmaceutically acceptable salt of amlodipine corresponds to about 0.8 mg/ml to about 1.2 mg/ml of amlodipine free base. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 24 months. Also disclosed herein is an oral liquid formulation, comprising: (i) a pharmaceutically acceptable salt of amlodipine in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) optionally about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments of an oral liquid formulation, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments of an oral liquid formulation, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed by the reaction of amlodipine besylate with a molar excess of a salt forming agent. In some embodiments of an oral liquid formulation, the salt forming agent is sodium benzoate. In some embodiments of an oral liquid formulation, the amount of sodium benzoate as the salt forming agent is about 1.0 mg/ml to about 10.0 mg/ml. In some embodiments of an oral liquid formulation, the salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments of an oral liquid formulation, the amount of sodium naphthalene-2-sulfonate as the salt forming agent is about 0.5 mg/ml to about 2.5 mg/ml. In some embodiments of an oral liquid formulation, the formulation further comprises a flavoring agent. In some embodiments of an oral liquid formulation, the formulation further comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of an oral liquid formulation, the oral liquid formulation further comprises unreacted salt forming agent. In some embodiments of an oral liquid formulation, the formulation is in the form of a suspension. In some embodiments of an oral liquid formulation, the pH of the formulation is between about 3 and about 8. In some embodiments of an oral liquid formulation, the pH is between about 4 and about 5. In some embodiments of an oral liquid formulation, the pH is between about 5 and about 6. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 24 months. Also disclosed herein is a process for preparing a stable amlodipine oral liquid formulation, the process comprising mixing a first mixture with a second mixture; the first mixture comprising: (i) amlodipine benzoate; (ii) sodium benzoate; (iii) optionally polysorbate 80; and (iv) water; and the second mixture comprising: (i) citric acid; (ii) sodium citrate; (iii) sucralose; (iv) optionally a flavoring agent; (v) hydroxypropyl methylcellulose; (vi) simethicone; (vii) silicon dioxide; and (viii) water. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the first mixture is obtained by a process comprising: (i) adding water to a first container which is not stainless steel; (ii) adding amlodipine besylate to the first container; (iii) adding sodium benzoate to the first container; (iv) optionally adding polysorbate 80 to the first container; and (v) stirring until amlodipine benzoate substantially precipitates. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the second mixture is obtained by a process comprising: (i) adding water to a second container; (ii) adding citric acid to the second container; (iii) adding sodium citrate to the second container; (iv) adding sucralose to the second container; (v) optionally adding the flavoring agent to the second container; (vi) adding hydroxypropyl methylcellulose to the second container; (vii) adding simethicone to the second container; (viii) adding silicon dioxide to the second container; and (ix) stirring. Also disclosed herein is a process for preparing a stable amlodipine oral liquid formulation, the process comprising mixing a first mixture with a second mixture; the first mixture comprising: (i) amlodipine naphthalene sulfonate; (ii) optionally sodium benzoate; (iii) optionally polysorbate 80; and (iv) water; and the second mixture comprising: (i) citric acid; (ii) sodium citrate; (iii) sucralose; (iv) optionally a flavoring agent; (v) hydroxypropyl methylcellulose; (vi) simethicone; (vii) silicon dioxide; and (viii) water. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the first mixture is obtained by a process comprising: (i) adding water to a first container which is not stainless steel; (ii) adding amlodipine besylate to the first container; (iii) adding sodium naphthalene-2-sulfonate to the first container; (iv) adding sodium benzoate to the first container; (v) optionally adding polysorbate 80 to the first container; and (vi) stirring until amlodipine naphthalene sulfonate substantially precipitates. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the second mixture is obtained by a process comprising: (i) adding water to a second container; (ii) adding citric acid to the second container; (iii) adding sodium citrate to the second container; (iv) adding sucralose to the second container; (v) optionally adding the flavoring agent to the second container; (vi) adding hydroxypropyl methylcellulose to the second container; (vii) adding simethicone to the second container; (viii) adding silicon dioxide to the second container; and (ix) stirring. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the first mixture does not comprise sodium benzoate and the second mixture further comprises a paraben. Also disclosed herein is a method of treating hypertension in a subject comprising administering to that subject a therapeutically effective amount of an amlodipine oral liquid formulation comprising: (i) a pharmaceutically acceptable salt of amlodipine in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) optionally about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of a method of treating hypertension, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments of a method of treating hypertension, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments of a method of treating hypertension, the oral liquid formulation further comprises unreacted salt forming agent. In some embodiments of a method of treating hypertension, the salt forming agent is sodium benzoate. In some embodiments of a method of treating hypertension, the salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments of a method of treating hypertension, the hypertension is primary (essential) hypertension. In some embodiments of a method of treating hypertension, the hypertension is secondary hypertension. In some embodiments of a method of treating hypertension, the subject has blood pressure values greater than or equal to 140/90 mmm Hg. In some embodiments of a method of treating hypertension, the subject is an adult. In some embodiments of a method of treating hypertension, the subject is elderly. In some embodiments of a method of treating hypertension, the subject is a child. In some embodiments of a method of treating hypertension, the formulation is administered to the subject in a fasted state. In some embodiments of a method of treating hypertension, the formulation is administered to the subject in a fed state. In some embodiments of a method of treating hypertension, the formulation is further administered in combination with an agent selected from the group consisting of diuretics, beta blockers, alpha blockers, mixed alpha and beta blockers, calcium channel blockers, angiotensin II receptor antagonists, ACE inhibitors, aldosterone antagonists, and alpha-2 agonists. Also disclosed herein is a method of treating Coronary Artery Disease (CAD) in a subject comprising administering to that subject a therapeutically effective amount of an amlodipine oral liquid formulation comprising: (i) a pharmaceutically acceptable salt of amlodipine in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) optionally about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments of a method of treating Coronary Artery Disease (CAD), the oral liquid formulation further comprises unreacted salt forming agent. In some embodiments of a method of treating Coronary Artery Disease (CAD), the salt forming agent is sodium benzoate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the Coronary Artery Disease (CAD) is chronic stable angina, vasospastic angina, or angiographically documented coronary artery disease. In some embodiments of a method of treating Coronary Artery Disease (CAD), the angiographically documented coronary artery disease is in patients without heart failure or an ejection fraction <40%. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is further administered in combination with an additional anti-anginal agent. INCORPORATION BY REFERENCE All publications, patents, and patent applications mentioned in this specification are herein incorporated by reference to the same extent as if each individual publication, patent, or patent application was specifically and individually indicated to be incorporated by reference. BRIEF DESCRIPTION OF THE DRAWINGS The novel features of the invention are set forth with particularity in the appended claims. A better understanding of the features and advantages of the present invention will be obtained by reference to the following detailed description that sets forth illustrative embodiments, in which the principles of the invention are utilized, and the accompanying drawings of which: FIG. 1 shows the amount of amlodipine remaining in solution over time. FIG. 2 shows the amount of amlodipine in solution for (x) amlodipine besylate and (∘) amlodipine benzoate in the presence of added sodium benzoate. DETAILED DESCRIPTION OF THE INVENTION Provided herein are stable amlodipine oral liquid formulations. These amlodipine formulations described herein are useful for the treatment of hypertension and coronary artery disease. The formulations are advantageous over conventional solid dosage administration of amlodipine ranging from ease of administration, accuracy of dosing, accessibility to additional patient populations such as to children and the elderly, and an increased patient compliance to medication. It is generally known that certain segments of the population have difficulty ingesting and swallowing solid oral dosage forms such as tablets and capsules. As many as a quarter of the total population has this difficulty. Often, this leads to non-compliance with the recommended medical therapy with the solid dosage forms, thereby resulting in rending the therapy ineffective. Further, solid dosage forms are not recommended for children or elderly due to increased risk in choking. Furthermore, the dose of amlodipine to be given to children is calculated according to the child's weight. When the calculated dose is something other than the amount present in one or more intact solid dosage forms, the solid dosage form must be divided to provide the correct dose. This leads to inaccurate dosing when solid dosages forms, such as tablets, are compounded to prepare other formulations for children. For amlodipine, one solution to overcoming the use of the tablet form is for a compounding pharmacist to pulverize and crush the amlodipine tablet(s) into a powder via mortar and pestle and reconstitute the powder in some liquid form. However, forming a amlodipine oral liquid in this fashion has significant drawbacks including large variability in the actual dosage, incomplete solubilizing of the amlodipine tablet in the liquid, rapid instability, inconsistent formulation methods per compounding pharmacy, and a number of other potential issues. The crushed tablet liquid formulation may also be potentially unsafe due to contamination with residual drugs and other substances from the mortar and pestle or other crushing agent. The present embodiments described herein provide a safe and effective oral administration of amlodipine for the treatment of hypertension and other disorders. In particular, the embodiments provide stable amlodipine oral liquid formulations. As used herein, “amlodipine” refers to amlodipine base, its salt, or solvate or derivative or isomer or polymorph thereof. Suitable compounds include the free base, the organic and inorganic salts, isomers, isomer salts, solvates, polymorphs, complexes etc. U.S. Pat. No. 4,572,909, U.S. Pat. No. 4,879,303, U.S. Pat. No. 6,846,931 and WO2002/053134 disclose amlodipine and exemplary amlodipine salt forms. In some embodiments, the amlodipine used in the formulations described herein is a pharmaceutically acceptable amlodipine salt. In some instances, the amlodipine salt is amlodipine benzoate. In other instances, the amlodipine salt is in the form of amlodipine naphthalene sulfonate. Amlodipine Oral Liquid Formulations Oral liquids include, but are not limited to, solutions (both aqueous and nonaqueous), suspensions, emulsions, syrups, slurries, juices, elixirs, dispersions, and the like. It is envisioned that solution/suspensions are also included where certain components described herein are in a solution while other components are in a suspension. In some embodiments, the oral liquid formulation is a suspension. In one aspect, the amlodipine liquid formulations described herein comprise a pharmaceutically acceptable salt of amlodipine, a buffer, water, and optionally one or more agents selected from the group consisting of preservatives, flavoring agents, sweetening agents, surfactants, suspension aids, and antifoaming agents. In one embodiment, the buffer is a citrate buffer. In one embodiment, the buffer comprises citric acid. In some embodiments, the buffer further comprises sodium citrate. In one embodiment, the buffer is a phosphate buffer. In one embodiment, the optional sweetening agent is sucralose. In one embodiment, the optional sweetening agent is a combination of sucralose and maltodextrin. In one embodiment, the optional sweetening agent is not maltitol. In another embodiment, the optional sweetening agent is not sucrose. In another embodiment, the optional preservative is sodium benzoate. In some embodiments, the optional preservative is a paraben. In some embodiments, the optional preservative is a mixture of parabens. In one embodiment, the optional surfactant is a polysorbate. In some embodiments, the optional surfactant is polysorbate 80. In one embodiment, the optional suspension aid is silicon dioxide. In some embodiments, the silicon dioxide is colloidal silicon dioxide. In some embodiments, the optional suspension aid is hydroxypropyl methylcellulose. In some embodiments, the optional suspension aid is a combination of hydroxypropyl methylcellulose and silicon dioxide. In some embodiments, the optional suspension aid is polyvinylpyrrolidone. In some embodiments, the optional suspension aid is methyl cellulose. In one embodiment, the optional antifoaming agent is simethicone. Pharmaceutically Acceptable Salt of Amlodipine in the Oral Liquid Formulations Disclosed herein is a stable amlodipine oral liquid formulation. In some embodiments, the stable amlodipine oral liquid formulation is in the form of a suspension. In some embodiments, the stable amlodipine oral liquid formulation comprises a pharmaceutically acceptable salt of amlodipine which is not soluble in an aqueous media. In some embodiments, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments, amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments, amlodipine benzoate or amlodipine naphthalene sulfonate are formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate or amlodipine naphthalene sulfonate with a molar excess of a salt forming agent. In some embodiments, the pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate or amlodipine naphthalene sulfonate is selected from the group consisting of amlodipine besylate, amlodipine tosylate, amlodipine mesylate, amlodipine succinate, amlodipine salicylate, amlodipine maleate, amlodipine acetate, and amlodipine hydrochloride. In some embodiments, the pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate or amlodipine naphthalene sulfonate is amlodipine besylate. In some embodiments, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate and is formed in situ by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate with a benzoate salt forming agent. In some embodiments, the benzoate salt forming agent is benzoic acid, sodium benzoate, calcium benzoate, or potassium benzoate. In some embodiments, an excess of the benzoate salt forming agent is used to form the benzoate salt in situ. In some embodiments, the benzoate salt forming agent is sodium benzoate. In some embodiments, an excess of sodium benzoate is used to form the benzoate salt in situ. In some embodiments, the amount of sodium benzoate used as the salt forming agent is about 1.0 mg/ml to about 10.0 mg/ml. In some embodiments, the amount of sodium benzoate used as the salt forming agent is about 1.0 mg/ml, about 1.1 mg/ml, about 1.2 mg/ml, about 1.3 mg/ml, about 1.4 mg/ml, about 1.5 mg/ml, about 1.6 mg/ml, about 1.7 mg/ml, about 1.8 mg/ml, about 1.9 mg/ml, about 2.0 mg/ml, about 2.1 mg/ml, about 2.2 mg/ml, about 2.3 mg/ml, about 2.4 mg/ml, about 2.5 mg/ml, about 2.6 mg/ml, about 2.7 mg/ml, about 2.8 mg/ml, about 2.9 mg/ml, about 3.0 mg/ml, about 3.1 mg/ml, about 3.2 mg/ml, about 3.3 mg/ml, about 3.4 mg/ml, about 3.5 mg/ml, about 3.6 mg/ml, about 3.7 mg/ml, about 3.8 mg/ml, about 3.9 mg/ml, about 4.0 mg/ml, about 4.1 mg/ml, about 4.2 mg/ml, about 4.3 mg/ml, about 4.4 mg/ml, about 4.5 mg/ml, about 4.6 mg/ml, about 4.7 mg/ml, about 4.8 mg/ml, about 4.9 mg/ml, about 5.0 mg/ml, about 5.1 mg/ml, about 5.2 mg/ml, about 5.3 mg/ml, about 5.4 mg/ml, about 5.5 mg/ml, about 5.6 mg/ml, about 5.7 mg/ml, about 5.8 mg/ml, about 5.9 mg/ml, about 6.0 mg/ml, about 6.1 mg/ml, about 6.2 mg/ml, about 6.3 mg/ml, about 6.4 mg/ml, about 6.5 mg/ml, about 6.6 mg/ml, about 6.7 mg/ml, about 6.8 mg/ml, about 6.9 mg/ml, about 7.0 mg/ml, about 7.1 mg/ml, about 7.2 mg/ml, about 7.3 mg/ml, about 7.4 mg/ml, about 7.5 mg/ml, about 7.6 mg/ml, about 7.7 mg/ml, about 7.8 mg/ml, about 7.9 mg/ml, about 8.0 mg/ml, about 8.1 mg/ml, about 8.2 mg/ml, about 8.3 mg/ml, about 8.4 mg/ml, about 8.5 mg/ml, about 8.6 mg/ml, about 8.7 mg/ml, about 8.8 mg/ml, about 8.9 mg/ml, about 9.0 mg/ml, about 9.1 mg/ml, about 9.2 mg/ml, about 9.3 mg/ml, about 9.4 mg/ml, about 9.5 mg/ml, about 9.6 mg/ml, about 9.7 mg/ml, about 9.8 mg/ml, about 9.9 mg/ml, or about 10.0 mg/ml. In some embodiments, the pharmaceutically acceptable salt of amlodipine is amlodipine naphthalene sulfonate and is formed in situ by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine naphthalene sulfonate with a naphthalene sulfonate salt forming agent. In some embodiments, the naphthalene sulfonate salt forming agent is 1-naphthalene sulfonic acid, 2-naphthalene sulfonic acid, sodium naphthalene-1-sulfonate, sodium naphthalene-2-sulfonate, or potassium naphthalene-2-sulfonate. In some embodiments, an excess of the naphthalene sulfonate salt forming agent is used to form the naphthalene sulfonate salt in situ. In some embodiments, the naphthalene sulfonate salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments, an excess of sodium naphthalene-2-sulfonate is used to form the naphthalene sulfonate salt in situ. In some embodiments, the amount of sodium naphthalene-2-sulfonate used as the salt forming agent is about 0.5 mg/ml to about 2.5 mg/ml. In some embodiments, the amount of sodium naphthalene-2-sulfonate used as the salt forming agent is about 0.5 mg/ml, about 0.6 mg/ml, about 0.7 mg/ml, about 0.8 mg/ml, about 0.9 mg/ml, about 1.0 mg/ml, about 1.1 mg/ml, about 1.2 mg/ml, about 1.3 mg/ml, about 1.4 mg/ml, about 1.5 mg/ml, about 1.6 mg/ml, about 1.7 mg/ml, about 1.8 mg/ml, about 1.9 mg/ml, about 2.0 mg/ml, about 2.1 mg/ml, about 2.2 mg/ml, about 2.3 mg/ml, about 2.4 mg/ml, or about 2.5 mg/ml. In some embodiments, the amount of the pharmaceutically acceptable salt of amlodipine in the oral liquid formulation corresponds to about 0.8 mg/ml to about 1.2 mg/ml of amlodipine free base. In other embodiments, the amount of the pharmaceutically acceptable salt of amlodipine in the oral liquid formulation correspond to about 0.8 mg/ml, about 0.81 mg/ml, about 0.82 mg/ml, about 0.83 mg/ml, about 0.84 mg/ml, about 0.85 mg/ml, about 0.86 mg/ml, about 0.87 mg/ml, about 0.88 mg/ml, about 0.89 mg/ml, about 0.9 mg/ml, about 0.91 mg/ml, about 0.92 mg/ml, about 0.93 mg/ml, about 0.94 mg/ml, about 0.95 mg/ml, about 0.96 mg/ml, about 0.97 mg/ml, about 0.98 mg/ml, about 0.99 mg/ml, about 1.0 mg/ml, about 1.01 mg/ml, about 1.02, mg/ml, about 1.03 mg/ml, about 1.04 mg/ml, about 1.05 mg/ml, about 1.06 mg/ml, about 1.07 mg/ml, about 1.08 mg/ml, about 1.09 mg/ml, about 1.1 mg/ml, about 1.11 mg/ml, about 1.12, mg/ml, about 1.13 mg/ml, about 1.14 mg/ml, about 1.15 mg/ml, about 1.16 mg/ml, about 1.17 mg/ml, about 1.18 mg/ml, about 1.19 mg/ml, or about 1.2 mg/ml of amlodipine free base. In some embodiments, the amount of the pharmaceutically acceptable salt of amlodipine in the oral liquid formulation corresponds to about 0.9 mg/ml to about 1.1 mg/ml of amlodipine free base. In some embodiments, the amount of the pharmaceutically acceptable salt of amlodipine in the oral liquid formulation corresponds to about 1.0 mg/ml of amlodipine free base. In some embodiments, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate. In some embodiments, the amount of amlodipine benzoate in the oral liquid formulation corresponds to about 1.0 mg/ml of amlodipine free base. In some embodiments, the pharmaceutically acceptable salt of amlodipine is amlodipine naphthalene sulfonate. In some embodiments, the amount of amlodipine naphthalene sulfonate in the oral liquid formulation corresponds to about 1.0 mg/ml of amlodipine free base. In some embodiments, the amount of the pharmaceutically acceptable salt of amlodipine corresponds to about 1% w/w to about 16% w/w of the solids in the oral liquid formulation. In other embodiments, the amount of the pharmaceutically acceptable salt of amlodipine correspond to about 1% w/w, about 1.1% w/w, about 1.2% w/w, about 1.3% w/w, about 1.4% w/w, about 1.5% w/w, about 1.6% w/w, about 1.7% w/w, about 1.8% w/w, about 1.9% w/w, about 2% w/w, about 2.1% w/w, about 2.2% w/w, about 2.3% w/w, about 2.4% w/w, about 2.5% w/w, about 2.6% w/w, about 2.7% w/w, about 2.8% w/w, about 2.9% w/w, about 3% w/w, about 3.1% w/w, about 3.2% w/w, about 3.3% w/w, about 3.4% w/w, about 3.5% w/w, about 3.6% w/w, about 3.7% w/w, about 3.8% w/w, about 3.9% w/w, about 4% w/w, about 4.1% w/w, about 4.2% w/w, about 4.3% w/w, about 4.4% w/w, about 4.5% w/w, about 4.6% w/w, about 4.7% w/w, about 4.8% w/w, about 4.9% w/w, about 5% w/w, about 5.1% w/w, about 5.2% w/w, about 5.3% w/w, about 5.4% w/w, about 5.5% w/w, about 5.6% w/w, about 5.7% w/w, about 5.8% w/w, about 5.9% w/w, about 6% w/w, about 6.1% w/w, about 6.2% w/w, about 6.3% w/w, about 6.4% w/w, about 6.5% w/w, about 6.6% w/w, about 6.7% w/w, about 6.8% w/w, about 6.9% w/w, about 7% w/w, about 7.1% w/w, about 7.2% w/w, about 7.3% w/w, about 7.4% w/w, about 7.5% w/w, about 7.6% w/w, about 7.7% w/w, about 7.8% w/w, about 7.9% w/w, about 8% w/w, about 8.1% w/w, about 8.2% w/w, about 8.3% w/w, about 8.4% w/w, about 8.5% w/w, about 8.6% w/w, about 8.7% w/w, about 8.8% w/w, about 8.9% w/w, about 9% w/w, about 9.1% w/w, about 9.2% w/w, about 9.3% w/w, about 9.4% w/w, about 9.5% w/w, about 9.6% w/w, about 9.7% w/w, about 9.8% w/w, about 9.9% w/w, about 10% w/w, about 10.1% w/w, about 10.2% w/w, about 10.3% w/w, about 10.4% w/w, about 10.5% w/w, about 10.6% w/w, about 10.7% w/w, about 10.8% w/w, about 10.9% w/w, about 11% w/w, about 11.1% w/w, about 11.2% w/w, about 11.3% w/w, about 11.4% w/w, about 11.5% w/w, about 11.6% w/w, about 11.7% w/w, about 11.8% w/w, about 11.9% w/w, about 12% w/w, about 12.1% w/w, about 12.2% w/w, about 12.3% w/w, about 12.4% w/w, about 12.5% w/w, about 12.6% w/w, about 12.7% w/w, about 12.8% w/w, about 12.9% w/w, about 13% w/w, about 13.1% w/w, about 13.2% w/w, about 13.3% w/w, about 13.4% w/w, about 13.5% w/w, about 13.6% w/w, about 13.7% w/w, about 13.8% w/w, about 13.9% w/w, about 14% w/w, about 14.1% w/w, about 14.2% w/w, about 14.3% w/w, about 14.4% w/w, about 14.5% w/w, about 14.6% w/w, about 14.7% w/w, about 14.8% w/w, about 14.9% w/w, about 15% w/w, about 15.1% w/w, about 15.2% w/w, about 15.3% w/w, about 15.4% w/w, about 15.5% w/w, about 15.6% w/w, about 15.7% w/w, about 15.8% w/w, about 15.9% w/w, or about 16% w/w of the solids in the oral liquid formulation. Sweetener in the Amlodipine Oral Liquid Formulations Sweeteners or sweetening agents include any compounds that provide a sweet taste. This includes natural and synthetic sugars, natural and artificial sweeteners, natural extracts and any material that initiates a sweet sensation in a subject. In some embodiments, a solid/powder sweetener is used in the oral liquid formulation described herein. In other embodiments, a liquid sweetening agent is used in the oral liquid formulation described herein. Sweetening agents illustratively include glucose, fructose, sucrose, xylitol, tagatose, sucralose, maltitol, isomaltulose, Isomalt™ (hydrogenated isomaltulose), lactitol, sorbitol, erythritol, trehalose, maltodextrin, polydextrose, and the like. Other sweetening agents illustratively include glycerin, inulin, maltol, acesulfame and salts thereof, e.g., acesulfame potassium, alitame, aspartame, neotame, sodium cyclamate, saccharin and salts thereof, e.g., saccharin sodium or saccharin calcium, neohesperidin dihydrochalcone, stevioside, thaumatin, and the like. Sweetening agents can be used in the form of crude or refined products such as hydrogenated starch hydrolysates, maltitol syrup, high fructose corn syrup, etc., and as branded products, e.g., Sweet Am™ liquid (propylene glycol, ethyl alcohol, and proprietary artificial flavor combination, Flavors of North America), Sweet Am™ powder (Product Code 918.005—maltodextrin, sorbitol, and fructose combination and Product Code 918.010—water, propylene glycol, sorbitol, fructose, and proprietary natural and artificial flavor combination, Flavors of North America), ProSweet™ (1-10% proprietary plant/vegetable extract and 90-99% dextrose combination, Virginia Dare), Maltisweet™ (maltitol solution, Ingredion), Sorbo™ (sorbitol and sorbitol/xylitol solution, SPI Polyols), Invertose™ (high fructose corn syrup, Ingredion), Rebalance M60 and X60 (sucralose and maltodextrin, Tate and Lyle), and Ora-Sweet® and Ora-Sweet-SF®, sugar containing and sugar-free, respectively flavored syrups (Paddock Laboratories, Inc.). Sweetening agents can be used singly or in combinations of two or more. Suitable concentrations of different sweetening agents can be selected based on published information, manufacturers' data sheets and by routine testing. In some embodiments, the amlodipine oral liquid formulation described herein comprises a sweetening agent. In some embodiments, the sweetening agent is sucralose. In some embodiments, the sweetening agent is a combination of sucralose and maltodextrin. In some embodiments, the sweetener is not maltitol. In some embodiments, the sweetener is not sucrose. In some embodiments, the sweetening agent is present in about 0.5 mg/ml to about 0.9 mg/ml in the oral liquid formulation. In other embodiments, the sweetening agent is present in about 0.51 mg/ml, about 0.52 mg/ml, about 0.53 mg/ml, about 0.54 mg/ml, about 0.55 mg/ml, about 0.56 mg/ml, about 0.57 mg/ml, about 0.58 mg/ml, about 0.59 mg/ml, about 0.60 mg/ml, about 0.61 mg/ml, about 0.62 mg/ml, about 0.63 mg/ml, about 0.64 mg/ml, about 0.65 mg/ml, about 0.66 mg/ml, about 0.67 mg/ml, about 0.68 mg/ml, about 0.69 mg/ml, about 0.70 mg/ml, about 0.71 mg/ml, about 0.72 mg/ml, about 0.73 mg/ml, about 0.74 mg/ml, about 0.75 mg/ml, about 0.76 mg/ml, about 0.77 mg/ml, about 0.78 mg/ml, about 0.79 mg/ml, about 0.80 mg/ml, about 0.81 mg/ml, about 0.82 mg/ml, about 0.83 mg/ml, about 0.84 mg/ml, about 0.85 mg/ml, about 0.86 mg/ml, about 0.87 mg/ml, about 0.88 mg/ml, about 0.89 mg/ml, or about 0.90 mg/ml in the oral liquid formulation. In some embodiments, the sweetening agent is present in about 0.6 mg/ml to about 0.8 mg/ml in the oral liquid formulation. In some embodiments, the sweetening agent is sucralose and is present in about 0.7 mg/ml in the oral liquid formulation. In some embodiments, the sweetening agent is present in about 1% w/w to about 10% w/w of the solids in the oral liquid formulation. In some embodiments, the sweetening agent is present in about 1% w/w, about 1.1% w/w, about 1.2% w/w, about 1.3% w/w, about 1.4% w/w, about 1.5% w/w, about 1.6% w/w, about 1.7% w/w, about 1.8% w/w, about 1.9% w/w, about 2% w/w, about 2.1% w/w, about 2.2% w/w, about 2.3% w/w, about 2.4% w/w, about 2.5% w/w, about 2.6% w/w, about 2.7% w/w, about 2.8% w/w, about 2.9% w/w, about 3% w/w, about 3.1% w/w, about 3.2% w/w, about 3.3% w/w, about 3.4% w/w, about 3.5% w/w, about 3.6% w/w, about 3.7% w/w, about 3.8% w/w, about 3.9% w/w, about 4% w/w, about 4.1% w/w, about 4.2% w/w, about 4.3% w/w, about 4.4% w/w, about 4.5% w/w, about 4.6% w/w, about 4.7% w/w, about 4.8% w/w, about 4.9% w/w, about 5% w/w, about 5.1% w/w, about 5.2% w/w, about 5.3% w/w, about 5.4% w/w, about 5.5% w/w, about 5.6% w/w, about 5.7% w/w, about 5.8% w/w, about 5.9% w/w, about 6% w/w, about 6.1% w/w, about 6.2% w/w, about 6.3% w/w, about 6.4% w/w, about 6.5% w/w, about 6.6% w/w, about 6.7% w/w, about 6.8% w/w, about 6.9% w/w, about 7% w/w, about 7.1% w/w, about 7.2% w/w, about 7.3% w/w, about 7.4% w/w, about 7.5% w/w, about 7.6% w/w, about 7.7% w/w, about 7.8% w/w, about 7.9% w/w, about 8% w/w, about 8.1% w/w, about 8.2% w/w, about 8.3% w/w, about 8.4% w/w, about 8.5% w/w, about 8.6% w/w, about 8.7% w/w, about 8.8% w/w, about 8.9% w/w, about 9% w/w, about 9.1% w/w, about 9.2% w/w, about 9.3% w/w, about 9.4% w/w, about 9.5% w/w, about 9.6% w/w, about 9.7% w/w, about 9.8% w/w, about 9.9% w/w, or about 10% w/w of the solids in the oral liquid formulation. Preservative in the Amlodipine Oral Liquid Formulations Preservatives include anti-microbials, anti-oxidants, and agents that enhance sterility. Exemplary preservatives include ascorbic acid, ascorbyl palmitate, BHA, BHT, citric acid, EDTA and its salts, erythorbic acid, fumaric acid, malic acid, propyl gallate, sodium ascorbate, sodium bisulfate, sodium metabisulfite, sodium sulfite, parabens (such as methylparaben, ethylparaben, propylparaben, butylparaben and their salts), benzoic acid, sodium benzoate, potassium sorbate, vanillin, and the like. In some embodiments, the amlodipine oral liquid formulation described herein comprises a preservative. In some embodiments, the preservative is a paraben, or a mixture of parabens and the sweetener is a sugar (such as, but not limited to glucose, fructose, sucrose, lactose, maltose) or a sugar alcohol (such as, but not limited to xylitol, mannitol, lactitol, maltitol, sorbitol). In some embodiments, the preservative is a paraben, or a mixture of parabens and the sweetener is not a sugar or a sugar alcohol. In some embodiments, the preservative is present in an amount sufficient to provide antimicrobial effectiveness to the amlodipine oral liquid formulation described herein. In some embodiments, the amount of preservative sufficient to provide antimicrobial effectiveness is between about 0.1 mg/ml and about 2.0 mg/ml. In other embodiments, the amount of preservative sufficient to provide antimicrobial effectiveness is about 0.1 mg/ml, about 0.11 mg/ml, about 0.12 mg/ml, about 0.13 mg/ml, about 0.14 mg/ml, about 0.15 mg/ml, about 0.16 mg/ml, about 0.17 mg/ml, about 0.18 mg/ml, about 0.19 mg/ml, about 0.2 mg/ml, about 0.21 mg/ml, about 0.22 mg/ml, about 0.23 mg/ml, about 0.24 mg/ml, about 0.25 mg/ml, about 0.26 mg/ml, about 0.27 mg/ml, about 0.28 mg/ml, about 0.29 mg/ml, about 0.3 mg/ml, about 0.31 mg/ml, about 0.32 mg/ml, about 0.33 mg/ml, about 0.34 mg/ml, about 0.35 mg/ml, about 0.36 mg/ml, about 0.37 mg/ml, about 0.38 mg/ml, about 0.39 mg/ml, about 0.4 mg/ml, about 0.41 mg/ml, about 0.42 mg/ml, about 0.43 mg/ml, about 0.44 mg/ml, about 0.45 mg/ml, about 0.46 mg/ml, about 0.47 mg/ml, about 0.48 mg/ml, about 0.49 mg/ml, about 0.5 mg/ml, about 0.51 mg/ml, about 0.52 mg/ml, about 0.53 mg/ml, about 0.54 mg/ml, about 0.55 mg/ml, about 0.56 mg/ml, about 0.57 mg/ml, about 0.58 mg/ml, about 0.59 mg/ml, about 0.6 mg/ml, about 0.61 mg/ml, about 0.62 mg/ml, about 0.63 mg/ml, about 0.64 mg/ml, about 0.65 mg/ml, about 0.66 mg/ml, about 0.67 mg/ml, about 0.68 mg/ml, about 0.69 mg/ml, about 0.7 mg/ml, about 0.71 mg/ml, about 0.72 mg/ml, about 0.73 mg/ml, about 0.74 mg/ml, about 0.75 mg/ml, about 0.76 mg/ml, about 0.77 mg/ml, about 0.78 mg/ml, about 0.79 mg/ml, about 0.8 mg/ml, about 0.81 mg/ml, about 0.82 mg/ml, about 0.83 mg/ml, about 0.84 mg/ml, about 0.85 mg/ml, about 0.86 mg/ml, about 0.87 mg/ml, about 0.88 mg/ml, about 0.89 mg/ml, about 0.9 mg/ml, about 0.91 mg/ml, about 0.92 mg/ml, about 0.93 mg/ml, about 0.94 mg/ml, about 0.95 mg/ml, about 0.96 mg/ml, about 0.97 mg/ml, about 0.98 mg/ml, about 0.99 mg/ml, about 1.0 mg/ml, about 1.1 mg/ml, about 1.2 mg/ml, about 1.3 mg/ml, about 1.4 mg/ml, about 1.5 mg/ml, about 1.6 mg/ml, about 1.7 mg/ml, about 1.8 mg/ml, about 1.9 mg/ml, or about 2.0 mg/ml. In some embodiments, the preservative is sodium benzoate and the amount of sodium benzoate sufficient to provide antimicrobial effectiveness is between about 0.2 mg/ml and about 1.0 mg/ml. In some embodiments, the preservative is methyl paraben and the amount of methyl paraben sufficient to provide antimicrobial effectiveness is between about 1.0 mg/ml and about 2.0 mg/ml. In some embodiments, the preservative is propyl paraben and the amount of propyl paraben sufficient to provide antimicrobial effectiveness is between about 0.1 mg/ml and about 0.2 mg/ml. In some embodiments, the preservative is present in about 0.5% w/w to about 15% w/w of the solids in the oral liquid formulation. In other embodiments, the preservative is present in about 0.5% w/w, about 1% w/w, about 1.5% w/w, about 2% w/w, about 2.5% w/w, about 3% w/w, about 3.5% w/w, about 4% w/w, about 4.5% w/w, about 5% w/w, about 5.5% w/w, about 6% w/w, about 6.5% w/w, about 7% w/w, about 7.5% w/w, about 8% w/w, about 8.5% w/w, about 9% w/w, about 9.5% w/w, about 10% w/w, about 11% w/w, about 11.5% w/w, about 12% w/w, about 12.5% w/w, about 13% w/w, about 13.5% w/w, about 14% w/w, about 14.5% w/w, or about 15% w/w of the solids in the oral liquid formulation. Sweetener and Preservative Incompatibility Paraben preservatives (especially methylparaben) can react with selected sugars (glucose, fructose, sucrose, lactose, maltose) and sugar alcohols (xylitol, mannitol, lactitol, maltitol, sorbitol) to form transesterification reaction products. This can be undesirable from a formulation and stability standpoint as the transesterification creates additional degradants. In some embodiments, the amlodipine oral liquid formulation described herein does not comprise a paraben preservative. In further embodiments, the amlodipine oral liquid formulation described herein does not comprise a paraben preservative when the formulation also comprises a sugar or sugar alcohol. Buffers in the Amlodipine Oral Liquid Formulations Buffering agents maintain the pH of the liquid amlodipine formulation. Non-limiting examples of buffering agents include, but are not limited to sodium bicarbonate, potassium bicarbonate, magnesium hydroxide, magnesium lactate, magnesium gluconate, aluminum hydroxide, aluminum hydroxide/sodium bicarbonate co-precipitate, mixture of an amino acid and a buffer, a mixture of aluminum glycinate and a buffer, a mixture of an acid salt of an amino acid and a buffer, and a mixture of an alkali salt of an amino acid and a buffer. Additional buffering agents include citric acid, sodium citrate, sodium tartrate, sodium acetate, sodium carbonate, phosphoric acid, sodium polyphosphate, potassium polyphosphate, sodium pyrophosphate, potassium pyrophosphate, disodium hydrogenphosphate, dipotassium hydrogenphosphate, trisodium phosphate, tripotassium phosphate, sodium acetate, potassium metaphosphate, magnesium oxide, magnesium hydroxide, magnesium carbonate, magnesium silicate, calcium acetate, calcium glycerophosphate, calcium chloride, calcium hydroxide, calcium lactate, calcium carbonate, calcium bicarbonate, and other calcium salts. In some embodiments, the oral liquid formulation comprises a buffer. In some embodiments, the oral liquid formulation comprises a citrate buffer. In some embodiments, the buffer in the amlodipine oral liquid formulation described herein comprises citric acid. In some embodiments, the buffer in the amlodipine oral liquid formulation described herein comprises citric acid and sodium citrate. In some embodiments, the sodium citrate is monosodium citrate. In some embodiments, the sodium citrate is disodium citrate. In some embodiments, the sodium citrate is trisodium citrate. In some embodiments, the oral liquid formulation comprises a phosphate buffer. In some embodiments, the buffer in the amlodipine oral liquid formulation described herein comprises phosphoric acid. In some embodiments, the buffer in the amlodipine oral liquid formulation described herein comprises phosphoric acid and sodium phosphate. In some embodiments, the buffer in the amlodipine oral liquid formulation described herein comprises sodium phosphate. In some embodiments, the sodium phosphate is sodium dihydrogen phosphate. In some embodiments, the sodium phosphate is sodium hydrogenphosphate. In some embodiments, the sodium phosphate is trisodium phosphate. In some embodiments, the pH of the amlodipine oral liquid formulation described herein is between about 3 and about 8. In some embodiments, the pH of the amlodipine oral liquid formulation described herein is between about 4 and about 5. In some embodiments, the pH of the amlodipine oral liquid formulation described herein is between about 5 and about 6. In some embodiments, the pH of the amlodipine oral liquid formulation described herein is less than about 4, less than about 4.5, less than about 5, less than about 5.5, less than about 6, less than about 6.5, less than about 7, less than about 7.5, or less than about 8. In some embodiments, the pH of the amlodipine oral liquid formulation described herein is about 3, about 3.1, about 3.2, about 3.3, about 3.4, about 3.5, about 3.6, about 3.7, about 3.8, about 3.9, about 4, about 4.1, about 4.2, about 4.3, about 4.4, about 4.5, about 4.6, about 4.7, about 4.8, about 4.9, about 5, about 5.1, about 5.2, about 5.3, about 5.4, about 5.5, about 5.6, about 5.7, about 5.8, about 5.9, about 6, about 6.1, about 6.2, about 6.3, about 6.4, about 6.5, about 6.6, about 6.7, about 6.8, about 6.9, about 7, about 7.1, about 7.2, about 7.3, about 7.4, about 7.5, about 7.6, about 7.7, about 7.8, about 7.9, or about 8. In some embodiments, the buffer concentration is between about 1 mM and about 60 mM. In some embodiments, the buffer concentration is about 1 mM, about 1.5 mM, about 2 mM, about 2.5 mM, about 3 mM, about 3.5 mM, about 4 mM, about 4.5 mM, about 5 mM, about 5.5 mM, about 6 mM, about 6.5 mM, about 7 mM, about 7.5 mM, about 8 mM, about 8.5 mM, about 9 mM, about 9.5 mM, about 10 mM, about 10.5 mM, about 11 mM, about 11.5 mM, about 12 mM, about 12.5 mM, about 13 mM, about 13.5 mM, about 14 mM, about 14.5 mM, about 15 mM, about 15.5 mM, about 16 mM, about 16.5 mM, about 17 mM, about 17.5 mM, about 18 mM, about 18.5 mM, about 19 mM, about 19.5 mM, about 20 mM, about 20.5 mM, about 21 mM, about 21.5 mM, about 22 mM, about 22.5 mM, about 23 mM, about 23.5 mM, about 24 mM, about 24.5 mM, about 25 mM, about 25.5 mM, about 26 mM, about 26.5 mM, about 27 mM, about 27.5 mM, about 28 mM, about 28.5 mM, about 29 mM, about 29.5 mM, about 30 mM, about 30.5 mM, about 31 mM, about 31.5 mM, about 32 mM, about 32.5 mM, about 33 mM, about 33.5 mM, about 34 mM, about 34.5 mM, about 35 mM, about 35.5 mM, about 36 mM, about 36.5 mM, about 37 mM, about 37.5 mM, about 38 mM, about 38.5 mM, about 39 mM, about 39.5 mM, about 40 mM, about 40.5 mM, about 41 mM, about 41.5 mM, about 42 mM, about 42.5 mM, about 43 mM, about 43.5 mM, about 44 mM, about 44.5 mM, about 45 mM, about 45.5 mM, about 46 mM, about 46.5 mM, about 47 mM, about 47.5 mM, about 48 mM, about 48.5 mM, about 49 mM, about 49.5 mM, about 50 mM, about 50.5 mM, about 51 mM, about 51.5 mM, about 52 mM, about 52.5 mM, about 53 mM, about 53.5 mM, about 54 mM, about 54.5 mM, about 55 mM, about 55.5 mM, about 56 mM, about 56.5 mM, about 57 mM, about 57.5 mM, about 58 mM, about 58.5 mM, about 59 mM, about 59.5 mM, or about 60 mM. In some embodiments, the buffer concentration is between about 1 mM and about 5 mM, or about 2 mM and about 4 mM. In some embodiments, the buffer concentration is about 3 mM. In some embodiments, the buffer in the amlodipine oral liquid formulation described herein comprises citric acid. In some embodiments, citric acid is present in about 0.1 mg/ml to about 1.0 mg/ml in the oral liquid formulation. In other embodiments, citric acid is present in about 0.1 mg/ml, about 0.11 mg/ml, about 0.12 mg/ml, about 0.13 mg/ml, about 0.14 mg/ml, about 0.15 mg/ml, about 0.16 mg/ml, about 0.17 mg/ml, about 0.18 mg/ml, about 0.19 mg/ml, about 0.2 mg/ml, about 0.21 mg/ml, about 0.22 mg/ml, about 0.23 mg/ml, about 0.24 mg/ml, about 0.25 mg/ml, about 0.26 mg/ml, about 0.27 mg/ml, about 0.28 mg/ml, about 0.29 mg/ml, about 0.3 mg/ml, about 0.31 mg/ml, about 0.32 mg/ml, about 0.33 mg/ml, about 0.34 mg/ml, about 0.35 mg/ml, about 0.36 mg/ml, about 0.37 mg/ml, about 0.38 mg/ml, about 0.39 mg/ml, about 0.4 mg/ml, about 0.41 mg/ml, about 0.42 mg/ml, about 0.43 mg/ml, about 0.44 mg/ml, about 0.45 mg/ml, about 0.46 mg/ml, about 0.47 mg/ml, about 0.48 mg/ml, about 0.49 mg/ml, about 0.5 mg/ml, about 0.51 mg/ml, about 0.52 mg/ml, about 0.53 mg/ml, about 0.54 mg/ml, about 0.55 mg/ml, about 0.56 mg/ml, about 0.57 mg/ml, about 0.58 mg/ml, about 0.59 mg/ml, about 0.6 mg/ml, about 0.61 mg/ml, about 0.62 mg/ml, about 0.63 mg/ml, about 0.64 mg/ml, about 0.65 mg/ml, about 0.66 mg/ml, about 0.67 mg/ml, about 0.68 mg/ml, about 0.69 mg/ml, about 0.7 mg/ml, about 0.71 mg/ml, about 0.72 mg/ml, about 0.73 mg/ml, about 0.74 mg/ml, about 0.75 mg/ml, about 0.76 mg/ml, about 0.77 mg/ml, about 0.78 mg/ml, about 0.79 mg/ml, about 0.8 mg/ml, about 0.81 mg/ml, about 0.82 mg/ml, about 0.83 mg/ml, about 0.84 mg/ml, about 0.85 mg/ml, about 0.86 mg/ml, about 0.87 mg/ml, about 0.88 mg/ml, about 0.89 mg/ml, about 0.9 mg/ml, about 0.91 mg/ml, about 0.92 mg/ml, about 0.93 mg/ml, about 0.94 mg/ml, about 0.95 mg/ml, about 0.96 mg/ml, about 0.97 mg/ml, about 0.98 mg/ml, about 0.99 mg/ml, or about 1.0 mg/ml in the oral liquid formulation. In one embodiment, citric acid is present in about 0.31 mg/ml in the oral liquid formulation. In some embodiments, citric acid is present in about 5.0 mg/ml to about 15 mg/ml in the oral liquid formulation. In other embodiments, citric acid is present in about 5.0 mg/ml, about 5.5 mg/ml, about 6.0 mg/ml, about 6.5 mg/ml, about 7.0 mg/ml, about 7.5 mg/ml, about 8.0 mg/ml, about 8.5 mg/ml, about 9.0 mg/ml, about 9.5 mg/ml, about 10.0 mg/ml, about 10.5 mg/ml, about 11.0 mg/ml, about 11.5 mg/ml, about 12.0 mg/ml, about 12.5 mg/ml, about 13.0 mg/ml, about 13.5 mg/ml, about 14.0 mg/ml, about 14.5 mg/ml, or about 15.0 mg/ml in the oral liquid formulation. In some embodiments, citric acid is present in about 1% w/w to about 45% w/w of the solids in the oral liquid formulation. In other embodiments, citric acid is present in about 1% w/w, about 1.1% w/w, about 1.2% w/w, about 1.3% w/w, about 1.4% w/w, about 1.5% w/w, about 1.6% w/w, about 1.7% w/w, about 1.8% w/w, about 1.9% w/w, about 2% w/w, about 2.1% w/w, about 2.2% w/w, about 2.3% w/w, about 2.4% w/w, about 2.5% w/w, about 2.6% w/w, about 2.7% w/w, about 2.8% w/w, about 2.9% w/w, about 3% w/w, about 3.1% w/w, about 3.2% w/w, about 3.3% w/w, about 3.4% w/w, about 3.5% w/w, about 3.6% w/w, about 3.7% w/w, about 3.8% w/w, about 3.9% w/w, about 4% w/w, about 4.1% w/w, about 4.2% w/w, about 4.3% w/w, about 4.4% w/w, about 4.5% w/w, about 4.6% w/w, about 4.7% w/w, about 4.8% w/w, about 4.9% w/w, about 5% w/w, about 6% w/w, about 7% w/w, about 8% w/w, about 9% w/w, about 10% w/w, about 11% w/w, about 12% w/w, about 13% w/w, about 14% w/w, about 15% w/w, about 16% w/w, about 17% w/w, about 18% w/w, about 19% w/w, about 20% w/w, about 21% w/w, about 22% w/w, about 23% w/w, about 24% w/w, about 25% w/w, about 26% w/w, about 27% w/w, about 28% w/w, about 29% w/w, about 30% w/w, about 31% w/w, about 32% w/w, about 33% w/w, about 34% w/w, about 35% w/w, about 36% w/w, about 37% w/w, about 38% w/w, about 39% w/w, about 40% w/w, about 41% w/w, about 42% w/w, about 43% w/w, about 44% w/w, or about 45% w/w of the solids in the oral liquid formulation. In some embodiments, citric acid is present in about 1% w/w to about 20% w/w of the solids in the oral liquid formulation. In some embodiments, citric acid is present in about 1% w/w to about 1.5% w/w of the solids in the oral liquid formulation. In some embodiments, the amlodipine oral liquid formulation further comprises sodium citrate. In some embodiments, sodium citrate is present in about 0.1 mg/ml to about 1.0 mg/ml in the oral liquid formulation. In other embodiments, sodium citrate is present in the oral liquid formulation is about 0.1 mg/ml, about 0.11 mg/ml, about 0.12 mg/ml, about 0.13 mg/ml, about 0.14 mg/ml, about 0.15 mg/ml, about 0.16 mg/ml, about 0.17 mg/ml, about 0.18 mg/ml, about 0.19 mg/ml, about 0.2 mg/ml, about 0.21 mg/ml, about 0.22 mg/ml, about 0.23 mg/ml, about 0.24 mg/ml, about 0.25 mg/ml, about 0.26 mg/ml, about 0.27 mg/ml, about 0.28 mg/ml, about 0.29 mg/ml, about 0.3 mg/ml, about 0.31 mg/ml, about 0.32 mg/ml, about 0.33 mg/ml, about 0.34 mg/ml, about 0.35 mg/ml, about 0.36 mg/ml, about 0.37 mg/ml, about 0.38 mg/ml, about 0.39 mg/ml, about 0.4 mg/ml, about 0.41 mg/ml, about 0.42 mg/ml, about 0.43 mg/ml, about 0.44 mg/ml, about 0.45 mg/ml, about 0.46 mg/ml, about 0.47 mg/ml, about 0.48 mg/ml, about 0.49 mg/ml, about 0.5 mg/ml, about 0.51 mg/ml, about 0.52 mg/ml, about 0.53 mg/ml, about 0.54 mg/ml, about 0.55 mg/ml, about 0.56 mg/ml, about 0.57 mg/ml, about 0.58 mg/ml, about 0.59 mg/ml, about 0.6 mg/ml, about 0.61 mg/ml, about 0.62 mg/ml, about 0.63 mg/ml, about 0.64 mg/ml, about 0.65 mg/ml, about 0.66 mg/ml, about 0.67 mg/ml, about 0.68 mg/ml, about 0.69 mg/ml, about 0.7 mg/ml, about 0.71 mg/ml, about 0.72 mg/ml, about 0.73 mg/ml, about 0.74 mg/ml, about 0.75 mg/ml, about 0.76 mg/ml, about 0.77 mg/ml, about 0.78 mg/ml, about 0.79 mg/ml, about 0.8 mg/ml, about 0.81 mg/ml, about 0.82 mg/ml, about 0.83 mg/ml, about 0.84 mg/ml, about 0.85 mg/ml, about 0.86 mg/ml, about 0.87 mg/ml, about 0.88 mg/ml, about 0.89 mg/ml, about 0.9 mg/ml, about 0.91 mg/ml, about 0.92 mg/ml, about 0.93 mg/ml, about 0.94 mg/ml, about 0.95 mg/ml, about 0.96 mg/ml, about 0.97 mg/ml, about 0.98 mg/ml, about 0.99 mg/ml, or about 1.0 mg/ml in the oral liquid formulation. In one embodiment, sodium citrate is present in about 0.36 mg/ml in the oral liquid formulation. In some embodiments, sodium citrate is present in about 1% w/w to about 20% w/w of the solids in the oral liquid formulation. In other embodiments, sodium citrate is present in about 1% w/w, about 1.1% w/w, about 1.2% w/w, about 1.3% w/w, about 1.4% w/w, about 1.5% w/w, about 1.6% w/w, about 1.7% w/w, about 1.8% w/w, about 1.9% w/w, about 2% w/w, about 2.1% w/w, about 2.2% w/w, about 2.3% w/w, about 2.4% w/w, about 2.5% w/w, about 2.6% w/w, about 2.7% w/w, about 2.8% w/w, about 2.9% w/w, about 3% w/w, about 3.1% w/w, about 3.2% w/w, about 3.3% w/w, about 3.4% w/w, about 3.5% w/w, about 3.6% w/w, about 3.7% w/w, about 3.8% w/w, about 3.9% w/w, about 4% w/w, about 4.1% w/w, about 4.2% w/w, about 4.3% w/w, about 4.4% w/w, about 4.5% w/w, about 4.6% w/w, about 4.7% w/w, about 4.8% w/w, about 4.9% w/w, about 5% w/w, about 6% w/w, about 7% w/w, about 8% w/w, about 9% w/w, about 10% w/w, about 11% w/w, about 12% w/w, about 13% w/w, about 14% w/w, about 15% w/w, about 16% w/w, about 17% w/w, about 18% w/w, about 19% w/w, or about 20% w/w of the solids in the oral liquid formulation. In some embodiments, sodium citrate is present in about 1% w/w to about 2% w/w of the solids in the oral liquid formulation. In other embodiments, sodium citrate is not added to the formulation. In some embodiments, the buffer in the amlodipine oral liquid formulation described herein comprises phosphoric acid. In some embodiments, phosphoric acid is present in about 0.1 mg/ml to about 2.0 mg/ml in the oral liquid formulation. In other embodiments, phosphoric acid is present in about 0.1 mg/ml, about 0.15 mg/ml, about 0.2 mg/ml, about 0.25 mg/ml, about 0.3 mg/ml, about 0.35 mg/ml, 0.4 mg/ml, about 0.45 mg/ml, about 0.5 mg/ml, about 0.55 mg/ml, about 0.6 mg/ml, about 0.65 mg/ml, about 0.7 mg/ml, about 0.75 mg/ml, about 0.8 mg/ml, about 0.85 mg/ml, about 0.9 mg/ml, about 0.95 mg/ml, about 1.0 mg/ml, about 1.1 mg/ml, about 1.15 mg/ml, about 1.2 mg/ml, about 1.25 mg/ml, about 1.3 mg/ml, about 1.35 mg/ml, about 1.4 mg/ml, about 1.45 mg/ml, about 1.5 mg/ml, about 1.55 mg/ml, about 1.6 mg/mL, about 1.65 mg/mL, about 1.7 mg/ml, about 1.75 mg/ml, about 1.8 mg/ml, about 1.85 mg/ml, about 1.9 mg/ml, about 1.95 mg/ml, or about 2.0 mg/ml in the oral liquid formulation. In some embodiments, phosphoric acid is present in about 1% w/w to about 10% w/w of the solids in the oral liquid formulation. In other embodiments, citric acid is present in about 1% w/w, about 1.1% w/w, about 1.2% w/w, about 1.3% w/w, about 1.4% w/w, about 1.5% w/w, about 1.6% w/w, about 1.7% w/w, about 1.8% w/w, about 1.9% w/w, about 2% w/w, about 2.1% w/w, about 2.2% w/w, about 2.3% w/w, about 2.4% w/w, about 2.5% w/w, about 2.6% w/w, about 2.7% w/w, about 2.8% w/w, about 2.9% w/w, about 3% w/w, about 3.1% w/w, about 3.2% w/w, about 3.3% w/w, about 3.4% w/w, about 3.5% w/w, about 3.6% w/w, about 3.7% w/w, about 3.8% w/w, about 3.9% w/w, about 4% w/w, about 4.1% w/w, about 4.2% w/w, about 4.3% w/w, about 4.4% w/w, about 4.5% w/w, about 4.6% w/w, about 4.7% w/w, about 4.8% w/w, about 4.9% w/w, about 5% w/w, about 5.1% w/w, about 5.2% w/w, about 5.3% w/w, about 5.4% w/w, about 5.5% w/w, about 5.6% w/w, about 5.7% w/w, about 5.8% w/w, about 5.9% w/w, about 6% w/w, about 6.1% w/w, about 6.2% w/w, about 6.3% w/w, about 6.4% w/w, about 6.5% w/w, about 6.6% w/w, about 6.7% w/w, about 6.8% w/w, about 6.9% w/w, about 7% w/w, about 7.1% w/w, about 7.2% w/w, about 7.3% w/w, about 7.4% w/w, about 7.5% w/w, about 7.6% w/w, about 7.7% w/w, about 7.8% w/w, about 7.9% w/w, about 8% w/w, about 8.1% w/w, about 8.2% w/w, about 8.3% w/w, about 8.4% w/w, about 8.5% w/w, about 8.6% w/w, about 8.7% w/w, about 8.8% w/w, about 8.9% w/w, about 9% w/w, about 9.1% w/w, about 9.2% w/w, about 9.3% w/w, about 9.4% w/w, about 9.5% w/w, about 9.6% w/w, about 9.7% w/w, about 9.8% w/w, about 9.9% w/w, or about 10% w/w of the solids in the oral liquid formulation. In some embodiments, the buffer in the amlodipine oral liquid formulation described herein comprises sodium hydrogenphosphate. In some embodiments, sodium hydrogenphosphate is present in about 0.1 mg/ml to about 1.0 mg/ml in the oral liquid formulation. In other embodiments, sodium hydrogenphosphate is present in the oral liquid formulation is about 0.1 mg/mL, about 0.11 mg/ml, about 0.12 mg/ml, about 0.13 mg/ml, about 0.14 mg/ml, about 0.15 mg/ml, about 0.16 mg/ml, about 0.17 mg/ml, about 0.18 mg/ml, about 0.19 mg/ml, about 0.2 mg/ml, about 0.21 mg/ml, about 0.22 mg/ml, about 0.23 mg/ml, about 0.24 mg/ml, about 0.25 mg/ml, about 0.26 mg/ml, about 0.27 mg/ml, about 0.28 mg/ml, about 0.29 mg/ml, about 0.3 mg/ml, about 0.31 mg/ml, about 0.32 mg/ml, about 0.33 mg/ml, about 0.34 mg/ml, about 0.35 mg/ml, about 0.36 mg/ml, about 0.37 mg/ml, about 0.38 mg/ml, about 0.39 mg/ml, about 0.4 mg/ml, about 0.41 mg/ml, about 0.42 mg/ml, about 0.43 mg/ml, about 0.44 mg/ml, about 0.45 mg/ml, about 0.46 mg/ml, about 0.47 mg/ml, about 0.48 mg/ml, about 0.49 mg/ml, about 0.5 mg/ml, about 0.51 mg/ml, about 0.52 mg/ml, about 0.53 mg/ml, about 0.54 mg/ml, about 0.55 mg/ml, about 0.56 mg/ml, about 0.57 mg/ml, about 0.58 mg/ml, about 0.59 mg/ml, about 0.6 mg/ml, about 0.61 mg/ml, about 0.62 mg/ml, about 0.63 mg/ml, about 0.64 mg/ml, about 0.65 mg/ml, about 0.66 mg/ml, about 0.67 mg/ml, about 0.68 mg/ml, about 0.69 mg/ml, about 0.7 mg/ml, about 0.71 mg/ml, about 0.72 mg/ml, about 0.73 mg/ml, about 0.74 mg/ml, about 0.75 mg/ml, about 0.76 mg/ml, about 0.77 mg/ml, about 0.78 mg/ml, about 0.79 mg/ml, about 0.8 mg/ml, about 0.81 mg/ml, about 0.82 mg/ml, about 0.83 mg/ml, about 0.84 mg/ml, about 0.85 mg/ml, about 0.86 mg/ml, about 0.87 mg/ml, about 0.88 mg/ml, about 0.89 mg/ml, about 0.9 mg/ml, about 0.91 mg/ml, about 0.92 mg/ml, about 0.93 mg/ml, about 0.94 mg/ml, about 0.95 mg/ml, about 0.96 mg/ml, about 0.97 mg/ml, about 0.98 mg/ml, about 0.99 mg/ml, or about 1.0 mg/ml in the oral liquid formulation. In some embodiments, sodium hydrogenphosphate is present in about 0.5% w/w to about 5% w/w of the solids in the oral liquid formulation. In other embodiments, sodium hydrogenphosphate is present in about 0.5% w/w, about 0.6% w/w, about 0.7% w/w, about 0.8% w/w, about 0.9% w/w, about 1% w/w, about 1.1% w/w, about 1.2% w/w, about 1.3% w/w, about 1.4% w/w, about 1.5% w/w, about 1.6% w/w, about 1.7% w/w, about 1.8% w/w, about 1.9% w/w, about 2% w/w, about 2.1% w/w, about 2.2% w/w, about 2.3% w/w, about 2.4% w/w, about 2.5% w/w, about 2.6% w/w, about 2.7% w/w, about 2.8% w/w, about 2.9% w/w, about 3% w/w, about 3.1% w/w, about 3.2% w/w, about 3.3% w/w, about 3.4% w/w, about 3.5% w/w, about 3.6% w/w, about 3.7% w/w, about 3.8% w/w, about 3.9% w/w, about 4% w/w, about 4.1% w/w, about 4.2% w/w, about 4.3% w/w, about 4.4% w/w, about 4.5% w/w, about 4.6% w/w, about 4.7% w/w, about 4.8% w/w, about 4.9% w/w, or about 5% w/w of the solids in the oral liquid formulation. Suspension Aid in the Amlodipine Oral Liquid Formulations A suspension aid or dispersion aid is used to prevent the settling of the pharmaceutically acceptable salt of amlodipine in the oral liquid formulation. Suitable suspension aids include but not limited to polymers such as 3-butoxy-2-hydroxypropylhydroxyethylcellulose, acrylamide homo- and copolymers, acrylic acid homo- and copolymer, alginates, carboxymethylcellulose (sodium and other salts), carboxymethylhydroxyethylcellulose, carboxy-vinyl copolymers, cellulose, such as microcrystalline cellulose, combinations of microcrystalline cellulose with carboxymethylcellulose sodium (such as Avicel RC-501, RC-581, RC-591, and CL-611), hydrophobically modified hydroxyethylcellulose, hydroxyethylcellulose, hydroxypropyl guar, hydroxypropyl methylcellulose (such as Benecel K750 ® or Benecel K1500®), hydroxypropylcellulose, methyl cellulose, natural gums and their derivatives, xanthan gum, guar gum, gum Arabic, partially and fully hydrolyzed polyvinyl alcohols, partially neutralized polyacrylic acid, polyalkylene glycol, polysaccharide gums, polyvinylpyrrolidone and derivatives thereof, starch and its derivatives, vinylpyrrolidone homo- and copolymers, water-soluble cellulose ethers, and the mixtures thereof. Other suitable suspension aids include silicon dioxide, silica powder prepared by precipitating water glass (sodium silicate) with sulfuric acid, which is then dried and sold as a fine powder, fumed alumina (made of primary particles which sinter together to form aggregates), clays such as bentonite, laponites, kaolinite, dickite, and nacrite, pyrophylite, talc, vermiculite, sauconite, saponte, nontronite, and montmorillonite, and organically modified montmorillonite clays. In some embodiments, the suspension aid comprises silicon dioxide. In some embodiment, the silicon dioxide is colloidal silicon dioxide. In some embodiments, the amlodipine oral liquid formulation described herein comprises a suspension aid. In some embodiments, the suspension aid comprises silicon dioxide, hydroxypropyl methylcellulose, methylcellulose, microcrystalline cellulose, polyvinylpyrrolidone, or combinations thereof. In some embodiments, the suspension aid is silicon dioxide. In some embodiments, the suspension aid is hydroxypropyl methylcellulose. In some embodiments, the suspension aid is a combination of silicon dioxide and hydroxypropyl methylcellulose. In some embodiments, the suspension aid is polyvinylpyrrolidone. In some embodiments, the suspension aid is present in about 0.1 mg/ml to about 1.0 mg/ml in the oral liquid formulation. In other embodiments, the suspension aid is present in about 0.1 mg/ml, about 0.15 mg/ml, about 0.2 mg/ml, about 0.25 mg/ml, about 0.3 mg/ml, about 0.35 mg/ml, about 0.4 mg/ml, about 0.45 mg/ml, about 0.5 mg/ml, about 0.55 mg/ml, about 0.6 mg/ml, about 0.65 mg/ml, about 0.7 mg/ml, about 0.75 mg/ml, about 0.8 mg/ml, about 0.85 mg/ml, about 0.9 mg/ml, about 0.95 mg/ml, or about 1.0 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is present in about 0.3 mg/ml to about 0.7 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is present in about 0.4 mg/ml to about 0.6 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is silicon dioxide and is present in about 0.5 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is present in about 3.0 mg/ml to about 10.0 mg/ml in the oral liquid formulation. In other embodiments, the suspension aid is present in about 3.0 mg/ml, about 3.1 mg/ml, about 3.2 mg/ml, about 3.3 mg/ml, about 3.4 mg/ml, about 3.5 mg/ml, about 3.6 mg/ml, about 3.7 mg/ml, about 3.8 mg/ml, about 3.9 mg/ml, about 4.0 mg/ml, about 4.1 mg/ml, about 4.2 mg/ml, about 4.3 mg/ml, about 4.4 mg/ml, about 4.5 mg/ml, about 4.6 mg/ml, about 4.7 mg/ml, about 4.8 mg/ml, about 4.9 mg/ml, about 5.0 mg/ml, about 5.1 mg/ml, about 5.2 mg/ml, about 5.3 mg/ml, about 5.4 mg/ml, about 5.5 mg/ml, about 5.6 mg/ml, about 5.7 mg/ml, about 5.8 mg/ml, about 5.9 mg/ml, about 6.0 mg/ml, about 6.1 mg/ml, about 6.2 mg/ml, about 6.3 mg/ml, about 6.4 mg/ml, about 6.5 mg/ml, about 6.6 mg/ml, about 6.7 mg/ml, about 6.8 mg/ml, about 6.9 mg/ml, about 7.0 mg/ml, about 7.1 mg/ml, about 7.2 mg/ml, about 7.3 mg/ml, about 7.4 mg/ml, about 7.5 mg/ml, about 7.6 mg/ml, about 7.7 mg/ml, about 7.8 mg/ml, about 7.9 mg/ml, about 8.0 mg/ml, about 8.1 mg/ml, about 8.2 mg/ml, about 8.3 mg/ml, about 8.4 mg/ml, about 8.5 mg/ml, about 8.6 mg/ml, about 8.7 mg/ml, about 8.8 mg/ml, about 8.9 mg/ml, about 9.0 mg/ml, about 9.1 mg/ml, about 9.2 mg/ml, about 9.3 mg/ml, about 9.4 mg/ml, about 9.5 mg/ml, about 9.6 mg/ml, about 9.7 mg/ml, about 9.8 mg/ml, about 9.9 mg/ml, or about 10.0 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is present in about 4.0 mg/ml to about 6.0 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is present in about 6.0 mg/ml to about 8.0 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is hydroxypropyl methyl cellulose and is present in about 5.0 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is hydroxypropyl methyl cellulose and is present in about 7.5 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is hydroxypropyl methyl cellulose and is present in about 10 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is present in about 10 mg/ml to about 30 mg/ml in the oral liquid formulation. In other embodiments, the suspension aid is present in about 10 mg/ml, about 11 mg/ml, about 12 mg/ml, about 13 mg/ml, about 14 mg/ml, about 15 mg/ml, about 16 mg/ml, about 17 mg/ml, about 18 mg/ml, about 19 mg/ml, about 20 mg/ml, about 21 mg/ml, about 22 mg/ml, about 23 mg/ml, about 24 mg/ml, about 25 mg/ml, about 26 mg/ml, about 27 mg/ml, about 28 mg/ml, about 29 mg/ml, or about 30 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is polyvinylpyrrolidone and is present in about 10 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is polyvinylpyrrolidone and is present in about 20 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is polyvinylpyrrolidone and is present in about 30 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is present in about 5 mg/ml to about 15 mg/ml in the oral liquid formulation. In other embodiments, the suspension aid is present in about 5.0 mg/ml, about 5.5 mg/ml, about 6.0 mg/ml, about 6.5 mg/ml, about 7.0 mg/ml, about 7.5 mg/ml, about 8 mg/ml, about 8.5 mg/ml, about 9 mg/ml, about 9.5 mg/ml, about 10 mg/ml, about 10.5 mg/ml, about 11 mg/ml, about 11.5 mg/ml, about 12 mg/ml, about 12.5 mg/ml, about 13 mg/ml, about 13.5 mg/ml, about 14 mg/ml, about 14.5 mg/ml, or about 15 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is Avicel® RC-591 and is present in about 5 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is Avicel® RC-591 and is present in about 7.5 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is Avicel RC-591 and is present in about 10 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is Avicel® RC-591 and is present in about 15 mg/ml in the oral liquid formulation. In some embodiments, the suspension aid is present in about 0.4% w/w to about 6% w/w of the solids in the oral liquid formulation. In other embodiments, the suspension aid is present in about 0.4% w/w, about 0.5% w/w, about 0.6% w/w, about 0.7% w/w, about 0.8% w/w, about 0.9% w/w, about 1% w/w, about 1.1% w/w, about 1.2% w/w, about 1.3% w/w, about 1.4% w/w, about 1.5% w/w, about 1.6% w/w, about 1.7% w/w, about 1.8% w/w, about 1.9% w/w, about 2% w/w, about 2.1% w/w, about 2.2% w/w, about 2.3% w/w, about 2.4% w/w, about 2.5% w/w, about 2.6% w/w, about 2.7% w/w, about 2.8% w/w, about 2.9% w/w, about 3% w/w, about 3.1% w/w, about 3.2% w/w, about 3.3% w/w, about 3.4% w/w, about 3.5% w/w, about 3.6% w/w, about 3.7% w/w, about 3.8% w/w, about 3.9% w/w, about 4% w/w, about 4.1% w/w, about 4.2% w/w, about 4.3% w/w, about 4.4% w/w, about 4.5% w/w, about 4.6% w/w, about 4.7% w/w, about 4.8% w/w, about 4.9% w/w, about 5% w/w, about 5.1% w/w, about 5.2% w/w, about 5.3% w/w, about 5.4% w/w, about 5.5% w/w, about 5.6% w/w, about 5.7% w/w, about 5.8% w/w, about 5.9% w/w, or about 6% w/w of the solids in the oral liquid formulation. In some embodiments, the suspension aid is present in about 20% w/w to about 50% w/w of the solids in the oral liquid formulation. In other embodiments, the suspension aid is present in about 20% w/w, about 20.5% w/w, about 21% w/w, about 21.5% w/w, about 22% w/w, about 22.5% w/w, about 23% w/w, about 23.5% w/w, about 24% w/w, about 24.5% w/w, about 25% w/w, about 25.5% w/w, about 26% w/w, about 26.5% w/w, about 27% w/w, about 27.5% w/w, about 28% w/w, about 28.5% w/w, about 29% w/w, about 29.5% w/w, about 30% w/w, about 30.5% w/w, about 31% w/w, about 31.5% w/w, about 32% w/w, about 32.5% w/w, about 33% w/w, about 33.5% w/w, about 34% w/w, about 34.5% w/w, about 35% w/w, about 35.5% w/w, about 36% w/w, about 36.5% w/w, about 37% w/w, about 37.5% w/w, about 38% w/w, about 38.5% w/w, about 39% w/w, about 39.5% w/w, about 40% w/w, about 41% w/w, about 41.5% w/w, about 42% w/w, about 42.5% w/w, about 43% w/w, about 43.5% w/w, about 44% w/w, about 44.5% w/w, about 45% w/w, about 45.5% w/w, about 46% w/w, about 46.5% w/w, about 47% w/w, about 47.5% w/w, about 48% w/w, about 48.5% w/w, about 49% w/w, about 39.5% w/w, or about 50% w/w of the solids in the oral liquid formulation. In some embodiments, the suspension aid is present in about 40% w/w to about 85% w/w of the solids in the oral liquid formulation. In other embodiments, the suspension aid is present in about 40% w/w, about 41% w/w, about 42% w/w, about 43% w/w, about 44% w/w, about 45% w/w, about 46% w/w, about 47% w/w, about 48% w/w, about 49% w/w, about 50% w/w, about 51% w/w, about 52% w/w, about 53% w/w, about 54% w/w, about 55% w/w, about 56% w/w, about 57% w/w, about 58% w/w, about 59% w/w, about 60% w/w, about 61% w/w, about 62% w/w, about 63% w/w, about 64% w/w, about 65% w/w, about 66% w/w, about 67% w/w, about 68% w/w, about 69% w/w, about 70% w/w, about 71% w/w, about 72% w/w, about 73% w/w, about 74% w/w, about 75% w/w, about 76% w/w, about 77% w/w, about 78% w/w, about 79% w/w, about 80% w/w, about 81% w/w, about 82% w/w, about 83% w/w, about 84% w/w, or about 85% w/w of the solids in the oral liquid formulation. In some embodiments, the suspension aid is present in about 35% w/w to about 55% w/w of the solids in the oral liquid formulation. In other embodiments, the suspension aid is present in about 35% w/w, about 36% w/w, about 37% w/w, about 38% w/w, about 39% w/w, about 40% w/w, about 41% w/w, about 42% w/w, about 43% w/w, about 44% w/w, about 45% w/w, about 46% w/w, about 47% w/w, about 48% w/w, about 49% w/w, about 50% w/w, about 51% w/w, about 52% w/w, about 53% w/w, about 54% w/w, or about 55% w/w of the solids in the oral liquid formulation. Antifoaming Agent in the Amlodipine Oral Liquid Formulations Antifoaming agents are chemical additives that reduce and hinder the formation of foam in the preparation of an oral liquid formulation. The terms antifoaming agent and defoamer are often used interchangeably. Commonly used agents are insoluble oils, polydimethylsiloxanes (e.g., simethicone) and other silicones, certain alcohols, stearates and glycols. Simethicone is available as a pure material (100%) and in combination with other excipients to facilitate dispersion and handling. Common simethicone containing products include NuSil MED-342 (30% w/w simethicone, solid), NuSil Med-340, Med-346, and Med-347 (100% silicone, liquid), Dow Corning® Q7-2587, 7-9245, and Medical Antifoam C (30% Simethicone Emulsion). The additive is used to prevent formation of foam or is added to break foam already formed. Antifoaming agents reduce foaming in the preparation of an oral liquid formulation which can result in coagulation of aqueous dispersions. In some embodiments, the amlodipine oral liquid formulation described herein comprises an antifoaming agent. In some embodiments, the antifoaming agent is simethicone. In some embodiments, the antifoaming agent is present in about 0.05 mg/ml to about 1.0 mg/ml in the oral liquid formulation. In other embodiments, the antifoaming agent is present in about 0.05 mg/ml, about 0.1 mg/ml, about 0.15 mg/ml, about 0.2 mg/ml, about 0.25 mg/ml, about 0.3 mg/ml, about 0.35 mg/ml, about 0.4 mg/ml, about 0.45 mg/ml, about 0.5 mg/ml, about 0.55 mg/ml, about 0.6 mg/ml, about 0.65 mg/ml, about 0.7 mg/ml, about 0.75 mg/ml, about 0.8 mg/ml, about 0.85 mg/ml, about 0.9 mg/ml, about 0.95 mg/ml, or about 1.0 mg/ml in the oral liquid formulation. In some embodiments, the antifoaming agent is present in about 0.05 mg/ml to about 0.3 mg/ml in the oral liquid formulation. In some embodiments, the antifoaming agent is present in about 0.1 mg/ml to about 0.2 mg/ml in the oral liquid formulation. In some embodiments, the antifoaming agent is simethicone and is present in about 0.15 mg/ml in the oral liquid formulation. In some embodiments, the antifoaming agent is present in about 0.1% w/w to about 7% w/w of the solids in the oral liquid formulation. In other embodiments, the antifoaming agent is present in about 0.1% w/w, about 0.2% w/w, about 0.3% w/w, about 0.4% w/w, about 0.5% w/w, about 0.6% w/w, about 0.7% w/w, about 0.8% w/w, about 0.9% w/w, about 1% w/w, about 1.1% w/w, about 1.2% w/w, about 1.3% w/w, about 1.4% w/w, about 1.5% w/w, about 1.6% w/w, about 1.7% w/w, about 1.8% w/w, about 1.9% w/w, about 2% w/w, about 2.1% w/w, about 2.2% w/w, about 2.3% w/w, about 2.4% w/w, about 2.5% w/w, about 2.6% w/w, about 2.7% w/w, about 2.8% w/w, about 2.9% w/w, about 3% w/w, about 3.1% w/w, about 3.2% w/w, about 3.3% w/w, about 3.4% w/w, about 3.5% w/w, about 3.6% w/w, about 3.7% w/w, about 3.8% w/w, about 3.9% w/w, about 4% w/w, about 4.1% w/w, about 4.2% w/w, about 4.3% w/w, about 4.4% w/w, about 4.5% w/w, about 4.6% w/w, about 4.7% w/w, about 4.8% w/w, about 4.9% w/w, about 5% w/w, about 5.1% w/w, about 5.2% w/w, about 5.3% w/w, about 5.4% w/w, about 5.5% w/w, about 5.6% w/w, about 5.7% w/w, about 5.8% w/w, about 5.9% w/w, about 6% w/w, about 6.1% w/w, about 6.2% w/w, about 6.3% w/w, about 6.4% w/w, about 6.5% w/w, about 6.6% w/w, about 6.7% w/w, about 6.8% w/w, about 6.9% w/w, or about 7% w/w of the solids in the oral liquid formulation. Surfactants in the Amlodipine Oral Liquid Formulations Surfactants are compounds that lower the surface tension (or interfacial tension) between two liquids or between a liquid and a solid. Most commonly, surfactants are classified according to polar head group. A non-ionic surfactant has no charged groups in its head. The head of an ionic surfactant carries a net positive, or negative charge. If the charge is negative, the surfactant is more specifically called anionic; if the charge is positive, it is called cationic. If a surfactant contains a head with two oppositely charged groups, it is termed zwitterionic. Anionic surfactants contain anionic functional groups at their head, such as sulfate, sulfonate, phosphate, and carboxylates. Prominent alkyl sulfates include ammonium lauryl sulfate, sodium lauryl sulfate (sodium dodecyl sulfate, SLS, or SDS), and the related alkyl-ether sulfates sodium laureth sulfate (sodium lauryl ether sulfate or SLES), and sodium myreth sulfate. Others include: docusate (dioctyl sodium sulfosuccinate), perfluorooctanesulfonate (PFOS), perfluorobutanesulfonate, alkyl-aryl ether phosphates, alkyl ether phosphates. Cationic surfactant include pH-dependent primary, secondary, or tertiary amines such as octenidine dihydrochloride; and permanently charged quaternary ammonium salts such as cetrimonium bromide (CTAB), cetylpyridinium chloride (CPC), benzalkonium chloride (BAC), benzethonium chloride (BZT), dimethyldioctadecylammonium chloride, and dioctadecyldimethylammonium bromide (DODAB). Zwitterionic (amphoteric) surfactants have both cationic and anionic centers attached to the same molecule. The cationic part is based on primary, secondary, or tertiary amines or quaternary ammonium cations. The anionic part can be more variable and include sulfonates, as in the sultaines CHAPS (3[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate) and cocamidopropyl hydroxysultaine. Betaines such as cocamidopropyl betaine have a carboxylate with the ammonium. The most common biological zwitterionic surfactants have a phosphate anion with an amine or ammonium, such as the phospholipids phosphatidylserine, phosphatidylethanolamine, phosphatidylcholine, and sphingomyelins. Nonionic surfactants include fatty alcohols, cetyl alcohol, stearyl alcohol, and cetostearyl alcohol, and oleyl alcohol. Also used as nonionic surfactants are polyethylene glycol alkyl ethers (such as octaethylene glycol monododecyl ether, pentaethylene glycol monododecyl ether), polypropylene glycol alkyl ethers, glucoside alkyl ethers (such as decyl glucoside, lauryl glucoside, octyl glucoside), polyethylene glycol octylphenyl ethers (such as Triton X-100), polyethylene glycol alkylphenyl ethers (such as nonoxynol-9), glycerol alkyl esters (such as glyceryl laurate), polyoxyethylene glycol sorbitan alkyl esters (such as polysorbate), sorbitan alkyl esters (such as Spans), cocamide MEA, cocamide DEA, dodecyldimethylamine oxide, block copolymers of polyethylene glycol and polypropylene glycol (such as poloxamers), and polyethoxylated tallow amine (POEA). The most commonly used surfactants are fatty acid esters of sorbitan polyethoxylates, i.e. polysorbate 20 and polysorbate 80. The two differ only in the length of the aliphatic chain that imparts hydrophobic character to the molecules, C-12 and C-18, respectively. Polysorbate 80 is more surface-active and has a lower critical micellar concentration than polysorbate 20. In some embodiments, the amlodipine oral liquid formulation described herein comprises a surfactant. In some embodiments, the surfactant is polysorbate 80. In some embodiments, the amlodipine oral liquid formulation described herein does not comprise a surfactant. In some embodiments, the surfactant, when present, is present in about 0.1 mg/ml to about 3.0 mg/ml in the oral liquid formulation. In other embodiments, the surfactant, when present, is present in about 0.1 mg/ml, about 0.15 mg/ml, about 0.2 mg/ml, about 0.25 mg/ml, about 0.3 mg/ml, about 0.35 mg/ml, about 0.4 mg/ml, about 0.45 mg/ml, about 0.5 mg/ml, about 0.55 mg/ml, about 0.6 mg/ml, about 0.65 mg/ml, about 0.7 mg/ml, about 0.75 mg/ml, about 0.8 mg/ml, about 0.85 mg/ml, about 0.9 mg/ml, about 0.95 mg/ml, about 1.0 mg/ml, about 1.1 mg/ml, about 1.15 mg/ml, about 1.2 mg/ml, about 1.25 mg/ml, about 1.3 mg/ml, about 1.35 mg/ml, about 1.4 mg/ml, about 1.45 mg/ml, about 1.5 mg/ml, about 1.55 mg/ml, about 1.6 mg/ml, about 1.65 mg/ml, about 1.7 mg/ml, about 1.75 mg/ml, about 1.8 mg/ml, about 1.85 mg/ml, about 1.9 mg/ml, about 1.95 mg/ml, about 2.0 mg/ml, about 2.1 mg/ml, about 2.15 mg/ml, about 2.2 mg/ml, about 2.25 mg/ml, about 2.3 mg/ml, about 2.35 mg/ml, about 2.4 mg/ml, about 2.45 mg/ml, about 2.5 mg/ml, about 2.55 mg/ml, about 2.6 mg/ml, about 2.65 mg/ml, about 2.7 mg/ml, about 2.75 mg/ml, about 2.8 mg/ml, about 2.85 mg/ml, about 2.9 mg/ml, about 2.95 mg/ml, or about 3.0 mg/ml in the oral liquid formulation. In some embodiments, the surfactant, when present, is polysorbate 80 and is present in about 0.5 mg/ml in the oral liquid formulation. In some embodiments, the surfactant, when present, is polysorbate 80 and is present in about 1.0 mg/ml in the oral liquid formulation. In some embodiments, the surfactant, when present, is polysorbate 80 and is present in about 2.0 mg/ml in the oral liquid formulation. In some embodiments, the surfactant, when present is present in about 1% w/w to about 15% w/w of the solids in the oral liquid formulation. In other embodiments, the surfactant, when present is present in about 1%, about 1.5%, about 2%, about 2.5%, about 3%, about 3.5%, about 4%, about 4.5%, about 5%, about 5.5%, about 6%, about 6.5%, about 7%, about 7.5%, about 8%, about 8.5%, about 9%, about 9.5%, about 10%, about 10.5%, about 11%, about 11.5%, about 12%, about 12.5%, about 13%, about 13.5%, about 14%, about 14.5%, or about 15% of the solids in the oral liquid formulation. In some embodiments, the surfactant, when present is present in about 1% w/w to about 5% w/w of the solids in the oral liquid formulation. In other embodiments, the surfactant, when present is present in about 1%, about 1.1%, about 1.2%, about 1.3%, about 1.4%, about 1.5%, about 1.6%, about 1.7%, about 1.8%, about 1.9%, about 2%, about 2.1%, about 2.2%, about 2.3%, about 2.4%, about 2.5%, about 2.6%, about 2.7%, about 2.8%, about 2.9%, about 3%, about 3.1%, about 3.2%, about 3.3%, about 3.4%, about 3.5%, about 3.6%, about 3.7%, about 3.8%, about 3.9%, about 4%, about 4.1%, about 4.2%, about 4.3%, about 4.4%, about 4.5%, about 4.6%, about 4.7%, about 4.8%, about 4.9%, or about 5% of the solids in the oral liquid formulation. Additional Excipients In further embodiments, the amlodipine oral liquid formulation described herein comprises additional excipients including, but not limited to flavoring agents, coloring agents and thickeners. Additional excipients such as bulking agents, tonicity agents and chelating agents are within the scope of the embodiments. In another embodiment, the amlodipine oral liquid formulation comprises a flavoring agent or flavorant to enhance the taste or aroma of the formulation in liquid form. Suitable natural or synthetic flavoring agents can be selected from standard reference books, for example Fenaroli's Handbook of Flavor Ingredients, 3rd edition (1995). Non-limiting examples of suitable natural flavors, some of which can readily be simulated with synthetic agents or combinations thereof, include almond, anise, apple, apricot, bergamot, blackberry, blackcurrant, blueberry, cacao, caramel, cherry, cinnamon, clove, coffee, coriander, cranberry, cumin, dill, eucalyptus, fennel, fig, ginger, grape, grapefruit, guava, hop, lemon, licorice, lime, malt, mandarin, molasses, nutmeg, mixed berry, orange, peach, pear, peppermint, pineapple, raspberry, rose, spearmint, strawberry, tangerine, tea, vanilla, wintergreen, etc. Also useful, particularly where the formulation is intended primarily for pediatric use, is tutti-frutti or bubblegum flavor, a compounded flavoring agent based on fruit flavors. Presently preferred flavoring agents include anise, cinnamon, cacao, orange, peppermint, cherry (in particular wild cherry), grape, bubblegum, vanilla, and mixed berry. Flavoring agents can be used singly or in combinations of two or more. In certain embodiments, the amlodipine oral liquid formulation comprises a flavoring agent. In further embodiments, the amlodipine oral liquid formulation comprises a coloring agent for identity and/or aesthetic purposes. Suitable coloring agents illustratively include FD&C Red No. 3, FD&C Red No. 20, FD&C Red No. 40, FD&C Yellow No. 6, FD&C Blue No. 2, FD&C Green No. 5, FD&C Orange No. 5, caramel, ferric oxide and mixtures thereof. Thickeners impart viscosity or weight to the resultant liquid forms from the amlodipine formulation described herein. Exemplary thickeners include dextrin, cellulose derivatives (carboxymethylcellulose and its salts, ethylcellulose, hydroxyethyl cellulose, methylcellulose, hypromellose, and the like) starches, pectin, polyethylene glycol, polyethylene oxide, trehalose, certain silicates (magnesium aluminum silicate, aluminum silicate, etc. such as Veegum, Bentonite, and Kaolin) and certain gums (xanthan gum, locust bean gum, etc.). In certain embodiments, the amlodipine oral liquid formulation comprises a thickener. In further embodiments, the amlodipine liquid formulation does not comprise glycerol which may cause headache, stomach upset, and diarrhea. Additional excipients are contemplated in the amlodipine oral liquid formulation embodiments. These additional excipients are selected based on function and compatibility with the amlodipine liquid formulations described herein and may be found, for example in Remington: The Science and Practice of Pharmacy, Nineteenth Ed (Easton, Pa.: Mack Publishing Company, 1995); Hoover, John E., Remington's Pharmaceutical Sciences, (Easton, Pa.: Mack Publishing Co 1975); Liberman, H. A. and Lachman, L., Eds., Pharmaceutical Dosage Forms (New York, N.Y.: Marcel Decker 1980); and Pharmaceutical Dosage Forms and Drug Delivery Systems, Seventh Ed (Lippincott Williams & Wilkins 1999), herein incorporated by reference in their entirety. Stability The amlodipine oral liquid formulations described herein are stable in various storage conditions including refrigerated, ambient and accelerated conditions. Stable as used herein refers to amlodipine oral liquid formulations having about 95% or greater of the initial amlodipine amount and/or about 5% w/w or less total impurities or related substances at the end of a given storage period. In some embodiment, the impurity is amlodipine USP impurity A (A.K.A EP impurity D): The percentage of impurities is calculated from the amount of impurities relative to the amount of amlodipine. Stability is assessed by HPLC or any other known testing method. In some embodiments, the stable amlodipine oral liquid formulations have about 5% w/w, about 4% w/w, about 3% w/w, about 2.5% w/w, about 2% w/w, about 1.5% w/w, about 1% w/w, or about 0.5% w/w total impurities or related substances. In other embodiments, the stable amlodipine oral liquid formulations have about 5% w/w total impurities or related substances. In yet other embodiments, the stable amlodipine oral liquid formulations have about 4% w/w total impurities or related substances. In yet other embodiments, the stable amlodipine oral liquid formulations have about 3% w/w total impurities or related substances. In yet other embodiments, the stable amlodipine oral liquid formulations have about 2% w/w total impurities or related substances. In yet other embodiments, the stable amlodipine oral liquid formulations have about 1% w/w total impurities or related substances. At refrigerated condition, the amlodipine oral liquid formulations described herein are stable for at least 1 month, at least 2 months, at least 3 months, at least 6 months, at least 9 months, at least 12 months, at least 15 months, at least 18 months, at least 24 months, at least 30 months and at least 36 months. In some embodiments, refrigerated condition is 5±5° C. In some embodiments, refrigerated condition is about 0° C., about 0.1° C., about 0.2° C., about 0.3° C., about 0.4° C., about 0.5° C., about 0.6° C., about 0.7° C., about 0.8° C., about 0.9° C., about 1° C., about 1.1° C., about 1.2° C., about 1.3° C., about 1.4° C., about 1.5° C., about 1.6° C., about 1.7° C., about 1.8° C., about 1.9° C., about 2° C., about 2.1° C., about 2.2° C., about 2.3° C., about 2.4° C., about 2.5° C., about 2.6° C., about 2.7° C., about 2.8° C., about 2.9° C., about 3° C., about 3.1° C., about 3.2° C., about 3.3° C., about 3.4° C., about 3.5° C., about 3.6° C., about 3.7° C., about 3.8° C., about 3.9° C., about 4° C., about 4.1° C., about 4.2° C., about 4.3° C., about 4.4° C., about 4.5° C., about 4.6° C., about 4.7° C., about 4.8° C., about 4.9° C., about 5° C., about 5.1° C., about 5.2° C., about 5.3° C., about 5.4° C., about 5.5° C., about 5.6° C., about 5.7° C., about 5.8° C., about 5.9° C., about 6° C., about 6.1° C., about 6.2° C., about 6.3° C., about 6.4° C., about 6.5° C., about 6.6° C., about 6.7° C., about 6.8° C., about 6.9° C., about 7° C., about 7.1° C., about 7.2° C., about 7.3° C., about 7.4° C., about 7.5° C., about 7.6° C., about 7.7° C., about 7.8° C., about 7.9° C., about 8° C., about 8.1° C., about 8.2° C., about 8.3° C., about 8.4° C., about 8.5° C., about 8.6° C., about 8.7° C., about 8.8° C., about 8.9° C., about 9° C., about 9.1° C., about 9.2° C., about 9.3° C., about 9.4° C., about 9.5° C., about 9.6° C., about 9.7° C., about 9.8° C., about 9.9° C., or about 10° C. At accelerated conditions, the amlodipine oral liquid formulations described herein are stable for at least 1 month, at least 2 months, at least 3 months, at least 4 months, at least 5 months, at least 6 months, at least 7 months, at least 8 months, at least 9 months, at least 10 months, at least 11 months, at least 12 months, at least 18 months, or at least 24 months. Accelerated conditions for the amlodipine oral liquid formulations described herein include temperatures that are at or above ambient levels (25±5° C.). In some instances, an accelerated condition is at about 25° C., about 30° C., about 35° C., about 40° C., about 45° C., about 50° C., about 55° C., or about 60° C. Accelerated conditions for the amlodipine oral liquid formulations described herein also include relative humidity (RH) that are at or above ambient levels (55±10% RH). In other instances, an accelerated condition is above 55% RH, about 65% RH, about 70% RH, about 75% RH, or about 80% RH. In further instances, an accelerated condition is about 40° C. or 60° C. at ambient humidity. In yet further instances, an accelerated condition is about 40° C. at 75±5% RH humidity. In some embodiments, the amlodipine oral liquid formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In one embodiment, the amlodipine oral liquid formulation is stable at about 5±5° C. for at least 12 months. In one embodiment, the amlodipine oral liquid formulation is stable at about 25±5° C. for at least 12 months. In one embodiment, the amlodipine oral liquid formulation is stable at about 5±5° C. for at least 24 months. In one embodiment, the amlodipine oral liquid formulation is stable at about 25±5° C. for at least 24 months. Kits and Articles of Manufacture For the amlodipine liquid formulations described herein, kits and articles of manufacture are also described. Such kits can comprise a carrier, package, or container that is compartmentalized to receive one or more containers such as vials, tubes, and the like, each of the container(s) comprising one of the separate elements to be used in a method described herein including an amlodipine liquid formulation. Suitable containers include, for example, bottles, vials, syringes, and test tubes. The containers can be formed from a variety of materials such as glass or plastic. A kit will typically comprise one or more additional containers, each with one or more of various materials (such as reagents, optionally in concentrated form, and/or devices) desirable from a commercial and user standpoint for an amlodipine liquid formulation described herein. Non-limiting examples of such materials include, but not limited to, buffers, diluents, filters, needles, syringes; carrier, package, container, vial and/or tube labels listing contents and/or instructions for use, and package inserts with instructions for use associated with an amlodipine liquid formulation. A set of instructions will also typically be included. A label can be on or associated with the container. A label can be on a container when letters, numbers or other characters forming the label are attached, molded or etched into the container itself; a label can be associated with a container when it is present within a receptacle or carrier that also holds the container, e.g., as a package insert. A label can be used to indicate that the contents are to be used for a specific therapeutic application. The label can also indicate directions for use of the contents, such as in the methods described herein. Method of Manufacturing Disclosed herein is a process for preparing a stable amlodipine oral liquid formulation. In some embodiments, the stable amlodipine oral liquid formulation is in the form of a suspension. In some embodiments, the stable amlodipine oral liquid formulation comprises a pharmaceutically acceptable salt of amlodipine which is very slightly soluble in an aqueous media. In some embodiments, the stable amlodipine oral liquid formulation comprises a pharmaceutically acceptable salt of amlodipine which is practically insoluble in an aqueous media. Disclosed herein is a process for preparing a stable amlodipine oral liquid formulation, the process comprising mixing a first mixture with a second mixture; the first mixture comprising: a pharmaceutically acceptable salt of amlodipine; optionally a salt comprising the counter ions from a water soluble salt of amlodipine and a salt forming agent; one or more agent selected from the group consisting of preservatives and surfactants; and water; and the second mixture comprising: a buffer; optionally one or more agents selected from the group consisting of flavoring agents, sweetening agents, suspensions aids, and antifoaming agents; and water. In some embodiments, the first mixture comprises a pharmaceutically acceptable salt of amlodipine; a preservative; a surfactant; and water. In some embodiments, the first mixture comprises a pharmaceutically acceptable amlodipine salt; a preservative; and water. In some embodiments, the first mixture is obtained by a process comprising adding water to a first container; adding a water soluble salt of amlodipine to the first container; adding a salt forming agent to the first container; adding a preservative; optionally adding a surfactant to the first container; and stirring until a new pharmaceutically acceptable salt of amlodipine substantially precipitates. In some embodiments, the second mixture comprises a buffer; optionally a flavoring agent; a sweetening agent; suspensions aids; an antifoaming agent; and water. In some embodiments, the second mixture is obtained by a process comprising adding water to a second container; adding a buffer to a second container; adding a sweetening agent to a second container; optionally adding a flavoring agent to a second container; adding an antifoaming agent to a second container; adding suspension aids to a second container; and stirring. In some embodiments, the preservative is sodium benzoate and the buffer is a citrate buffer. In some embodiments, the preservative is a paraben or a mixture of parabens and the buffer is a phosphate buffer. Disclosed herein is a process for preparing a stable amlodipine oral liquid formulation, the process comprising mixing a first mixture with a second mixture; the first mixture comprising: amlodipine benzoate; sodium benzoate; optionally sodium besylate; optionally polysorbate 80; and water; and the second mixture comprising: citric acid; sodium citrate; sucralose; optionally a flavoring agent; hydroxypropyl methylcellulose; simethicone; silicon dioxide; and water. In some embodiments, the first mixture is obtained by a process comprising adding water to a first container which is not stainless steel; adding amlodipine besylate to the first container; adding sodium benzoate to the first container; optionally adding polysorbate 80 to the first container; and stirring until amlodipine benzoate substantially precipitates. In some embodiments, the second mixture is obtained by a process comprising adding water to a second container; adding citric acid to the second container; adding sodium citrate to the second container; adding sucralose to the second container; optionally adding a flavoring agent to the second container; adding hydroxypropyl methylcellulose to the second container; adding simethicone to the second container; adding silicon dioxide to the second container; and stirring. Disclosed herein is a process for preparing a stable amlodipine oral liquid formulation, the process comprising mixing a first mixture with a second mixture; the first mixture comprising: amlodipine benzoate; sodium benzoate; polysorbate 80; optionally sodium besylate; and water; and the second mixture comprising: citric acid; sodium citrate; sucralose; optionally a flavoring agent; hydroxypropyl methylcellulose; simethicone; silicon dioxide; and water. In some embodiments, the first mixture is obtained by a process comprising adding water to a first container which is not stainless steel; adding amlodipine besylate to the first container; adding sodium benzoate to the first container; adding polysorbate 80 to the first container; and stirring until amlodipine benzoate substantially precipitates. In some embodiments, the second mixture is obtained by a process comprising adding water to a second container; adding citric acid to the second container; adding sodium citrate to the second container; adding sucralose to the second container; optionally adding the flavoring agent to the second container; adding hydroxypropyl methylcellulose to the second container; adding simethicone to the second container; adding silicon dioxide to the second container; and stirring. Disclosed herein is a process for preparing a stable amlodipine oral liquid formulation, the process comprising mixing a first mixture with a second mixture; the first mixture comprising: amlodipine naphthalene sulfonate; sodium benzoate; optionally sodium besylate; optionally polysorbate 80; and water; and the second mixture comprising: citric acid; sodium citrate; sucralose; optionally a flavoring agent; hydroxypropyl methylcellulose; simethicone; silicon dioxide; and water. In some embodiments, the first mixture is obtained by a process comprising adding water to a first container which is not stainless steel; adding amlodipine besylate to the first container; adding sodium naphthalene-2-sulfonate to the first container; adding sodium benzoate to the first container; optionally adding polysorbate 80 to the first container; and stirring until amlodipine naphthalene sulfonate substantially precipitates. In some embodiments, the second mixture is obtained by a process comprising adding water to a second container; adding citric acid to the second container; adding sodium citrate to the second container; adding sucralose to the second container; optionally adding the flavoring agent to the second container; adding hydroxypropyl methylcellulose to the second container; adding simethicone to the second container; adding silicon dioxide to the second container; and stirring. In some embodiments, the first mixture is obtained by a process comprising adding water to a first container which is not stainless steel; adding amlodipine besylate to the first container; adding sodium naphthalene-2-sulfonate to the first container; adding sodium benzoate to the first container; and stirring until amlodipine naphthalene sulfonate substantially precipitates. In some embodiments, the second mixture is obtained by a process comprising adding water to a second container; adding citric acid to the second container; adding sodium citrate to the second container; adding sucralose to the second container; optionally adding the flavoring agent to the second container; adding hydroxypropyl methylcellulose to the second container; adding simethicone to the second container; adding silicon dioxide to the second container; and stirring. In some embodiments, the sodium benzoate is added to the second container. In some embodiments sodium benzoate is not added to the first container. Disclosed herein is a process for preparing a stable amlodipine oral liquid formulation in a single container. In some embodiments, the process for preparing a stable amlodipine oral liquid formulation in a single container comprises the formation of a pharmaceutically acceptable salt of amlodipine; followed by addition of one or more agents selected from the group consisting of preservatives, surfactants, flavoring agents, sweetening agents, suspensions aids, and antifoaming agents. In some embodiments, the pharmaceutically acceptable salt of amlodipine is obtained by a process comprising adding water to a container, adding a buffer to the container; adding a water soluble salt of amlodipine to the container; adding a salt forming agent to the container; and stirring until a new pharmaceutically acceptable salt of amlodipine substantially precipitates. The process further comprises cooling the suspension of the new pharmaceutically acceptable salt of amlodipine. The process further comprises adding optional components selected from preservatives, surfactants, flavoring agents, sweetening agents, suspensions aids, and antifoaming agents. In some embodiments, the container is not stainless steel. In some embodiments, high shear mixing is used. In some embodiments, sonication is used. In some embodiments, the process for preparing a stable amlodipine oral liquid formulation in a single container comprises the formation of a pharmaceutically acceptable salt of amlodipine following the addition of one or more agent selected from the group consisting of buffers, preservatives, surfactants, flavoring agents, sweetening agents, suspensions aids, and antifoaming agents. In some embodiments, process comprises adding water to a container; adding a salt forming agent to the container; optionally adding one or more agent selected from the group consisting of buffers, preservatives, surfactants, flavoring agents, sweetening agents, suspensions aids, and antifoaming agents to the container; adding a water soluble salt of amlodipine to the container; and stirring until a new pharmaceutically acceptable salt of amlodipine substantially precipitates. In some embodiments, the container is not stainless steel. Methods of Treatment Provided herein, in one aspect, are methods of treatment comprising administration of the amlodipine oral liquid formulations described herein to a subject. In some embodiments, the amlodipine oral liquid formulations described herein treat hypertension in a subject. Hypertension as used herein includes both primary (essential) hypertension and secondary hypertension. In certain instances, hypertension is classified in cases when blood pressure values are greater than or equal to 140/90 (systolic/diastolic) mm Hg in a subject. In certain instances, the amlodipine oral liquid formulations described herein treat a subject having a blood pressure values are greater than or equal to 140/90 mm Hg. In certain instances, the amlodipine oral liquid formulations described herein treat primary (essential) hypertension in a subject. In other instances, the amlodipine oral liquid formulations described herein treat secondary hypertension in a subject. In other embodiments, the amlodipine oral liquid formulations described herein treat prehypertension in a subject. Prehypertension as used herein refers to cases where a subject's blood pressure is elevated above normal but not to the level considered to be hypertension. In some instances, prehypertension is classified in cases when blood pressure values are 120-139/80-89 mm Hg. In certain instances, the amlodipine oral liquid formulations described herein treat a subject having blood pressure values of 120-139/80-89 mm Hg. In yet other embodiments, the amlodipine oral liquid formulations described herein are prophylactically administered to subjects suspected of having, predisposed to, or at risk of developing hypertension. In some embodiments, the administration of amlodipine oral liquid formulations described herein allow for early intervention prior to onset of hypertension. In certain embodiments, upon detection of a biomarker, environmental, genetic factor, or other marker, the amlodipine oral liquid formulations described herein are prophylactically administered to subjects. In further embodiments, the amlodipine oral liquid formulations described herein treat Coronary Artery Disease (CAD). In some embodiments, the amlodipine oral liquid formulations described herein treat chronic stable angina. In some embodiments, the amlodipine oral liquid formulations described herein treat vasospastic angina (Prinzmetal's or Variant angina). In some embodiments, the amlodipine oral liquid formulations described herein treat angiographically documented coronary artery disease in patients without heart failure or an ejection fraction <40%. Dosing In one aspect, the amlodipine oral liquid formulations are used for the treatment of diseases and conditions described herein. In addition, a method for treating any of the diseases or conditions described herein in a subject in need of such treatment, involves administration of amlodipine oral liquid formulations in therapeutically effective amounts to said subject. Dosages of amlodipine oral liquid formulations described can be determined by any suitable method. Maximum tolerated doses (MTD) and maximum response doses (MRD) for amlodipine can be determined via established animal and human experimental protocols as well as in the examples described herein. For example, toxicity and therapeutic efficacy of amlodipine can be determined by standard pharmaceutical procedures in cell cultures or experimental animals, including, but not limited to, for determining the LD50 (the dose lethal to 50% of the population) and the ED50 (the dose therapeutically effective in 50% of the population). The dose ratio between the toxic and therapeutic effects is the therapeutic index and it can be expressed as the ratio between LD50 and ED50. Amlodipine dosages exhibiting high therapeutic indices are of interest. The data obtained from cell culture assays and animal studies can be used in formulating a range of dosage for use in human. The dosage of such compounds lies preferably within a range of circulating concentrations that include the ED50 with minimal toxicity. The dosage may vary within this range depending upon the dosage form employed and the route of administration utilized. Additional relative dosages, represented as a percent of maximal response or of maximum tolerated dose, are readily obtained via the protocols. In some embodiments, the amount of a given amlodipine oral liquid formulation that corresponds to such an amount varies depending upon factors such as the particular amlodipine salt or form, disease condition and its severity, the identity (e.g., weight, sex) of the subject or host in need of treatment, but can nevertheless be determined according to the particular circumstances surrounding the case, including, e.g., the specific agent being administered, the liquid composition type, the condition being treated, and the subject or host being treated. In some embodiments, the amlodipine oral liquid formulations described herein are provided in a dose per day from about 0.01 mg to 100 mg, from about 0.1 mg to about 80 mg, from about 1 to about 60, from about 2 mg to about 40 mg of amlodipine. In certain embodiments, the amlodipine oral liquid formulations described herein are provided in a daily dose of about 0.01 mg, about 0.05 mg, about 0.1 mg, about 0.2 mg, about 0.4 mg, about 0.6 mg, about 0.8 mg, about 1 mg, about 1.5 mg, about 2 mg, about 2.5 mg, about 3 mg, about 4 mg, about 5 mg, about 6 mg, about 7 mg, about 8 mg, about 9 mg, about 10 mg, about 11 mg, about 12 mg, about 15 mg, about 20 mg, about 25 mg, about 30 mg, about 35 mg, about 40 mg, about 45 mg, about 50 mg, about 55 mg, about 60 mg, about 65 mg, about 70 mg, about 76, mg, about 80 mg, about 85 mg, about 90 mg or about 100 mg, or any range derivable therein. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 1 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 2 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 3 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 4 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 5 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 6 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 7 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 8 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 9 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 10 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 11 mg. In certain instances, the amlodipine oral liquid formulations described herein are provided in a dose per day of about 12 mg. The dose per day described herein can be given once per day or multiple times per day in the form of sub-doses given b.i.d., t.i.d., q.i.d., or the like where the number of sub-doses equal the dose per day. In further embodiments, the daily dosages appropriate for the amlodipine oral liquid formulations described herein are from about 0.01 to about 1.0 mg/kg per body weight. In one embodiment, the daily dosages appropriate for the amlodipine oral liquid formulations are from about 0.02 to about 0.8 mg/kg amlodipine per body weight. In another embodiment, the daily dosage appropriate for the amlodipine oral liquid formulations are from about 0.05 to about 0.6 mg/kg per body weight. In another embodiment, the daily dosage appropriate for the amlodipine oral liquid formulations is about 0.05 mg/kg, about 0.06 mg/kg, about 0.07 mg/kg, about 0.08 mg/kg, about 0.10 mg/kg, about 0.15 mg/kg, about 0.20 mg/kg, about 0.25 mg/kg, about 0.30 mg/kg, about 0.40 mg/kg, about 0.50 mg/kg, or about 0.60 mg/kg. In other embodiments, the amlodipine oral liquid formulations are provided at the maximum tolerated dose (MTD) for amlodipine. In other embodiments, the amount of the amlodipine oral liquid formulations administered is from about 10% to about 90% of the maximum tolerated dose (MTD), from about 25% to about 75% of the MTD, or about 50% of the MTD. In particular embodiments, the amount of the amlodipine oral liquid formulations administered is from about 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 99%, or higher, or any range derivable therein, of the MTD for amlodipine. In further embodiments, the amlodipine oral liquid formulations are provided in a dosage that is similar, comparable or equivalent to a dosage of a known amlodipine tablet formulation. In other embodiments, the amlodipine oral liquid formulations are provided in a dosage that provides similar, comparable or equivalent pharmacokinetic parameters (e.g., AUC, Cmax, Tmax, Cmin, T1/2) as a dosage of a known amlodipine tablet formulation. Similar, comparable or equivalent pharmacokinetic parameters, in some instances, refer to within 80% to 125%, 80% to 120%, 85% to 125%, 90% to 110%, or increments therein, of the given values. It should be recognized that the ranges can, but need not be symmetrical, e.g., 85% to 105%. Administration Administration of an amlodipine oral liquid formulation is at a dosage described herein or at other dose levels and formulations determined and contemplated by a medical practitioner. In certain embodiments, the amlodipine oral liquid formulations described herein are administered for prophylactic and/or therapeutic treatments. In certain therapeutic applications, the amlodipine oral liquid formulations are administered to a patient already suffering from a disease, e.g., hypertension, in an amount sufficient to cure the disease or at least partially arrest or ameliorate the symptoms, e.g., lower blood pressure. Amounts effective for this use depend on the severity of the disease, previous therapy, the patient's health status, weight, and response to the amlodipine formulations, and the judgment of the treating physician. Therapeutically effective amounts are optionally determined by methods including, but not limited to, a dose escalation clinical trial. In prophylactic applications, the amlodipine oral liquid formulations described herein are administered to a patient susceptible to or otherwise at risk of a particular disease, e.g., hypertension. Such an amount is defined to be a “prophylactically effective amount or dose.” In this use, the precise amounts also depend on the patient's state of health, weight, and the like. When used in a patient, effective amounts for this use will depend on the risk or susceptibility of developing the particular disease, previous therapy, the patient's health status and response to the amlodipine formulations, and the judgment of the treating physician. In certain embodiments wherein the patient's condition does not improve, upon the doctor's discretion the administration of an amlodipine oral liquid formulations described herein are administered chronically, that is, for an extended period of time, including throughout the duration of the patient's life in order to ameliorate or otherwise control or limit the symptoms of the patient's disease. In other embodiments, administration of an amlodipine oral liquid formulation continues until complete or partial response of a disease. In certain embodiments wherein a patient's status does improve, the dose of an amlodipine oral liquid formulation being administered may be temporarily reduced or temporarily suspended for a certain length of time (i.e., a “drug holiday”). In specific embodiments, the length of the drug holiday is between 2 days and 1 year, including by way of example only, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, 10 days, 12 days, 15 days, 20 days, 28 days, 35 days, 50 days, 70 days, 100 days, 120 days, 150 days, 180 days, 200 days, 250 days, 280 days, 300 days, 320 days, 350 days, and 365 days. The dose reduction during a drug holiday is, by way of example only, by 10%400%, including by way of example only 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, and 100%. In some embodiments, amlodipine oral liquid formulations described herein are administered chronically. For example, in some embodiments, an amlodipine oral liquid formulation is administered as a continuous dose, i.e., administered daily to a subject. In some other embodiments, amlodipine oral liquid formulations described herein are administered intermittently (e.g. drug holiday that includes a period of time in which the formulation is not administered or is administered in a reduced amount). In some embodiments, the amlodipine oral liquid formulation is administered to a subject who is in a fasted state. A fasted state refers to a subject who has gone without food or fasted for a certain period of time. General fasting periods include at least 4 hours, at least 6 hours, at least 8 hours, at least 10 hours, at least 12 hours, at least 14 hours and at least 16 hours without food. In some embodiments, an amlodipine oral liquid formulation is administered orally to a subject who is in a fasted state for at least 8 hours. In other embodiments, an amlodipine oral liquid formulation is administered to a subject who is in a fasted state for at least 10 hours. In yet other embodiments, an amlodipine oral liquid formulation is administered to a subject who is in a fasted state for at least 12 hours. In other embodiments, an amlodipine oral liquid formulation is administered to a subject who has fasted overnight. In other embodiments, the amlodipine oral liquid formulation is administered to a subject who is in a fed state. A fed state refers to a subject who has taken food or has had a meal. In certain embodiments, an amlodipine oral liquid formulation is administered to a subject in a fed state 5 minutes post-meal, 10 minutes post-meal, 15 minutes post-meal, 20 minutes post-meal, 30 minutes post-meal, 40 minutes post-meal, 50 minutes post-meal, 1 hour post-meal, or 2 hours post-meal. In certain instances, an amlodipine oral liquid formulation is administered to a subject in a fed state 30 minutes post-meal. In other instances, an amlodipine oral liquid formulation is administered to a subject in a fed state 1 hour post-meal. In yet further embodiments, an amlodipine oral liquid formulation is administered to a subject with food. In further embodiments described herein, an amlodipine oral liquid formulation is administered at a certain time of day for the entire administration period. For example, an amlodipine oral liquid formulation can be administered at a certain time in the morning, in the evening, or prior to bed. In certain instances, an amlodipine oral liquid formulation is administered in the morning. In other embodiments, an amlodipine oral liquid formulation can be administered at different times of the day for the entire administration period. For example, an amlodipine oral liquid formulation can be administered on 8:00 am in the morning for the first day, 12 pm noon for the next day or administration, 4 pm in the afternoon for the third day or administration, and so on. Combinations The treatment of certain diseases or conditions (e.g., hypertension, heart failure, myocardial infarction and the like) in a subject with an amlodipine oral liquid formulation described herein encompass additional therapies and treatment regimens with other agents in some embodiments. Such additional therapies and treatment regimens can include another therapy, e.g., additional anti-hypertensives, for treatment of the particular disease or condition in some embodiments. Alternatively, in other embodiments, additional therapies and treatment regimens include other agents used to treat adjunct conditions associated with the disease or condition or a side effect from the amlodipine oral liquid formulation in the therapy. Additional agents for use in combination with an amlodipine oral liquid formulation described herein include, but are not limited to, diuretics (loop, thiazide, potassium-sparing, and the like), beta blockers (metoprolol, propanolol, pronethalol, and the like), alpha blockers (phentolamine, phenoxybenzamine, tamsulosin, prazosin, and the like), mixed alpha and beta blockers (bucindolol, carvedilol, labetalol), calcium channel blockers (dihydropyridines such as nifedipine, etc., diltiazem, verapamil and the like), angiotensin II receptor antagonists (saralasin, losartan, eprosartin, irbesartan, valsartan, and the like), other ACE inhibitors (enalapril, captopril, quinapril, ramipril, lisinopril, zofenopril, and the like), aldosterone antagonists (eplerenone, spironolactone and the like), vasodilators (hydralazine and the like) and alpha-2 agonists (clonidine, moxonidine, guanabenz and the like). Certain Definitions Unless defined otherwise, all technical and scientific terms used herein have the same meanings as commonly understood by one of ordinary skill in the art. Although any methods and materials similar or equivalent to those described herein can be used in the practice or testing of embodiments described herein, certain preferred methods, devices, and materials are now described. As used herein and in the appended claims, the singular forms “a”, “an”, and “the” include plural reference unless the context clearly dictates otherwise. Thus, for example, reference to “an excipient” is a reference to one or more excipients and equivalents thereof known to those skilled in the art, and so forth. The term “about” is used to indicate that a value includes the standard level of error for the device or method being employed to determine the value. The use of the term “or” in the claims is used to mean “and/or” unless explicitly indicated to refer to alternatives only or the alternatives are mutually exclusive, although the disclosure supports a definition that refers to only alternatives and to “and/or.” The terms “comprise,” “have” and “include” are open-ended linking verbs. Any forms or tenses of one or more of these verbs, such as “comprises,” “comprising,” “has,” “having,” “includes” and “including,” are also open-ended. For example, any method that “comprises,” “has” or “includes” one or more steps is not limited to possessing only those one or more steps and also covers other unlisted steps. “Optional” or “optionally” may be taken to mean that the subsequently described structure, event or circumstance may or may not occur, and that the description includes instances where the events occurs and instances where it does not. As used herein, the term “therapeutic” means an agent utilized to treat, combat, ameliorate, prevent or improve an unwanted condition or disease of a patient. In some embodiments, a therapeutic agent such as amlodipine is directed to the treatment and/or the amelioration of, reversal of, or stabilization of the symptoms of hypertension described herein. “Administering” when used in conjunction with a therapeutic means to administer a therapeutic systemically or locally, as directly into or onto a target tissue, or to administer a therapeutic to a patient whereby the therapeutic positively impacts the tissue to which it is targeted. Thus, as used herein, the term “administering”, when used in conjunction with an amlodipine formulation, can include, but is not limited to, providing an amlodipine formulation into or onto the target tissue; providing an amlodipine formulation systemically to a patient by, e.g., oral administration whereby the therapeutic reaches the target tissue or cells. “Administering” a formulation may be accomplished by injection, topical administration, and oral administration or by other methods alone or in combination with other known techniques. The term “animal” as used herein includes, but is not limited to, humans and non-human vertebrates such as wild, domestic and farm animals. As used herein, the terms “patient,” “subject” and “individual” are intended to include living organisms in which certain conditions as described herein can occur. Examples include humans, monkeys, cows, sheep, goats, dogs, cats, mice, rats, and transgenic species thereof. In a preferred embodiment, the patient is a primate. In certain embodiments, the primate or subject is a human. In certain instances, the human is an adult. In certain instances, the human is child. In further instances, the human is 12 years of age or younger. In certain instances, the human is elderly. In other instances, the human is 60 years of age or older. Other examples of subjects include experimental animals such as mice, rats, dogs, cats, goats, sheep, pigs, and cows. The experimental animal can be an animal model for a disorder, e.g., a transgenic mouse with hypertensive pathology. A patient can be a human suffering from hypertension, or its variants or etiological forms. By “pharmaceutically acceptable”, it is meant the carrier, diluent or excipient must be compatible with the other ingredients of the formulation and not deleterious to the recipient thereof. The term “pharmaceutical composition” shall mean a composition comprising at least one active ingredient, whereby the composition is amenable to investigation for a specified, efficacious outcome in a mammal (for example, without limitation, a human). Those of ordinary skill in the art will understand and appreciate the techniques appropriate for determining whether an active ingredient has a desired efficacious outcome based upon the needs of the artisan. A “therapeutically effective amount” or “effective amount” as used herein refers to the amount of active compound or pharmaceutical agent that elicits a biological or medicinal response in a tissue, system, animal, individual or human that is being sought by a researcher, veterinarian, medical doctor or other clinician, which includes one or more of the following: (1) preventing the disease; for example, preventing a disease, condition or disorder in an individual that may be predisposed to the disease, condition or disorder but does not yet experience or display the pathology or symptomatology of the disease, (2) inhibiting the disease; for example, inhibiting a disease, condition or disorder in an individual that is experiencing or displaying the pathology or symptomatology of the disease, condition or disorder (i.e., arresting further development of the pathology and/or symptomatology), and (3) ameliorating the disease; for example, ameliorating a disease, condition or disorder in an individual that is experiencing or displaying the pathology or symptomatology of the disease, condition or disorder (i.e., reversing the pathology and/or symptomatology). As such, a non-limiting example of a “therapeutically effective amount” or “effective amount” of a formulation of the present disclosure may be used to inhibit, block, or reverse the activation, migration, or proliferation of cells or to effectively treat hypertension or ameliorate the symptoms of hypertension. The terms “treat,” “treated,” “treatment,” or “treating” as used herein refers to both therapeutic treatment in some embodiments and prophylactic or preventative measures in other embodiments, wherein the object is to prevent or slow (lessen) an undesired physiological condition, disorder or disease, or to obtain beneficial or desired clinical results. For the purposes described herein, beneficial or desired clinical results include, but are not limited to, alleviation of symptoms; diminishment of the extent of the condition, disorder or disease; stabilization (i.e., not worsening) of the state of the condition, disorder or disease; delay in onset or slowing of the progression of the condition, disorder or disease; amelioration of the condition, disorder or disease state; and remission (whether partial or total), whether detectable or undetectable, or enhancement or improvement of the condition, disorder or disease. Treatment includes eliciting a clinically significant response without excessive levels of side effects. Treatment also includes prolonging survival as compared to expected survival if not receiving treatment. A prophylactic benefit of treatment includes prevention of a condition, retarding the progress of a condition, stabilization of a condition, or decreasing the likelihood of occurrence of a condition. As used herein, “treat,” “treated,” “treatment,” or “treating” includes prophylaxis in some embodiments. The terms “precipitate,” “precipitates,” or “precipitation” as used herein, refers to the creation of a new solid phase comprising one or more chemical entities from solution. Those of ordinary skill in the art will understand and appreciate that the solid phase may exist in crystalline and/or amorphous forms and that crystalline forms may include, but are not limited to, polymorphs, cocrystals, ionic cocrystals, ionic cocrystal solvates, salts, solvated salts and solvates. The terms “substantially precipitate,” “substantially precipitates” or “substantial precipitation” as used herein, refers to an amount of precipitation that is detectable, directly or indirectly, by techniques known to a person of ordinary skill in the art. Examples of techniques may include, but are not limited to, visual inspection of solutions to determine changes in solution opaqueness/transparency, Focused Beam Reflectance Measurement (FBRM) technology, Infrared Spectroscopy, Raman Spectroscopy, UV spectroscopy and turbidity analysis. The terms “very slightly soluble” or “practically insoluble” as used herein, refers to a concentration of less than about 0.6 mg/mL, preferably of less than about 0.2 mg/mL, and most preferably of less than about 0.05 mg/mL. EXAMPLES Example 1. Formation of Amlodipine Salt Crystals in the Absence or Presence of a Magnetic Stir Bar (1A) Purified water (200 ml) was added to a 400 ml glass container fitted with overhead rotational stirring using a PTFE (polytetrafluoroethylene) coated 2″ diameter impeller and shaft. Stirring was initiated at 250 rpm and anhydrous citric acid (110 mg) was added and dissolved. Amlodipine besylate (278 mg) was then added followed by 1000 mg sodium benzoate. After 25 minutes, the stirring speed was increased to 450 rpm for 45 additional minutes. Results: No precipitate of amlodipine benzoate salt appeared until after 1 hour of stirring. The particles were large, >100 microns in length. (1B) The procedure in example (1A) was repeated with the exception that a magnetic stir bar was placed in the glass container in addition to the overhead stirrer. No external magnetic stirring apparatus was present, only the stir bar. The stirring speed was maintained at 250 rpm. Results: Amlodipine benzoate salt precipitated after 3 minutes of stirring. The particles were small, at <50 microns in length. (1C) Purified water (100 ml) was added to a 250 ml glass container fitted with overhead rotational stirring using a PTFE (polytetrafluoroethylene) coated 2″ diameter impeller and shaft. Stirring was initiated at 275 rpm and polysorbate 80 (1.0 grams) was added and dissolved. Amlodipine besylate (1.39 grams) was added and allowed to disperse, then sodium benzoate (5.0 grams) was added. The suspension was stirred for 30 minutes after the sodium benzoate addition then the stirring was stopped and a sample taken for microscopic evaluation. Results: A precipitate appeared in the suspension that was primarily large rod-shaped crystals, >100 microns in length. (1D) The procedure in example (1C) was repeated with the exception that a magnetic stir bar was placed in the glass container in addition to the overhead stirrer. No external magnetic stirring apparatus was present, only the stir bar. The overhead stirring speed was maintained at 275 rpm. Results: Amlodipine benzoate salt precipitated after ˜3 minutes of stirring. The particles were small and needle-shaped, at <50 microns in length. Example 2. Concentration Effect on Amlodipine Salt Crystal Formation with Non-Magnetic Stirring (2A) Purified water (50 ml) was added to a glass container fitted with overhead rotational stirring using a PTFE coated 2″ diameter impeller and shaft. Stirring was initiated at 250 rpm and 2500 mg sodium benzoate were added and dissolved. Amlodipine besylate (695 mg) was then added followed by 275 mg anhydrous citric acid. This solution is equivalent to preparing the crystals using a water amount of 10% of a final formulation weight. Results: Amlodipine benzoate salt began precipitating immediately as particles <˜50 micron. (2B) Purified water (150 ml) was added to a glass container fitted with overhead rotational stirring using a PTFE coated impeller and shaft. Stirring was initiated at 250 rpm and 2500 mg sodium benzoate were added and dissolved. Amlodipine besylate (695 mg) was then added followed by 275 mg anhydrous citric acid. This solution is equivalent to preparing the crystals using a water amount of 30% of a final formulation weight. Results: Amlodipine benzoate salt began precipitating immediately as particles <˜50 micron. (2C) Purified water (250 ml) was added to a glass container fitted with overhead rotational stirring using a PTFE coated impeller and shaft. Stirring was initiated at 250 rpm and 2500 mg sodium benzoate were added and dissolved. Amlodipine besylate (695 mg) was then added followed by 275 mg anhydrous citric acid. This solution is equivalent to preparing the crystals using a water amount of 50% of a final formulation weight. Results: Amlodipine benzoate salt began precipitating, then dissolved, and finally re-precipitated as large particles (>50 microns) after ˜1 hour. (2D) Purified water (45 ml) was added to a 250 ml glass container fitted with overhead rotational stirring using a PTFE coated 2″ diameter impeller and shaft. Stirring was initiated at 250 rpm and 500 mg of a 30% w/w simethicone powder were added and dissolved. Sodium benzoate (5000 mg) was added and dissolved and then amlodipine besylate (1390 mg in 5 ml water) was added. This solution is equivalent to preparing the crystals using a water amount of 5% of a final formulation weight. Results: Amlodipine benzoate salt precipitated immediately as very fine particles that caked on the stirrer and did not disperse easily. (2E) Purified water (90 ml) was added to a 250 mL HDPE container fitted with overhead rotational stirring using a PTFE coated 2″ diameter impeller and shaft. Stirring was initiated at 250 rpm and 500 mg of a 30% w/w simethicone powder were added and dissolved. Sodium benzoate (5000 mg) was added and dissolved and then amlodipine besylate (1390 mg in 10 ml water) was added. This solution is equivalent to preparing the crystals using a water amount of 10% of a final formulation weight. Results: Amlodipine benzoate salt precipitated rapidly as small particles that dispersed easily. (2F) Purified water (95 ml) was added to a 250 ml glass container fitted with overhead rotational stirring using a PTFE coated 2″ diameter impeller and shaft. Stirring was initiated at 250 rpm and 250 mg of a 30% w/w simethicone powder were added and dissolved. Sodium benzoate (2500 mg) was added and dissolved and then amlodipine besylate (695 mg in 5 mL water) was added. This solution is equivalent to preparing the crystals using a water amount of 20% of a final formulation weight. Results: Amlodipine benzoate salt precipitated rapidly as small particles with some agglomeration. Example 3 Amlodipine compositions were prepared using a process in which the preferred amlodipine salt is formed in one container, another part of the formulation was prepared in a second container, and the contents of the first container and the second container were combined. (3A) Purified water (approximately 10% of the final formulation weight) was added to a polyethylene first vessel (e.g., LLPD) fitted with magnetic stirring. Stirring was initiated and polysorbate 80 was added and dispersed in the solution. Amlodipine was then added with stirring until it was well dispersed, followed by the addition of the salt forming agent (e.g., sodium benzoate or sodium naphthalene-2-sulfonate). Stirring was continued for approximately 30 minutes after the addition of the salt forming agent. Purified water (approximately 80% of the final formulation weight) was added to a stainless steel second vessel fitted with overhead rotational stirring using a shaft and impeller. Stirring was initiated and the following components were added individually with sufficient stirring after each addition, to ensure each component was dissolved (citric acid, sodium citrate, sucralose, flavoring agent, hypromellose) or well dispersed (simethicone, silicon dioxide). High shear mixing was used during and after the addition of the hypromellose to facilitate dispersion and solubilization of this component. The contents of the first vessel were then transferred to the second vessel with stirring. Additional water was added to the second vessel to bring its weight to approximately 98% of the final formulation weight. The pH of the solution was measured and if required, adjusted to the desired pH, then the solution was brought to the final weight with purified water. (3B) Purified water (approximately 10% of the final formulation weight) was added to a glass vessel fitted with magnetic stirring. Stirring was initiated and simethicone was added and dispersed in the solution. The salt forming agent was then added and dissolved. Amlodipine was dispersed in purified water (approximately 1% of the final formulation weight) and the resulting liquid slowly added to the first vessel with stirring. Stirring was continued for approximately 30 minutes after the addition of the amlodipine. Purified water (approximately 22% of the final formulation weight) was added to a second glass vessel fitted with magnetic stirring. The water was heated to approximately 70° C. and silicone dioxide and hypromellose were added with stirring. The heating was discontinued and an equal portion of cold water was added to the second vessel. Stirring was continued and sucralose and flavor were added and dissolved. Purified water (approximately 6% of the final formulation weight) was then added. The solutions from the two vessels were combined with stirring. The vessels were rinsed with purified water (approximately 20% of the final formulation weight) and the rinses added to the formulation. The pH was checked, and as needed adjusted to pH 4.9 with a solution of citric acid (1.1 g anhydrous citric acid in 50 ml purified water). The solution was brought to final weight with purified water and mixed with high shear mixing. (3C) Purified water (approximately 10% of the final formulation weight) was added to a first glass vessel fitted with magnetic stirring. Stirring was initiated and one-half of the simethicone and nine-tenths of the salt forming agent were added. Amlodipine was then added over about 5 minutes. Stirring was continued for approximately 30 minutes after the addition of the amlodipine was completed. Purified water (approximately 70% of the final formulation weight) was added to a second glass vessel fitted with magnetic stirring. The remaining one-half of the simethicone, the remaining one-tenth of the salt forming agent, sucralose, silicon dioxide, flavor, and hypromellose were added to the vessel with stirring. High shear mixing was used after the addition of the hypromellose to facilitate dispersion and solubilization of this component. The contents of the first vessel were then transferred to the second vessel with stirring. Additional water was added to the second vessel to bring its weight to approximately 90% of the final formulation weight. The formulation was again subjected to high shear mixing, and then allowed to deaerate. The preparation was brought to final weight with purified water and mixed. The pH of the solution was measured and as required, adjusted to the desired pH with anhydrous citric acid. Example 4 Amlodipine compositions were prepared using a process in which the preferred amlodipine salt is formed in one container, and then transferred to a second container for the remaining process. Purified water (approximately 10% of the final formulation weight) was added to a HDPE vessel fitted with a magnetic stirrer. Stirring was initiated and simethicone was added and dispersed in the solution. The salt forming agent was then added with stirring followed by the addition of amlodipine dispersed in purified water (approximately 1% of the final formulation weight). Stirring was continued for approximately 30 minutes after the addition of the amlodipine. The preparation was transferred to a stainless steel vessel and additional purified water (approximately 45% of the final formulation weight) was added to the vessel. Stirring was initiated and the following components were added individually with stirring; citric acid, sucralose, silicon dioxide, flavor, and hypromellose. High shear mixing was used after the addition of the hypromellose to facilitate dispersion and solubilization. Purified water (30% of the final formulation weight) was added with stirring and the preparation was allowed to deaerate. The preparation was brought to final weight with purified water and mixed. The pH was measured. Example 5 Amlodipine compositions were prepared using processes in which the preferred amlodipine salt is formed in a small portion of the final volume in one container, and then additional components are added to the same container to complete the process. (5A) Purified water (approximately 10% of the final formulation weight) was added to a glass vessel fitted with magnetic stirring. Stirring was initiated and simethicone was added and dispersed in the solution. The salt forming agent was then added with stirring followed by the addition of amlodipine. Stirring was continued for approximately 30 minutes after the addition of the amlodipine. Additional purified water (approximately 85% of the final formulation weight) was added to the vessel. Stirring was initiated and the following components were added individually with stirring; citric acid, sodium citrate, sucralose, silicon dioxide, flavor, and hypromellose. High shear mixing was used after the addition of the hypromellose to facilitate dispersion and solubilization, then the preparation was allowed to deaerate. The pH was checked and adjusted if necessary, and the preparation was brought to final weight with purified water. (5B) Polysorbate 80 was added to a glass vessel fitted with magnetic stirring. Purified water (approximately 10% of the final formulation weight) was added and stirring was initiated to ensure dispersion of the polysorbate in the solution. Amlodipine was then added with stirring until it was well dispersed, followed by the addition of the salt forming agent. Stirring was continued for approximately 30 minutes after the addition of the salt forming agent. Additional purified water (approximately 85% of the final formulation weight) was added to the vessel. Stirring was initiated and the following components were added individually with stirring; citric acid, sodium citrate, sucralose, silicon dioxide, flavor, simethicone and hypromellose. High shear mixing was used after the addition of the hypromellose to facilitate dispersion and solubilization, then the preparation was allowed to deaerate. The pH was checked and adjusted if necessary, and the preparation was brought to final weight with purified water. Example 6 Amlodipine compositions were prepared using processes in which the preferred amlodipine salt is formed in one container in a volume greater than one-half of the final volume, and then additional components were added to the same container to complete the process. (6A) Purified water (approximately 90% of the final formulation weight) was added to a glass vessel fitted with magnetic stirring. Stirring was initiated and citric acid was added and dissolved in the solution, followed by amlodipine, followed by the salt forming agent. The solution was stirred for approximately 30 minutes to allow formation of the amlodipine salt. The solution was then cooled to 2-8° C. for 1 hour with continued stirring. Sucralose, silicon dioxide, simethicone, povidone for some formulations, and hypromellose were added with stirring. High shear mixing was applied to the formulation after the hypromellose addition. The formulation was then stirred for 30 minutes, brought to final weight with purified water, and stirred for another 30 minutes. (6B) Purified water (approximately 90% of the final formulation weight) was added to a glass vessel fitted with magnetic stirring. Stirring was initiated and citric acid was added and dissolved in the solution, followed by sodium citrate, amlodipine, then the salt forming agent. The solution was stirred for approximately 30 minutes to allow formation of the amlodipine salt. Sodium benzoate, sucralose, silicon dioxide, simethicone, (flavor and color in some formulations) and hypromellose were added with stirring. High shear mixing was applied to the formulation after the hypromellose addition. The formulation was then stirred for 30 minutes, brought to final weight with purified water, and stirred for another 30 minutes. (6C) Purified water (approximately 90% of the final formulation weight) was added to a glass vessel fitted with magnetic stirring. Stirring was initiated and citric acid was added and dissolved in the solution, followed by amlodipine, then the salt forming agent. The solution was stirred for approximately 30 minutes to allow formation of the amlodipine salt. The solution was then cooled to 2-8° C. for 1 hour with continued stirring. Sucralose, silicon dioxide, simethicone and povidone were added with stirring. The formulation was then stirred for 30 minutes, brought to final weight with purified water, and stirred for another 30 minutes. (6D) Purified water (approximately 90% of the final formulation weight) was added to a glass vessel fitted with magnetic stirring. Stirring was initiated and hypromellose was added and dissolved in the water with high shear mixing. Citric acid, salt forming agent, sucralose, simethicone, flavoring agent and color in some preparations, were then added with stirring. The solution was brought to its final weight with purified water, and the amlodipine was added with stirring. The solution was stirred for approximately 30 minutes to allow formation of the amlodipine salt. (6E) Purified water (approximately 90% of the final formulation weight) was added to a glass vessel fitted with magnetic stirring. Stirring was initiated and mannitol was added and dissolved in the solution, followed by hypromellose, citric acid, salt forming agent, sucralose, simethicone, silicon dioxide, and in some formulations, a flavor. The solution was brought to its final weight with purified water, and the amlodipine was added with stirring. In some preparations, the formulation was subjected to ultrasonic energy (sonication) and in some preparations the formulation was mixed with high shear mixing. The solution was then stirred for approximately 30 minutes to allow formation of the amlodipine salt. Example A: Effect of pH on the Formation of Degradants in Amlodipine Formulations Formulations were prepared containing Amlodipine according to Table A-1. Each formulation was dispensed into screw-capped high density polyethylene (HDPE) bottles and stored at both 5° C. and ambient temperature. Samples were removed periodically and analyzed by a stability indicating high performance liquid chromatography (HPLC) method for content of amlodipine and any degradants. The HPLC method provided separation of amlodipine, amlodipine degradants and formulation components on a C18 column with a gradient program using mobile phases containing 0.1% trifluoroacetic acid (TFA) in water, and 0.1% TFA in acetonitrile flowing at 1 mL/min. Detection was by UV absorbance at 237 nm for amlodipine and its degradants. Any unknown impurities were reported by their relative retention time (RRT) to amlodipine. TABLE A-1 Composition (in mg/ml) of Amlodipine Formulations at Varying pH Levels Formulation Component A1 A2 A3 A4 A5 A6 A7 A8 Amlodipine besylatea 1.39 1.39 1.39 1.39 1.39 1.39 1.39 1.39 Mannitol 90.00 — — — — — — — Hypromellose K750 5.00 — — — — — — — Citric acid, anhydrous 3.42 1.35 0.84 0.53 0.36 0.31 0.23 0.17 Sodium citrate, dihydrate — — — — — 0.36 0.47 0.55 Sodium benzoate 5.00 5.00 5.00 5.00 5.00 5.00 5.00 5.00 Sucralose/maltodextrin 4.00 — — — — — — — Sucralose — 0.70 0.70 0.70 0.70 0.70 0.70 0.70 Simethicone 0.15 0.15 0.15 0.15 0.15 0.15 0.15 0.15 Silicon dioxide 0.50 0.50 0.50 0.50 0.50 0.50 0.50 0.50 Artificial cherry flavor — 0.50 0.50 0.50 0.50 0.50 0.50 0.50 Hypromellose K1500 — 5.00 5.00 5.00 5.00 5.00 5.00 5.00 Water q.s. q.s. q.s. q.s. q.s. q.s. q.s. q.s. pH 3.98 4.51 4.71 4.90 5.09 5.31 5.54 5.75 a= equivalent to 1 mg/ml Amlodipine The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at 5° C. are provided in Table A-2. The results show a decrease in total impurities as pH is increased from 4.0 to 5.7. TABLE A-2 Assay and Primary Degradants Present in the Formulations Formulation Weeks A1 A2 A3 A4 A5 A6 A7 A8 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.00 100.00 100.00 4 97.77 96.61 99.30 99.99 100.96 99.20 101.11 96.49 8 97.47 97.32 104.37 100.07 101.33 100.58 98.10 97.04 12 97.88 97.41 102.28 102.09 101.88 100.59 100.74 96.38 26 95.14 97.02 100.80 99.69 105.89 102.46 102.01 98.37 52 96.02 97.16 100.08 101.26 101.94 100.40 99.96 97.34 78 98.24 98.37 101.86 100.40 101.93 107.40 99.59 99.08 104 97.32 98.02 99.66 109.83 102.00 101.79 100.25 97.37 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.06 0.02 0.03 0.00 0.03 0.00 0.00 0.00 4 0.08 0.05 0.03 0.04 0.04 0.00 0.02 0.04 8 0.12 0.01 0.01 0.01 0.01 0.04 0.01 0.03 12 0.13 0.17 0.02 0.02 0.03 0.05 0.02 0.04 26 0.15 0.04 0.04 0.04 0.05 0.05 0.04 0.04 52 0.15 0.07 0.06 0.06 0.06 0.07 0.06 0.06 78 0.27 0.08 0.07 0.07 0.06 0.10 0.06 0.07 104 0.33 0.06 0.05 0.04 0.04 0.05 0.04 0.04 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.02 0.00 0.00 0.00 0.00 0.00 0.00 0.00 4 0.02 0.00 0.01 0.00 0.00 0.01 0.00 0.00 8 0.06 0.02 0.02 0.01 0.01 0.00 0.00 0.00 12 0.04 0.04 0.03 0.02 0.02 0.01 0.01 0.01 26 0.07 0.08 0.07 0.05 0.04 0.04 0.03 0.02 52 0.11 0.13 0.13 0.12 0.10 0.09 0.06 0.04 78 0.16 0.21 0.20 0.18 0.15 0.14 0.10 0.06 104 0.22 0.26 0.25 0.24 0.20 0.18 0.13 0.08 Total Impurities (wt % of Amlodipine) Initial 0.23 0.07 0.06 0.03 0.08 0.06 0.06 0.08 4 0.28 0.11 0.09 0.09 0.08 0.04 0.06 0.14 8 0.66 0.09 0.09 0.07 0.09 0.07 0.06 0.10 12 0.35 0.34 0.12 0.08 0.09 0.10 0.07 0.09 26 0.42 0.25 0.21 0.18 0.17 0.15 0.12 0.10 52 0.64 0.41 0.35 0.31 0.33 0.33 0.26 0.24 78 0.84 0.53 0.46 0.38 0.33 0.40 0.27 0.25 104 1.07 0.65 0.61 0.51 0.44 0.36 0.31 0.28 The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at ambient temperature are provided in Table A-3. The results show a decrease in total impurities as pH is increased from 4.0 to 5.7. TABLE A-3 Assay and Primary Degradants Present in the Formulations Formulation Weeks A1 A2 A3 A4 A5 A6 A7 A8 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.00 100.00 100.00 32 89.38 98.81 102.36 99.31 102.33 102.05 101.23 101.34 4 90.71 97.05 99.80 100.54 105.81 101.27 99.14 98.06 6 85.22 95.86 102.42 101.22 100.86 102.45 100.42 97.03 8 83.75 97.13 99.80 101.38 103.48 101.81 100.14 101.44 12 79.33 96.28 100.33 100.61 103.18 101.61 100.90 97.50 26 — 91.68 96.97 98.87 101.72 101.53 100.27 99.20 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.06 0.02 0.03 0.00 0.03 0.00 0.00 0.00 2 0.30 0.05 0.05 0.05 0.04 0.03 0.01 0.04 4 0.43 0.08 0.08 0.07 0.07 0.06 0.06 0.06 6 0.65 0.05 0.05 0.03 0.04 0.10 0.05 0.05 8 0.79 0.05 0.04 0.03 0.04 0.10 0.17 0.09 12 1.03 0.06 0.05 0.05 0.04 0.14 0.12 0.13 26 — 0.27 0.21 0.20 0.18 0.26 0.23 0.24 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.02 0.00 0.00 0.00 0.00 0.00 0.00 0.00 2 0.29 0.12 0.10 0.07 0.05 0.03 0.03 0.01 4 0.43 0.25 0.20 0.15 0.11 0.07 0.05 0.04 6 0.58 0.33 0.28 0.22 0.16 0.13 0.10 0.06 8 0.67 0.40 0.35 0.29 0.22 0.18 0.11 0.07 12 0.73 0.47 0.43 0.38 0.32 0.25 0.17 0.10 26 — 0.51 0.48 0.45 0.41 0.37 0.30 0.21 Total Impurities (wt % of Amlodipine) Initial 0.23 0.07 0.06 0.03 0.08 0.06 0.06 0.08 2 1.19 0.32 0.29 0.23 0.17 0.15 0.09 0.13 4 1.78 0.60 0.49 0.39 0.37 0.24 0.24 0.30 6 2.41 0.75 0.62 0.50 0.39 0.47 0.37 0.30 8 2.43 0.94 0.75 0.60 0.53 0.50 0.49 0.36 12 3.77 1.29 0.94 0.76 0.73 0.72 0.58 0.49 26 — 1.85 1.47 1.23 1.18 1.21 1.05 0.95 Example B. Effect of Benzoate Concentration on the Stability of Amlodipine Formulations Formulations were prepared containing Amlodipine according to Table B-1. Each formulation was dispensed into screw-capped HDPE bottles and stored at ambient temperature. Formulations B6, B7, and B8 were also stored at 5° C. Samples were removed periodically and analyzed using the HPLC method in Example A. TABLE B-1 Composition (in mg/ml) of Amlodipine Formulations at Varying Benzoate Levels Formulation Component B1 B2 B3 B4 B5 B6 B7 B8 Amlodipine besylatea 1.39 1.39 1.39 1.39 1.39 1.39 1.39 1.39 Hypromellose K750 — — — — — 5.00 5.00 5.00 Citric acid, anhydrous b b b b b 0.55 0.90 1.15 Sodium benzoate 1.00 2.00 3.00 4.00 5.00 5.00 7.50 10.00 Sucralose 0.70 0.70 0.70 0.70 0.70 0.70 0.70 0.70 Simethicone 0.15 0.15 0.15 0.15 0.15 0.15 0.15 0.15 Silicon dioxide 0.50 0.50 0.50 0.50 0.50 — — — Artificial cherry flavor 0.50 0.50 0.50 0.50 0.50 — — 0.50 Hypromellose K1500 5.00 5.00 5.00 5.00 5.00 — — — Red 40 Al lake color — — — — — — — 90.015 Water q.s. q.s. q.s. q.s. q.s. q.s. q.s. q.s. pH 4.85 4.89 4.89 4.89 4.89 4.88 4.84 4.87 a= equivalent to 1 mg/ml Amlodipine b adjusted pH to 4.9 with a solution containing 1.1 g citric acid in 50 ml purified water before final dilution. The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at 5° C. are provided in Table B-2. TABLE B-2 Assay and Primary Degradants Present in the Formulations Formulation Weeks B6 B7 B8 Amlodipine (% initial) Initial 100.00 100.00 100.00 2 97.56 99.22 98.15 4 97.18 98.00 98.18 6 99.13 99.04 97.28 8 98.81 98.44 98.17 12 99.17 98.80 98.80 26 99.89 97.03 97.42 52 96.34 98.04 97.19 78 98.10 99.20 99.07 104 97.33 98.59 97.56 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.03 0.00 0.04 2 0.03 0.02 0.02 4 0.02 0.03 0.03 6 0.03 0.02 0.02 8 0.03 0.04 0.03 12 0.04 0.03 0.02 26 0.05 0.03 0.04 52 0.04 0.03 0.03 78 0.11 0.09 0.09 104 0.13 0.10 0.10 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 2 0.00 0.00 0.00 4 0.01 0.01 0.01 6 0.02 0.01 0.01 8 0.02 0.02 0.01 12 0.05 0.04 0.03 26 0.10 0.08 0.07 52 0.19 0.15 0.12 78 0.28 0.25 0.21 104 0.35 0.32 0.27 Total Impurities (wt % of Amlodipine) Initial 0.10 0.09 0.15 2 0.08 0.08 0.07 4 0.07 0.07 0.07 6 0.10 0.07 0.09 8 0.10 0.09 0.08 12 0.13 0.11 0.10 26 0.22 0.17 0.17 52 0.37 0.30 0.24 78 0.54 0.44 0.39 104 0.73 0.58 0.52 The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at ambient temperature are provided in Table B-3. TABLE B-3 Assay and Primary Degradants Present in the Formulations Formulation Weeks B1 B2 B3 B4 B5 B6 B7 B8 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.00 100.00 100.00 2 98.98 105.36 100.82 97.67 100.22 98.62 98.70 99.05 4 97.06 104.08 99.24 95.90 97.91 96.01 98.44 97.90 6 96.31 103.13 99.36 97.32 97.01 97.10 97.89 97.37 8 96.51 103.91 99.54 96.90 96.84 97.04 97.26 97.39 12 96.38 95.78 95.40 26 92.69 95.34 94.49 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.05 0.04 0.03 0.03 0.03 0.03 0.00 0.04 2 0.17 0.10 0.08 0.07 0.07 0.05 0.04 0.05 4 0.22 0.12 0.10 0.08 0.07 0.09 0.07 0.08 6 0.28 0.15 0.11 0.10 0.08 0.12 0.09 0.09 8 0.32 0.16 0.13 0.11 0.12 0.12 0.11 0.11 12 0.16 0.14 0.13 26 0.24 0.23 0.22 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 2 0.07 0.08 0.09 0.09 0.08 0.09 0.13 0.12 4 0.19 0.19 0.19 0.18 0.19 0.22 0.28 0.25 6 0.28 0.28 0.28 0.26 0.26 0.33 0.38 0.36 8 0.34 0.33 0.34 0.34 0.33 0.40 0.47 0.44 12 0.51 0.55 0.55 26 0.60 0.63 0.63 Total Impurities (wt % of Amlodipine) Initial 0.22 0.08 0.06 0.07 0.09 0.10 0.09 0.15 2 0.59 0.40 0.43 0.39 0.35 0.26 0.27 0.29 4 0.80 0.59 0.56 0.55 0.45 0.48 0.52 0.48 6 0.99 0.70 0.63 0.60 0.57 0.69 0.70 0.65 8 1.11 0.83 0.72 0.70 0.72 0.81 0.89 0.80 12 1.06 1.05 1.07 26 1.45 1.54 1.50 Example C. Effect of Hypromellose on the Formation of Degradants in Amlodipine Formulations Formulations were prepared containing Amlodipine according to Table C-1. Each formulation was dispensed into screw-capped HDPE bottles and stored at both 5° C. and ambient temperature. Samples were removed periodically and analyzed using the HPLC method in Example A. TABLE C-1 Composition (in mg/ml) of Amlodipine Formulations with Varying Hypromellose Content Formulation Component C1 C2 C3 C4 C5 C6 C7 C8 Amlodipine besylate a 1.39 1.39 1.39 1.39 1.39 1.39 1.39 1.39 Hypromellose K750 3.00 5.00 7.50 7.50 — — — — Citric acid, anhydrous 0.55 0.55 0.55 0.55 0.55 0.55 0.55 0.55 Sodium benzoate 5.00 5.00 5.00 5.00 5.00 5.00 5.00 5.00 Sucralose 0.70 0.70 0.70 0.70 0.70 0.70 0.70 0.70 Simethicone 0.15 0.15 0.15 0.15 0.15 0.15 0.15 0.15 Silicon dioxide 0.50 0.50 0.50 0.50 0.50 0.50 0.50 Artificial cherry flavor — — — 0.50 — 0.50 — 0.50 Hypromellose K1500 — — — — 3.00 5.00 7.50 7.50 Water q.s. q.s. q.s. q.s. q.s. q.s. q.s. q.s. pH 4.88 4.88 4.86 4.89 4.88 4.88 4.87 4.91 a = equivalent to 1 mg/ml Amlodipine The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at 5° C. are provided in Table C-2. TABLE C-2 Assay and Primary Degradants Present in the Formulations Formulation Weeks C1 C2 C3 C4 C5 C6 C7 C8 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.00 100.00 100.00 4 100.00 97.18 99.17 98.39 97.30 98.96 97.08 98.08 8 100.49 98.81 99.23 98.67 96.88 98.32 96.76 98.17 12 99.72 99.17 100.27 99.57 95.76 98.49 97.42 98.95 26 99.46 99.89 98.00 98.64 92.35 97.30 96.94 97.96 52 95.73 96.34 98.91 99.67 96.59 100.29 97.44 96.27 78 98.78 98.10 98.74 99.14 99.39 97.91 97.48 95.92 104 97.56 97.33 98.54 97.56 95.74 96.98 97.94 99.09 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.01 0.03 0.01 0.16 0.02 0.10 0.02 0.11 4 0.01 0.02 0.03 0.17 0.02 0.11 0.03 0.10 8 0.03 0.03 0.03 0.21 0.02 0.11 0.04 0.12 12 0.03 0.04 0.04 0.21 0.03 0.10 0.04 0.11 26 0.02 0.05 0.05 0.26 0.03 0.11 0.06 0.15 52 0.06 0.04 0.07 0.35 0.06 0.14 0.07 0.20 78 0.06 0.11 0.11 0.41 0.07 0.18 0.10 0.24 104 0.09 0.13 0.11 0.32 0.09 0.13 0.13 0.19 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 4 0.00 0.01 0.01 0.00 0.00 0.00 0.01 0.00 8 0.01 0.02 0.02 0.02 0.01 0.02 0.02 0.01 12 0.03 0.05 0.03 0.02 0.03 0.02 0.04 0.02 26 0.06 0.10 0.06 0.07 0.06 0.06 0.08 0.06 52 0.11 0.19 0.13 0.15 0.09 0.12 0.14 0.15 78 0.18 0.28 0.25 0.26 0.14 0.19 0.23 0.24 104 0.21 0.35 0.35 0.34 0.18 0.23 0.32 0.31 Total Impurities (wt % of Amlodipine) Initial 0.05 0.10 0.14 0.27 0.06 0.18 0.22 0.21 4 0.07 0.07 0.08 0.28 0.08 0.16 0.10 0.16 8 0.08 0.10 0.10 0.34 0.06 0.20 0.10 0.22 12 0.10 0.13 0.12 0.35 0.10 0.21 0.14 0.23 26 0.16 0.22 0.18 0.51 0.16 0.29 0.25 0.34 52 0.25 0.37 0.31 0.74 0.24 0.42 0.33 0.55 78 0.44 0.54 0.49 1.00 0.37 0.58 0.51 0.76 104 0.46 0.73 0.61 1.02 0.44 0.65 0.63 0.80 The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at ambient temperature are provided in Table C-3. TABLE C-3 Assay and Primary Degradants Present in the Formulations Formulation Weeks C1 C2 C3 C4 C5 C6 C7 C8 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.00 100.00 100.00 2 100.27 98.62 100.25 103.21 97.02 100.83 97.57 102.18 4 96.72 96.01 99.88 99.64 96.57 97.86 97.00 98.33 6 100.45 97.10 — 100.18 96.32 98.48 — 98.24 8 99.82 97.04 99.93 99.68 96.12 97.16 95.71 97.90 12 98.33 96.38 98.93 96.31 95.40 97.05 96.84 96.80 26 96.35 92.69 96.55 94.46 92.50 94.29 94.39 93.84 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.01 0.03 0.01 0.16 0.02 0.10 0.02 0.11 2 0.03 0.05 0.08 0.27 0.03 0.12 0.07 0.16 4 0.05 0.09 0.10 0.35 0.04 0.14 0.09 0.20 6 0.06 0.12 — 0.47 0.05 0.19 — 0.24 8 0.09 0.12 0.13 0.56 0.06 0.21 0.12 0.32 12 0.08 0.16 0.17 0.73 0.08 0.29 0.16 0.40 26 0.16 0.24 0.26 1.30 0.16 0.50 0.25 0.70 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 0.00 0.00 0.00 0.00 0.00 2 0.05 0.09 0.10 0.08 0.05 0.07 0.09 0.08 4 0.13 0.22 0.20 0.19 0.12 0.17 0.17 0.19 6 0.20 0.33 — 0.30 0.17 0.24 — 0.29 8 0.24 0.40 0.40 0.41 0.21 0.30 0.33 0.37 12 0.32 0.51 0.58 0.58 0.26 0.38 0.49 0.50 26 0.38 0.60 0.89 0.91 0.30 0.47 0.69 0.69 Total Impurities (wt % of Amlodipine) Initial 0.05 0.10 0.14 0.27 0.06 0.18 0.22 0.21 2 0.16 0.26 0.26 0.50 0.16 0.36 0.23 0.44 4 0.34 0.48 0.43 0.80 0.31 0.52 0.37 0.60 6 0.41 0.69 — 1.10 0.42 0.69 — 0.79 8 0.54 0.81 0.72 1.44 0.53 0.87 0.64 1.06 12 0.70 1.06 1.02 1.90 0.66 1.15 0.94 1.40 26 1.02 1.45 1.64 3.40 1.00 1.97 1.44 2.45 Example D. Effect of Povidone on the Formation of Degradants in Amlodipine Formulations Formulations were prepared containing Amlodipine according to Table D-1. Each formulation was dispensed into screw-capped HDPE bottles and stored at both 5° C. and ambient temperature. Samples were removed periodically and analyzed using the HPLC method in Example A. TABLE D-1 Composition (in mg/ml) of Amlodipine Formulations with Varying Povidone Content Formulation Component D1 D2 D3 D4 D5 D6 Amlodipine besylate a 1.39 1.39 1.39 1.39 1.39 1.39 Hypromellose K750 — — — — — 3.00 Citric acid, anhydrous 0.90 0.90 0.90 0.55 0.43 0.55 Sodium benzoate 7.50 7.50 7.50 5.00 3.00 5.00 Sucralose 0.70 0.70 0.70 0.70 0.70 0.70 Simethicone — — — — — 0.15 Silicon dioxide 0.50 0.50 0.50 0.50 0.50 0.50 K-90 Povidone 10.00 20.00 30.00 30.00 30.00 10.00 Water q.s. q.s. q.s. q.s. q.s. q.s. pH 4.87 4.89 4.92 4.96 4.83 4.91 a = equivalent to 1 mg/ml Amlodipine The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at 5° C. are provided in Table D-2. TABLE D-2 Assay and Primary Degradants Present in the Formulations Formulation Weeks D1 D2 D3 D4 D5 D6 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.00 4 95.19 99.46 99.87 99.23 101.99 97.83 8 96.51 98.13 99.21 96.18 102.95 99.57 12 96.40 96.19 97.81 91.38 101.78 97.16 26 97.22 98.13 100.19 100.70 97.51 100.40 52 94.66 96.70 99.27 89.30 93.84 99.65 78 96.81 98.79 99.53 98.55 89.66 100.84 104 94.89 99.34 99.50 98.92 94.48 97.93 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.03 0.06 0.05 0.06 0.03 0.02 4 0.07 0.04 0.06 0.06 0.05 0.04 8 0.04 0.07 0.06 0.07 0.07 0.05 12 0.05 0.06 0.05 0.06 0.06 0.08 26 0.04 0.03 0.07 0.08 0.09 0.05 52 0.04 0.04 0.06 0.08 0.07 0.07 78 0.05 0.06 0.07 0.09 0.11 0.08 104 0.07 0.07 0.08 0.11 0.12 0.09 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 0.00 0.00 0.00 4 0.00 0.00 0.00 0.00 0.00 0.00 8 0.00 0.00 0.00 0.00 0.00 0.01 12 0.00 0.00 0.00 0.00 0.00 0.01 26 0.00 0.00 0.01 0.01 0.02 0.05 52 0.01 0.01 0.02 0.02 0.03 0.10 78 0.01 0.02 0.03 0.04 0.05 0.14 104 0.02 0.03 0.04 0.05 0.07 0.21 Total Impurities (wt % of Amlodipine) Initial 0.09 0.11 0.10 0.09 0.07 0.07 4 0.11 0.08 0.10 0.12 0.10 0.08 8 0.10 0.14 0.10 0.12 0.12 0.10 12 0.18 0.17 0.21 0.12 0.13 0.14 26 0.11 0.16 0.18 0.16 0.19 0.16 52 0.17 0.15 0.24 0.16 0.20 0.21 78 0.14 0.16 0.20 0.20 0.28 0.31 104 0.18 0.20 0.23 0.31 0.33 0.43 The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at ambient temperature are provided in Table D-3. TABLE D-3 Assay and Primary Degradants Present in the Formulations Formulation Weeks D1 D2 D3 D4 D5 D6 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.00 2 94.21 97.15 98.15 91.04 99.93 99.36 4 95.69 97.67 99.15 99.49 99.87 97.93 6 95.18 97.15 97.20 97.49 101.11 98.11 8 94.74 96.16 96.17 98.99 98.59 99.38 12 91.38 95.07 95.50 97.35 96.85 96.51 26 93.65 92.14 93.58 96.84 92.72 96.77 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.03 0.06 0.05 0.06 0.03 0.02 2 0.06 0.07 0.08 0.12 0.10 0.10 4 0.07 0.08 0.08 0.12 0.13 0.10 6 0.08 0.11 0.10 0.16 — 0.12 8 0.08 0.10 0.12 0.17 0.17 0.15 12 0.10 0.15 0.13 0.21 0.25 0.18 26 0.16 0.21 0.26 0.34 0.44 0.31 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 0.00 0.00 0.00 2 0.00 0.01 0.02 0.01 0.01 0.05 4 0.02 0.03 0.05 0.04 0.05 0.13 6 0.03 0.04 0.06 0.06 — 0.20 8 0.04 0.06 0.08 0.08 0.08 0.25 12 0.04 0.07 0.09 0.09 0.10 0.32 26 0.05 0.10 0.13 0.13 0.14 0.41 Total Impurities (wt % of Amlodipine) Initial 0.09 0.11 0.10 0.09 0.07 0.07 2 0.17 0.19 0.20 0.25 0.26 0.24 4 0.27 0.26 0.31 0.37 0.44 0.38 6 0.30 0.36 0.38 0.48 — 0.50 8 0.25 0.47 0.49 0.51 0.64 0.61 12 0.48 0.60 0.60 0.60 0.74 0.70 26 0.59 0.82 1.07 1.29 1.83 1.47 Example E. Formulations Containing 2-Naphthalene Sulfonate Salt Form of Amlodipine Formulations were prepared containing Amlodipine according to Table E-1. Each formulation was dispensed into screw-capped HDPE bottles and stored at both ambient temperature and 40° C. Samples were removed periodically and analyzed using the HPLC method in Example A. TABLE E-1 Composition (in mg/ml) of Amlodipine Formulations Formulation Component E1 E2 E3 Amlodipine besylatea 1.39 1.39 1.39 Sodium 2-naphthalene sulfonate 1.13 1.13 2.26 Citric acid, anhydrous 0.31 0.31 0.31 Sodium citrate 0.42 0.42 0.42 Sodium benzoate 1.00 1.00 1.00 Sucralose 0.70 0.70 0.70 Simethicone 0.15 0.15 0.15 Silicon dioxide 0.50 0.50 0.50 Artificial cherry flavor — 0.50 — Red 40 Al lake color — 0.015 — Hypromellose K750 5.00 5.00 5.00 Water q.s. q.s. q.s. pH 5.09 5.10 5.08 a= equivalent to 1 mg/ml Amlodipine The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at ambient temperature are provided in Table E-2. TABLE E-2 Assay and Primary Degradants Present in the Formulations Formulation Weeks E1 E2 E3 Amlodipine (% initial) Initial 100.00 100.00 100.00 4 98.82 99.90 100.13 8 98.02 99.22 99.78 12 98.62 99.66 99.76 26 97.56 98.86 99.99 52 98.80 100.17 99.51 78 98.46 100.15 100.21 104 98.36 100.38 102.36 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.06 0.03 0.02 4 0.04 0.04 0.04 8 0.04 0.04 0.04 12 0.05 0.05 0.06 26 0.09 0.07 0.08 52 0.14 0.12 0.14 78 0.21 0.17 0.16 104 0.26 0.22 0.22 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 4 0.01 0.01 0.00 8 0.02 0.02 0.00 12 0.03 0.03 0.01 26 0.06 0.07 0.03 52 0.13 0.13 0.05 78 0.18 0.19 0.07 104 0.23 0.24 0.09 Total Impurities (wt % of Amlodipine) Initial 0.31 0.51 0.45 4 0.10 0.10 0.08 8 0.10 0.09 0.13 12 0.12 0.12 0.12 26 0.23 0.26 0.17 52 0.42 0.36 0.36 78 0.50 0.48 0.31 104 0.69 0.60 0.54 The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at 40° C. are provided in Table E-3. TABLE E-3 Assay and Primary Degradants Present in the Formulations Formulation Weeks E1 E2 E3 Amlodipine (% initial) Initial 100.00 100.00 100.00 2 98.23 98.65 98.59 4 98.20 98.67 99.41 8 95.28 97.08 97.82 12 94.44 95.59 97.12 26 87.62 90.88 91.30 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.06 0.03 0.02 2 0.13 0.12 0.12 4 0.20 0.19 0.19 8 0.42 0.33 0.44 12 0.67 0.47 0.87 26 1.95 1.06 5.18 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 2 0.11 0.12 0.05 4 0.19 0.20 0.09 8 0.32 0.33 0.15 12 0.38 0.39 0.20 26 0.41 0.41 0.20 Total Impurities (wt % of Amlodipine) Initial 0.31 0.51 0.45 2 0.40 0.41 0.32 4 0.63 0.66 0.53 8 1.20 1.10 1.06 12 1.80 1.78 1.83 26 4.07 3.21 8.22 Example F. Stability of Amlodipine Formulations Prepared by Two-Container, One-Container, and Pharmacy Compounding Processes Formulation F6 was prepared by crushing 50 commercially available 5 mg amlodipine besylate tablets (Norvasc®, Pfizer Labs) with a mortar and pestle. A small amount of Ora-Blend (Paddock Laboratories, Inc.) was triturated with the resulting powder, and then more Ora-Blend was added geometrically with mixing. The suspension was transferred to a graduated cylinder and the mortar was rinsed with Ora-Blend. The rinse was added to the cylinder then additional Ora-Blend was added to reach a final volume of 250 ml and the suspension was mixed. Formulations F1, F2, and F3 were prepared according to example 5B (one-container) and formulations F4 and F5 were prepared according to example 3A (two-container). Each formulation was dispensed into screw-capped HDPE bottles and stored at both 5° C. and ambient temperature. Samples were removed periodically and analyzed using the HPLC method in Example A. TABLE F-1 Composition (in mg/mL) of Amlodipine Formulations Formulation Component F1 F2 F3 F4 F5 F6 Amlodipine besylate a 1.39 1.39 1.39 1.39 1.39 50 tablets Citric acid, anhydrous 0.31 0.31 0.31 0.31 0.31 — Sodium citrate, anhydrous 0.36 0.36 0.36 0.36 0.36 — Sodium benzoate 5.00 5.00 5.00 5.00 5.00 — Sucralose 0.70 0.70 0.70 0.70 0.70 — Simethicone 0.15 0.15 0.15 0.15 0.15 — Silicon dioxide 0.50 0.50 0.50 0.50 0.50 — Artificial cherry flavor 0.50 0.50 0.50 0.50 — — Polysorbate 80 0.50 1.00 2.00 1.00 1.00 — 0Hypromellose K1500 5.00 5.00 5.00 7.50 7.50 — Water q.s. q.s. q.s. q.s. q.s. — Ora-Blend ™ — — — — — q.s. to 250 ml pH 5.31 5.33 5.35 5.35 5.36 4.64 a = equivalent to 1 mg/ml Amlodipine The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at 5° C. are provided in Table F-2. TABLE F-2 Assay and Primary Degradants Present in the Formulations Formulation Weeks F1 F2 F3 F4 F5 F6 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.0 2 99.23 100.74 99.17 — 101.85 — 4 — — — 100.37 101.69 100.3 6 98.98 101.53 99.72 — 101.09 — 8 99.70 100.86 99.06 101.12 101.40 97.2 12 98.98 100.49 98.91 100.35 101.12 26 101.14 100.91 100.20 100.26 52 99.69 100.87 99.85 101.52 78 97.82 99.94 98.94 101.72 104 99.74 99.90 98.19 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.04 0.06 0.04 0.01 0.00 1.34 2 0.00 0.00 0.01 — 0.02 — 4 — — — 0.01 0.03 0.71 6 0.04 0.02 0.02 — 0.03 — 8 0.01 0.02 0.02 0.03 0.05 1.24 12 0.03 0.02 0.02 0.10 0.04 26 0.05 0.06 0.06 0.05 52 0.04 0.04 0.05 0.07 78 0.06 0.05 0.06 0.04 104 0.04 0.04 0.06 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 0.00 0.00 0.00 2 0.00 0.00 0.00 — 0.00 — 4 — — — 0.00 0.00 0.00 6 0.00 0.00 0.00 — 0.01 — 8 0.00 0.00 0.00 0.01 0.01 0.00 12 0.01 0.00 0.01 0.02 0.03 26 0.04 0.04 0.04 0.05 52 0.09 0.09 0.11 0.11 78 0.14 0.15 0.16 0.20 104 0.19 0.20 0.22 Total Impurities (wt % of Amlodipine) Initial 0.09 0.14 0.11 0.04 0.00 1.76 2 0.04 0.03 0.06 — 0.06 — 4 — — — 0.04 0.08 1.00 6 0.07 0.05 0.06 — 0.09 — 8 0.05 0.06 0.07 0.06 0.08 1.52 12 0.08 0.05 0.06 0.19 0.09 26 0.12 0.13 0.14 0.13 52 0.23 0.22 0.29 0.31 78 0.42 0.40 0.45 0.43 104 0.41 0.44 0.53 The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at ambient temperature are provided in Table F-3. TABLE F-3 Assay and Primary Degradants Present in the Formulations Formulation Weeks F1 F2 F3 F4 F5 F6 Amlodipine (% initial) Initial 100.00 100.00 100.00 100.00 100.00 100.0 2 100.65 100.52 99.57 101.16 100.89 97.7 4 — — — 99.99 100.41 102.1 6 100.23 100.42 98.78 100.38 100.47 94.3 8 99.16 100.28 98.99 102.38 100.68 90.6 12 99.71 99.46 98.52 100.53 99.44 26 98.13 98.53 97.24 97.27 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.04 0.06 0.04 0.01 0.00 1.34 2 0.05 0.04 0.05 0.04 0.05 1.62 4 — — — 0.05 0.06 2.24 6 0.06 0.06 0.07 0.09 0.08 2.78 8 0.07 0.06 0.08 0.10 0.11 3.24 12 0.10 0.09 0.10 0.15 0.13 26 0.18 0.17 0.18 0.24 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 0.00 0.00 0.00 2 0.03 0.03 0.04 0.03 0.04 0.03 4 — — — 0.06 0.10 0.05 6 0.12 0.13 0.13 0.11 0.13 0.09 8 0.17 0.17 0.17 0.17 0.18 0.11 12 0.23 0.23 0.24 0.28 0.30 26 0.36 0.35 0.36 0.49 Total Impurities (wt % of Amlodipine) Initial 0.09 0.14 0.11 0.04 0.00 1.76 2 0.16 0.16 0.17 0.10 0.18 2.09 4 — — — 0.24 0.37 3.09 6 0.39 0.38 0.43 0.38 0.50 4.20 8 0.46 0.48 0.52 0.51 0.64 5.05 12 0.69 0.68 0.76 0.85 1.02 26 1.26 1.38 1.47 1.65 Example G. Effect of pH, Preservatives, and Hypromellose on Stability of Amlodipine Benzoate Formulations at Accelerated Temperatures Formulations were prepared containing Amlodipine according to Table G-1. Each formulation was dispensed into screw-capped HDPE bottles and stored at 60° C. Samples were removed periodically and analyzed using the HPLC method in Example A. TABLE G-1 Composition (in mg/mL) of Amlodipine Formulations Formulation Component G1 G2 G3 G4 G5 G6 G7 G8 Amlodipine besylate a 1.39 1.39 1.39 1.39 1.39 1.39 1.39 1.39 Citric acid, anhydrous 11.66 0.33 0.71 — — — 0.31 0.31 Sodium citrate, anhydrous — 0.35 — — — — 0.36 0.36 Phosphoric acid — — — 0.96 0.67 0.39 — — Sodium benzoate 5.0 5.0 5.0 5.0 5.0 5.0 5.0 5.0 Sucralose 0.7 0.7 0.7 0.7 0.7 0.7 0.7 0.7 Methylparaben sodium — — 1.72 1.72 1.72 1.72 — — Propylparaben sodium — — 0.17 0.17 0.17 0.17 — — Simethicone 0.15 0.15 0.15 0.15 0.15 0.15 0.15 0.15 Silicon dioxide 0.5 0.5 0.5 0.5 0.5 0.5 0.5 0.5 Artificial cherry flavor 0.5 0.5 0.5 0.5 0.5 0.5 — — Polysorbate 80 1.0 1.0 1.0 1.0 1.0 1.0 1.0 1.0 Hypromellose K1500 5.0 5.0 5.0 5.0 5.0 5.0 7.5 10.0 Water q.s. q.s. q.s. q.s. q.s. q.s. q.s. q.s pH 3.0 5.3 6.4 6.4 7.2 8.0 5.4 5.4 a = equivalent to 1 mg/ml Amlodipine The results of the HPLC analysis for amlodipine and the main degradants in the samples are provided in Table G-2. TABLE G-2 Assay and Primary Degradants Present in the Formulations Formulation Hours G1 G2 G3 G4 G5 G6 G7 G8 Amlodipine (% initial) 0 100.00 100.00 100.00 100.00 100.00 100.00 100.00 100.00 16 79.51 94.37 93.87 92.75 91.50 85.26 — — 17 — — — — — — 93.42 96.47 36 — — — — — — 90.28 — 40 66.39 91.31 91.68 92.04 85.87 75.43 — — 52 — — — — — — 87.31 89.50 USP Impurity A/EP Impurity D (wt % of Amlodipine) 0 0.20 0.03 0.03 0.03 0.06 0.03 0.03 0.01 16 2.39 0.16 0.14 0.24 0.24 0.21 — — 17 — — — — — — 0.18 0.18 36 — — — — — — 0.29 — 40 4.24 0.29 0.21 0.35 0.34 0.35 — — 52 — — — — — — 0.58 0.50 Impurity RRT 0.97 (wt % of Amlodipine) 0 0.00 0.00 0.00 0.00 0.00 0.00 0.04 0.00 16 0.37 0.16 0.07 0.03 0.04 0.05 — — 17 — — — — — — 0.21 0.20 36 — — — — — — 0.44 — 40 0.52 0.30 0.15 0.08 0.08 0.13 — — 52 0.54 0.62 Total Impurities (wt % of Amlodipine) 0 0.48 0.08 0.19 0.23 0.43 0.72 0.10 0.08 16 7.86 1.36 1.38 1.18 2.06 3.22 — — 17 — — — — — — 1.43 1.41 36 — — — — — — 3.12 — 40 14.22 2.79 2.53 2.41 3.88 5.94 — — 52 — — — — — — 4.82 4.65 Example H. Effect of pH and Preservatives on Stability of Amlodipine Naphthalene Sulfonate Formulations at Accelerated Temperatures Formulations were prepared containing Amlodipine according to Table H-1. Each formulation was dispensed into screw-capped HDPE bottles and stored at 60° C. Samples were removed periodically and analyzed using the HPLC method in Example A. TABLE H-1 Composition (in mg/mL) of Amlodipine Formulations Formulation Component H1 H2 H3 H4 H5 H6 Amlodipine besylate a 1.39 1.39 1.39 1.39 1.39 1.39 Citric acid, anhydrous 2.92 0.73 0.28 — — — Sodium citrate, anhydrous — — 0.41 — — — Phosphoric acid — — — 1.28 0.85 0.30 Dibasic sodium phosphate, — — — 0.31 — 0.18 heptahydrate Sodium benzoate 1.0 1.0 1.0 — — — Sodium 2-naphthalene sulfonate 1.13 1.13 1.13 1.13 1.13 1.13 Sucralose 0.7 0.7 0.7 0.7 0.7 0.7 Methylparaben sodium — — — 1.72 1.72 1.72 Propylparaben sodium — — — 0.17 0.17 0.17 Simethicone 0.15 0.15 0.15 0.15 0.15 0.15 Silicon dioxide 0.5 0.5 0.5 0.5 0.5 0.5 Artificial cherry flavor 0.5 0.5 0.5 0.5 0.5 0.5 Polysorbate 80 1.0 1.0 1.0 1.0 1.0 1.0 Hypromellose K1500 5.0 5.0 5.0 5.0 5.0 5.0 Water q.s. q.s. q.s. q.s. q.s. q.s. pH 3.0 4.0 5.0 5.9 6.9 7.9 The results of the HPLC analysis for amlodipine and the main degradants in the samples are provided in Table H-2. TABLE H-2 Assay and Primary Degradants Present in the Formulations Formulation Hours H1 H2 H3 H4 H5 H6 Amlodipine (% initial) 0 100.00 100.00 100.00 100.00 100.00 100.00 16 90.01 96.31 97.94 99.10 99.76 92.65 40 69.77 85.46 90.42 95.03 91.15 65.16 USP Impurity A/EP Impurity D (wt % of Amlodipine) 0 0.07 0.03 0.04 0.08 0.06 0.23 16 1.44 0.33 0.14 0.37 0.42 0.40 40 4.98 2.65 1.01 0.88 0.75 1.14 Impurity RRT 0.97 (wt % of Amlodipine) 0 0.00 0.00 0.00 0.00 0.00 0.00 16 0.15 0.20 0.11 0.00 0.02 0.05 40 0.38 0.52 0.31 0.02 0.07 0.05 Total Impurities (wt % of Amlodipine) 0 0.13 0.09 0.25 1.09 2.92 5.57 16 3.44 1.17 0.81 1.76 3.04 13.64 40 10.82 5.76 3.39 3.21 6.92 35.53 Example I. Effect of Crystallization Time on the Formation of Amlodipine Salts A formulation was prepared in a polyethylene vessel with magnetic stirring. Purified water (33.5 kg) was added to the vessel and stirring was initiated. Polysorbate 80 (350 g) was added to the vessel along with a 500 g aliquot of purified water used to rinse the polysorbate container. The solution was stirred for 10 minutes. Amlodipine Besylate (485.5 g) was then added to the vessel along with a 500 g aliquot of purified water used to rinse the amlodipine container. The solution was stirred for 5 minutes then 1750 g of sodium benzoate were added to the container. Samples were taken from the formulation every five minutes for an hour, filtered through 0.2 micron filters to isolate only the soluble amlodipine, and analyzed by HPLC for amlodipine content. The results of the HPLC analysis for the free amlodipine fraction are provided in FIG. 1. Example J. Stability of Formulations Using Avicel RC-591 as the Suspending Agent Formulations were prepared containing Amlodipine according to Table J-1. Each formulation was dispensed into screw-capped HDPE bottles and stored at both 5° C. and 25° C. Samples were removed periodically and analyzed using the HPLC method in Example A. TABLE J-1 Composition (in mg/ml) of Amlodipine Formulations Formulation Component J1 J2 J3 Amlodipine besylatea 1.39 1.39 1.39 Citric acid, anhydrous 0.31 0.31 0.31 Sodium citrate 0.36 0.36 0.36 Sodium benzoate 5.00 5.00 5.00 Sucralose 0.70 0.70 0.70 Simethicone 0.15 0.15 0.15 Artificial cherry flavor 0.50 0.50 0.50 Polysorbate 80 0.50 0.50 0.50 Avicel ® RC-591 7.5 10.00 15.00 Water q.s. q.s. q.s. pH 5.36 5.33 5.34 a= equivalent to 1 mg/ml Amlodipine The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at 5° C. are provided in Table J-2. TABLE J-2 Assay and Primary Degradants Present in the Formulations Formulation Weeks J1 J2 J3 Amlodipine (% initial) Initial 100.00 100.00 100.00 2 98.80 96.18 96.45 4 99.03 96.35 96.89 6 100.53 99.32 98.52 8 98.71 96.96 96.77 12 97.58 96.75 96.00 26 99.24 98.27 97.90 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.02 0.02 0.04 2 0.03 0.03 0.02 4 0.04 0.04 0.06 6 0.02 0.02 0.04 8 0.03 0.03 0.05 12 0.02 0.03 0.03 26 0.04 0.06 0.07 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 2 0.00 0.00 0.00 4 0.00 0.00 0.00 6 0.00 0.00 0.00 8 0.00 0.00 0.00 12 0.00 0.00 0.00 26 0.01 0.01 0.01 Total Impurities (wt % of Amlodipine) Initial 0.09 0.09 0.14 2 0.14 0.16 0.10 4 0.12 0.14 0.14 6 0.09 0.10 0.09 8 0.16 0.13 0.18 12 0.16 0.18 0.18 26 0.18 0.22 0.18 The results of the HPLC analysis for amlodipine and the main degradants in the samples stored at 25° C. are provided in Table J-3. TABLE J-3 Assay and Primary Degradants Present in the Formulations Formulation Weeks J1 J2 J3 Amlodipine (% initial) Initial 100.00 100.00 100.00 2 99.27 97.16 96.52 4 98.94 97.73 96.89 6 99.61 98.81 98.20 8 97.34 96.91 95.85 12 95.57 95.48 93.25 26 95.39 93.67 92.65 USP Impurity A/EP Impurity D (wt % of Amlodipine) Initial 0.02 0.02 0.04 2 0.05 0.04 0.06 4 0.06 0.04 0.06 6 0.08 0.05 0.06 8 0.05 0.06 0.08 12 0.06 0.07 0.09 26 0.09 0.09 0.13 Impurity RRT 0.97 (wt % of Amlodipine) Initial 0.00 0.00 0.00 2 0.01 0.01 0.01 4 0.02 0.02 0.03 6 0.03 0.03 0.03 8 0.03 0.03 0.04 12 0.03 0.03 0.04 26 0.03 0.03 0.04 Total Impurities (wt % of Amlodipine) Initial 0.09 0.09 0.14 2 0.20 0.27 0.28 4 0.38 0.39 0.42 6 0.52 0.55 0.59 8 0.69 0.73 0.83 12 0.96 1.11 1.15 26 1.64 1.37 1.98 Example K. Clinical Trial: Bioavailability Study of 5 mg Amlodipine Oral Suspension Vs. Norvasc® 5 mg Tablets Under Fasted Conditions The objective of this single dose open-label, randomized, two-period, two-treatment crossover study was to compare the relative oral bioavailability of a test formulation of 5 mL of amlodipine oral suspension, 1 mg/mL (formulation F4), to an equivalent oral dose of the commercially available comparator product, Norvasc® (amlodipine besylate) 5 mg tablet, when administered under fasted conditions in healthy adults. Study design: Ten healthy adult subjects received a single 5 mL dose of amlodipine oral suspension, 1 mg/mL, formulation F4 (Treatment A), in one period and a separate single dose of Norvasc® (amlodipine besylate) 5 mg tablet (Treatment B) in another period. Each treatment was administered after an overnight fast of at least 10 hours, followed by a 4-hour fast postdose. During each period, blood samples were obtained prior to and following each dose at selected times through 168 hours postdose. Pharmacokinetic parameters were calculated for each formulation using non-compartmental methods. Statistical Methods: The concentration-time data were analyzed using noncompartmental methods in Phoenix™ WinNonlin® (Version 6.3, Pharsight Corporation). Concentration-time data that were below the limit of quantitation (BLQ) were treated as zero in the data summarization and descriptive statistics. In the pharmacokinetic analysis, BLQ concentrations were treated as zero from time-zero up to the time at which the first quantifiable concentration was observed; embedded and/or terminal BLQ concentrations were treated as “missing”. Actual sample times were used for all pharmacokinetic and statistical analyses. Analysis of variance (ANOVA) and the Schuirmann's two one-sided t-test procedures at the 5% significance level were applied to the log-transformed pharmacokinetic exposure parameters, Cmax, AUClast, and AUCinf. The 90% confidence interval for the ratio of the geometric means (Test/Reference) was calculated. Bioequivalence was declared if the lower and upper confidence intervals (CIs) of the log-transformed parameters were within 80% to 125%. Results: A total of 10 subjects participated in the study and 8 of these subjects completed both study periods. Based on the geometric mean ratios of amlodipine AUCs (AUClast and AUCinf), the bioavailability of the amlodipine oral suspension (formulation F4) relative to the Norvasc® tablet was approximately 103% to 104%. The geometric mean ratio of amlodipine Cmax was approximately 100%. The 90% CI for comparing the maximum exposure to amlodipine, based on ln (Cmax), was within the accepted 80% to 125% limits. The 90% CIs for comparing total systemic exposure to amlodipine, based on ln (AUClast) and ln (AUCinf), was within the accepted 80% to 125% limits. Therefore, the 5 mL test formulation of amlodipine oral suspension, 1 mg/mL, is bioequivalent to the reference product, Norvasc® (amlodipine besylate) tablet, 5 mg, under fasted conditions. Example L. Characterization of Amlodipine Benzoate A suspension was prepared by adding 0.50 g of NuSil Med-342 simethicone (30% simethicone) to 90 mL water in a glass beaker with stirring. Sodium benzoate (5.00 g) was added to the suspension and dissolved. Amlodipine besylate (1.40 g) was added to 10 mL water, then the amlodipine suspension was added to the benzoate suspension over 2-4 minutes. The resulting suspension was mixed for 30 minutes at ambient temperature. The solids were collected on filter paper and washed with ˜150 mL cold water in 15 mL portions. The solid was dried under vacuum for 1 hour, then dried in a desiccator for 18 hours. A portion of the solids were weighed and dissolved in water/HPLC diluent and the resulting solution was analyzed by a validated HPLC procedure for the presence of amlodipine and benzoic acid. The resulting molar ratio of benzoic acid:amlodipine in the solid was calculated as 1.00:1.05 demonstrating the formation of amlodipine benzoate. Example M. Solubility of Amlodipine Besylate and Amlodipine Benzoate in the Presence of Added Sodium Benzoate Amlodipine benzoate was prepared by adding 1.39 g amlodipine besylate to 100 ml purified water in a glass container. Five grams of sodium benzoate were then added and the solution was stirred for 30 minutes at ambient temperature. The resulting suspension was vacuum filtered through #1 Whatman filter paper to collect the insoluble fraction. The collected solids were rinsed with ten separate 15 mL increments (150 mL total) of 1-5° C. degree water. The solids were dried on the vacuum filtration apparatus for 1 hour then dried overnight in a desiccator. Fifteen milliliter polypropylene centrifuge tubes were set up in duplicate as shown in Table M-1. Amlodipine besylate or amlodipine benzoate was added to each tube in amounts in excess of the anticipated solubility. Ten milliliter aliquots of water, or water with varying amounts of sodium benzoate were added to each tube. The pH of each tube was adjusted to 5.3 with the addition of citric acid. The tubes were capped and mixed by inversion for 5 days to allow the suspensions to equilibrate. After the equilibration time, the tubes were opened and immediately filtered through 0.45 micron nylon filters. The clear filtrates were analyzed according to the method in Example A. The results of the HPLC analysis for the amounts of amlodipine in solution are presented in FIG. 2. TABLE M-1 Composition of Solubility Study Tubes Duplicate Tube Set Component J1 J2 J3 J4 J5 J6 Amlodipine besylate (mg) 50 — — — — — Amlodipine benzoate (mg) — 50 50 50 50 50 Citric acid, anhydrous (mg) Amount as needed to achieve pH 5.3 Sodium benzoate (mg) 0 0 2 10 30 50 Water (mL) 10 10 10 10 10 10 Measured pH 5.3 5.3 5.3 5.3 5.3 5.3 While preferred embodiments of the present invention have been shown and described herein, it will be obvious to those skilled in the art that such embodiments are provided by way of example only. Numerous variations, changes, and substitutions will now occur to those skilled in the art without departing from the invention. It should be understood that various alternatives to the embodiments of the invention described herein may be employed in practicing the invention. It is intended that the following claims define the scope of the invention and that methods and structures within the scope of these claims and their equivalents be covered thereby."},"background":{"kind":"string","value":"<SOH> BACKGROUND OF THE INVENTION <EOH>Hypertension, or high blood pressure, is a serious health issue in many countries. According to the National Heart Blood and Lung Institute, it is thought that about 1 in 3 adults in the United States alone have hypertension. Left unchecked, hypertension is considered a substantial risk factor for cardiovascular and other diseases including coronary heart disease, myocardial infarction, congestive heart failure, stroke and kidney failure. Hypertension is classified as primary (essential) hypertension or secondary hypertension. Primary hypertension has no known cause and may be related to a number of environmental, lifestyle and genetic factors such as stress, obesity, smoking, inactivity and sodium intake. Secondary hypertension can be caused by drug or surgical interventions or by abnormalities in the renal, cardiovascular or endocrine system. A number of antihypertensive drugs are available for treating hypertension. Various therapeutic classes of antihypertensive drugs include alpha-adrenergic blockers, beta-adrenergic blockers, calcium-channel blockers, hypotensives, mineralcorticoid antagonists, central alpha-agonists, diuretics and rennin-angiotensin-aldosterone inhibitors which include angiotensin II receptor antagonists (ARB) and angiotensin-converting enzyme (ACE) inhibitors. Angiotensin-converting enzyme (ACE) inhibitors inhibit angiotensin-converting enzyme (ACE), a peptidyl dipeptidase that catalyzes angiotension I to angiotension II, a potent vasoconstrictor involved in regulating blood pressure. Amlodipine is a calcium channel blocker. It affects the movement of calcium into the cells of the heart and blood vessels. As a result, amlodipine relaxes blood vessels and increases the supply of blood and oxygen to the heart while reducing its workload. The structural formula of amlodipine is as follows: Amlodipine is currently administered in the form of oral tablets, (e.g., Norvasc) or in the form of a refrigerated liquid formulation. In addition to the treatment of hypertension, amlodipine tablets have been used for coronary artery disease (CAD) such as chronic stable angina, vasospastic angina, or angiographically documented coronary artery disease in patients without heart failure or an ejection fraction <40%."},"summary":{"kind":"string","value":"<SOH> SUMMARY OF THE INVENTION <EOH>Disclosed herein is an oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the amlodipine benzoate is formed in situ. In some embodiments of an oral liquid formulation, the amlodipine benzoate is formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate with a molar excess of sodium benzoate. In some embodiments of an oral liquid formulation, the salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate is selected from amlodipine besylate, amlodipine tosylate, amlodipine mesylate, amlodipine succinate, amlodipine salicylate, amlodipine maleate, amlodipine acetate, and amlodipine hydrochloride. In some embodiments of an oral liquid formulation, the amlodipine benzoate is formed by the reaction of amlodipine besylate with a molar excess of sodium benzoate. In some embodiments of an oral liquid formulation, the formulation further comprises a flavoring agent. In some embodiments of an oral liquid formulation, the formulation further comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of an oral liquid formulation, the formulation is in the form of a suspension. In some embodiments of an oral liquid formulation, the pH of the formulation is between about 3 and about 8. In some embodiments of an oral liquid formulation, the pH is between about 4 and about 5. In some embodiments of an oral liquid formulation, the pH is between about 5 and about 6. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 24 months. Also disclosed herein is a method of treating hypertension in a subject comprising administering to that subject an oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of a method of treating hypertension, the amlodipine benzoate is formed in situ. In some embodiments of a method of treating hypertension, the amlodipine benzoate is formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate with a molar excess of sodium benzoate. In some embodiments of a method of treating hypertension, the salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate is selected from amlodipine besylate, amlodipine tosylate, amlodipine mesylate, amlodipine succinate, amlodipine salicylate, amlodipine maleate, amlodipine acetate, and amlodipine hydrochloride. In some embodiments of a method of treating hypertension, the amlodipine benzoate is formed by the reaction of amlodipine besylate with a molar excess of sodium benzoate. In some embodiments of a method of treating hypertension, the formulation further comprises a flavoring agent. In some embodiments of a method of treating hypertension, the formulation further comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of a method of treating hypertension, the formulation is in the form of a suspension. In some embodiments of a method of treating hypertension, the pH of the formulation is between about 3 and about 8. In some embodiments of a method of treating hypertension, the pH is between about 4 and about 5. In some embodiments of a method of treating hypertension, the pH is between about 5 and about 6. In some embodiments of a method of treating hypertension, the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of a method of treating hypertension, the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of a method of treating hypertension, the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of a method of treating hypertension, the formulation is stable at about 5±5° C. for at least 24 months. In some embodiments of a method of treating hypertension, the hypertension is primary (essential) hypertension. In some embodiments of a method of treating hypertension, the hypertension is secondary hypertension. In some embodiments of a method of treating hypertension, the subject has blood pressure values greater than or equal to 140/90 mmm Hg. In some embodiments of a method of treating hypertension, the subject is an adult. In some embodiments of a method of treating hypertension, the subject is elderly. In some embodiments of a method of treating hypertension, the subject is a child. In some embodiments of a method of treating hypertension, the formulation is administered to the subject in a fasted state. In some embodiments of a method of treating hypertension, the formulation is administered to the subject in a fed state. In some embodiments of a method of treating hypertension, the formulation is further administered in combination with an agent selected from the group consisting of diuretics, beta blockers, alpha blockers, mixed alpha and beta blockers, calcium channel blockers, angiotensin II receptor antagonists, ACE inhibitors, aldosterone antagonists, and alpha-2 agonists. Also disclosed herein is a method of treating Coronary Artery Disease (CAD) in a subject comprising administering to that subject an oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the amlodipine benzoate is formed in situ. In some embodiments of a method of treating Coronary Artery Disease (CAD), the amlodipine benzoate is formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate with a molar excess of sodium benzoate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate is selected from amlodipine besylate, amlodipine tosylate, amlodipine mesylate, amlodipine succinate, amlodipine salicylate, amlodipine maleate, amlodipine acetate, and amlodipine hydrochloride. In some embodiments of a method of treating Coronary Artery Disease (CAD), the amlodipine benzoate is formed by the reaction of amlodipine besylate with a molar excess of sodium benzoate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation further comprises a flavoring agent. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation further comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is in the form of a suspension. In some embodiments of a method of treating Coronary Artery Disease (CAD), the pH of the formulation is between about 3 and about 8. In some embodiments of a method of treating Coronary Artery Disease (CAD), the pH is between about 4 and about 5. In some embodiments of a method of treating Coronary Artery Disease (CAD), the pH is between about 5 and about 6. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is stable at about 5±5° C. for at least 24 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the Coronary Artery Disease (CAD) is chronic stable angina, vasospastic angina, or angiographically documented coronary artery disease. In some embodiments of a method of treating Coronary Artery Disease (CAD), the angiographically documented coronary artery disease is in patients without heart failure or an ejection fraction <40%. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is further administered in combination with an additional anti-anginal agent. Disclosed herein is an oral liquid formulation, comprising: (i) a pharmaceutically acceptable salt of amlodipine; (ii) a buffer; (iii) water; and (iv) optionally one or more agents selected from the group consisting of preservatives, flavoring agents, sweetening agents, surfactants, suspensions aids, and antifoaming agents; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments of an oral liquid formulation, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments of an oral liquid formulation, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed by the reaction of a pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate or amlodipine naphthalene sulfonate with a molar excess of a salt forming agent. In some embodiments of an oral liquid formulation, the pharmaceutically acceptable salt of amlodipine that is more soluble in aqueous media than amlodipine benzoate or amlodipine naphthalene sulfonate is amlodipine besylate. In some embodiments of an oral liquid formulation, the salt forming agent is sodium benzoate. In some embodiments of an oral liquid formulation, the amount of sodium benzoate as the salt forming agent is about 1.0 mg/ml to about 10.0 mg/ml. In some embodiments of an oral liquid formulation, the salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments of an oral liquid formulation, the amount of sodium naphthalene-2-sulfonate as the salt forming agent is about 0.5 mg/ml to about 2.5 mg/ml. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises a surfactant. In some embodiments of an oral liquid formulation, the surfactant is polysorbate 80. In some embodiments of an oral liquid formulation, the amount of the surfactant is about 0.1 mg/ml to about 2.5 mg/ml. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises a preservative. In some embodiments of an oral liquid formulation, the preservative is selected from the group consisting of sodium benzoate, a paraben or paraben salt, and combinations thereof. In some embodiments of an oral liquid formulation, the amount of preservative is about 0.1 mg/ml to about 2.0 mg/ml. In some embodiments of an oral liquid formulation, the buffer comprises a citrate buffer. In some embodiments of an oral liquid formulation, the citrate buffer concentration is about 3 mM. In some embodiments of an oral liquid formulation, the buffer comprises a phosphate buffer. In some embodiments of an oral liquid formulation, the phosphate buffer concentration is about 3 mM. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises a suspension aid. In some embodiments of an oral liquid formulation, the suspension aid comprises silicon dioxide, hydroxypropyl methylcellulose, methylcellulose, microcrystalline cellulose, carboxymethylcellulose sodium, polyvinylpyrrolidone, or combinations thereof. In some embodiments of an oral liquid formulation, the suspension aid is silicon dioxide. In some embodiments of an oral liquid formulation, the amount of silicon dioxide is about 0.1 mg/ml to about 1.0 mg/ml. In some embodiments of an oral liquid formulation, the suspension aid is hydroxypropyl methylcellulose. In some embodiments of an oral liquid formulation, the amount of hydroxypropyl methylcellulose is about 3 mg/ml to about 10 mg/ml. In some embodiments of an oral liquid formulation, the suspension aid is a combination of silicon dioxide and hydroxypropyl methylcellulose. In some embodiments of an oral liquid formulation, the amount of silicon dioxide is about 0.1 mg/ml to about 1.0 mg/ml and the amount of hydroxypropyl methylcellulose is about 3 mg/ml to about 10 mg/ml. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises an antifoaming agent. In some embodiments of an oral liquid formulation, the antifoaming agent is simethicone. In some embodiments of an oral liquid formulation, the amount of the antifoaming agent is about 0.05 mg/ml to about 1.0 mg/ml. In some embodiments of an oral liquid formulation, the formulation comprises a flavoring agent. In some embodiments of an oral liquid formulation, the oral liquid formulation comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of an oral liquid formulation, the oral liquid formulation further comprises unreacted salt forming agent. In some embodiments of an oral liquid formulation, the oral liquid formulation is in the form of a suspension. In some embodiments of an oral liquid formulation, the pH of the oral liquid formulation is between about 3 and about 8. In some embodiments of an oral liquid formulation, the pH is between about 4 and about 5. In some embodiments of an oral liquid formulation, the pH is between about 5 and about 6. In some embodiments of an oral liquid formulation, the amount of the pharmaceutically acceptable salt of amlodipine corresponds to about 0.8 mg/ml to about 1.2 mg/ml of amlodipine free base. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 24 months. Also disclosed herein is an oral liquid formulation, comprising: (i) a pharmaceutically acceptable salt of amlodipine in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) optionally about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments of an oral liquid formulation, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments of an oral liquid formulation, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed by the reaction of amlodipine besylate with a molar excess of a salt forming agent. In some embodiments of an oral liquid formulation, the salt forming agent is sodium benzoate. In some embodiments of an oral liquid formulation, the amount of sodium benzoate as the salt forming agent is about 1.0 mg/ml to about 10.0 mg/ml. In some embodiments of an oral liquid formulation, the salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments of an oral liquid formulation, the amount of sodium naphthalene-2-sulfonate as the salt forming agent is about 0.5 mg/ml to about 2.5 mg/ml. In some embodiments of an oral liquid formulation, the formulation further comprises a flavoring agent. In some embodiments of an oral liquid formulation, the formulation further comprises a sweetener. In some embodiments of an oral liquid formulation, the sweetener is sucralose. In some embodiments of an oral liquid formulation, the oral liquid formulation further comprises unreacted salt forming agent. In some embodiments of an oral liquid formulation, the formulation is in the form of a suspension. In some embodiments of an oral liquid formulation, the pH of the formulation is between about 3 and about 8. In some embodiments of an oral liquid formulation, the pH is between about 4 and about 5. In some embodiments of an oral liquid formulation, the pH is between about 5 and about 6. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 12 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 25±5° C. for at least 24 months. In some embodiments of an oral liquid formulation, the formulation is stable at about 5±5° C. for at least 24 months. Also disclosed herein is a process for preparing a stable amlodipine oral liquid formulation, the process comprising mixing a first mixture with a second mixture; the first mixture comprising: (i) amlodipine benzoate; (ii) sodium benzoate; (iii) optionally polysorbate 80; and (iv) water; and the second mixture comprising: (i) citric acid; (ii) sodium citrate; (iii) sucralose; (iv) optionally a flavoring agent; (v) hydroxypropyl methylcellulose; (vi) simethicone; (vii) silicon dioxide; and (viii) water. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the first mixture is obtained by a process comprising: (i) adding water to a first container which is not stainless steel; (ii) adding amlodipine besylate to the first container; (iii) adding sodium benzoate to the first container; (iv) optionally adding polysorbate 80 to the first container; and (v) stirring until amlodipine benzoate substantially precipitates. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the second mixture is obtained by a process comprising: (i) adding water to a second container; (ii) adding citric acid to the second container; (iii) adding sodium citrate to the second container; (iv) adding sucralose to the second container; (v) optionally adding the flavoring agent to the second container; (vi) adding hydroxypropyl methylcellulose to the second container; (vii) adding simethicone to the second container; (viii) adding silicon dioxide to the second container; and (ix) stirring. Also disclosed herein is a process for preparing a stable amlodipine oral liquid formulation, the process comprising mixing a first mixture with a second mixture; the first mixture comprising: (i) amlodipine naphthalene sulfonate; (ii) optionally sodium benzoate; (iii) optionally polysorbate 80; and (iv) water; and the second mixture comprising: (i) citric acid; (ii) sodium citrate; (iii) sucralose; (iv) optionally a flavoring agent; (v) hydroxypropyl methylcellulose; (vi) simethicone; (vii) silicon dioxide; and (viii) water. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the first mixture is obtained by a process comprising: (i) adding water to a first container which is not stainless steel; (ii) adding amlodipine besylate to the first container; (iii) adding sodium naphthalene-2-sulfonate to the first container; (iv) adding sodium benzoate to the first container; (v) optionally adding polysorbate 80 to the first container; and (vi) stirring until amlodipine naphthalene sulfonate substantially precipitates. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the second mixture is obtained by a process comprising: (i) adding water to a second container; (ii) adding citric acid to the second container; (iii) adding sodium citrate to the second container; (iv) adding sucralose to the second container; (v) optionally adding the flavoring agent to the second container; (vi) adding hydroxypropyl methylcellulose to the second container; (vii) adding simethicone to the second container; (viii) adding silicon dioxide to the second container; and (ix) stirring. In some embodiments of a process for preparing a stable amlodipine oral liquid formulation, the first mixture does not comprise sodium benzoate and the second mixture further comprises a paraben. Also disclosed herein is a method of treating hypertension in a subject comprising administering to that subject a therapeutically effective amount of an amlodipine oral liquid formulation comprising: (i) a pharmaceutically acceptable salt of amlodipine in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) optionally about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of a method of treating hypertension, the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments of a method of treating hypertension, the amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments of a method of treating hypertension, the oral liquid formulation further comprises unreacted salt forming agent. In some embodiments of a method of treating hypertension, the salt forming agent is sodium benzoate. In some embodiments of a method of treating hypertension, the salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments of a method of treating hypertension, the hypertension is primary (essential) hypertension. In some embodiments of a method of treating hypertension, the hypertension is secondary hypertension. In some embodiments of a method of treating hypertension, the subject has blood pressure values greater than or equal to 140/90 mmm Hg. In some embodiments of a method of treating hypertension, the subject is an adult. In some embodiments of a method of treating hypertension, the subject is elderly. In some embodiments of a method of treating hypertension, the subject is a child. In some embodiments of a method of treating hypertension, the formulation is administered to the subject in a fasted state. In some embodiments of a method of treating hypertension, the formulation is administered to the subject in a fed state. In some embodiments of a method of treating hypertension, the formulation is further administered in combination with an agent selected from the group consisting of diuretics, beta blockers, alpha blockers, mixed alpha and beta blockers, calcium channel blockers, angiotensin II receptor antagonists, ACE inhibitors, aldosterone antagonists, and alpha-2 agonists. Also disclosed herein is a method of treating Coronary Artery Disease (CAD) in a subject comprising administering to that subject a therapeutically effective amount of an amlodipine oral liquid formulation comprising: (i) a pharmaceutically acceptable salt of amlodipine in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; (vi) about 0.15 mg/ml simethicone; (vii) optionally about 1.0 mg/ml of polysorbate 80; and (viii) water; wherein the formulation is stable between about 5±5° C. and about 25±5° C. for at least 12 months. In some embodiments of a method of treating Coronary Artery Disease (CAD), the pharmaceutically acceptable salt of amlodipine is amlodipine benzoate or amlodipine naphthalene sulfonate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the amlodipine benzoate or amlodipine naphthalene sulfonate are formed in situ. In some embodiments of a method of treating Coronary Artery Disease (CAD), the oral liquid formulation further comprises unreacted salt forming agent. In some embodiments of a method of treating Coronary Artery Disease (CAD), the salt forming agent is sodium benzoate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the salt forming agent is sodium naphthalene-2-sulfonate. In some embodiments of a method of treating Coronary Artery Disease (CAD), the Coronary Artery Disease (CAD) is chronic stable angina, vasospastic angina, or angiographically documented coronary artery disease. In some embodiments of a method of treating Coronary Artery Disease (CAD), the angiographically documented coronary artery disease is in patients without heart failure or an ejection fraction <40%. In some embodiments of a method of treating Coronary Artery Disease (CAD), the formulation is further administered in combination with an additional anti-anginal agent."},"cpc_label":{"kind":"string","value":"A61K314422"},"filing_date":{"kind":"string","value":"20171006"},"patent_issue_date":{"kind":"string","value":""},"date_published":{"kind":"string","value":"20180412"},"examiner_id":{"kind":"string","value":"96348.0"},"ipc_label":{"kind":"string","value":"A61K314422"},"npe_litigated_count":{"kind":"number","value":1,"string":"1"},"examiner_full_name":{"kind":"string","value":"SOROUSH, LAYLA"},"invention_title":{"kind":"string","value":"AMLODIPINE FORMULATIONS"},"small_entity_indicator":{"kind":"string","value":"UNDISCOUNTED"},"continuation":{"kind":"number","value":0,"string":"0"},"decision_as_of_2020":{"kind":"string","value":"ACCEPTED"},"main_ipcr_label_subclass":{"kind":"string","value":"A61K"},"filing_year":{"kind":"number","value":2017,"string":"2,017"}}}],"truncated":false,"partial":false},"paginationData":{"pageIndex":328,"numItemsPerPage":100,"numTotalItems":33158,"offset":32800,"length":100}},"jwt":"eyJhbGciOiJFZERTQSJ9.eyJyZWFkIjp0cnVlLCJwZXJtaXNzaW9ucyI6eyJyZXBvLmNvbnRlbnQucmVhZCI6dHJ1ZX0sImlhdCI6MTc4MDQ0OTgxNiwic3ViIjoiL2RhdGFzZXRzL3R1cmluZ21hY2hpbmUvaHVwZC1ucGUtYmFsYW5jZWQtc2FtZS15ZWFyLXNhbWUtY2xhc3Mtc3Vic2V0IiwiZXhwIjoxNzgwNDUzNDE2LCJpc3MiOiJodHRwczovL2h1Z2dpbmdmYWNlLmNvIn0.5pYQkLHvgGUvuY8zhCD__Nk3d377oCgs_xrqkbRvkgU-5jDfoIDsykq3Mup1j3Wh6KMsbrGvwRTVaQbzrYzmBA","displayUrls":true,"splitSizeSummaries":[{"config":"default","split":"train","numRows":33158,"numBytesParquet":1015448971}]},"discussionsStats":{"closed":0,"open":1,"total":1},"fullWidth":true,"hasGatedAccess":true,"hasFullAccess":true,"isEmbedded":false,"savedQueries":{"community":[],"user":[]}}">
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15,673,763 | PENDING | Wireless Power Receiver and Control Method Thereof | A wireless power receiver according to an embodiment wirelessly receives power from a wireless power transmitter. The wireless power receiver includes a printed circuit board having a reception space in a predetermined area, a receiving coil disposed in the reception space of the printed circuit board for receiving pow... | 1. A wireless power receiver that wirelessly receives power from a wireless power transmitter, the wireless power receiver comprising: a board comprising a plurality of layers; a wireless receiving coil disposed in the board; a short-range communication coil disposed in the board; and a shielding unit disposed in the b... | CROSS REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. application Ser. No. 15/195,390, filed Jun. 28, 2016, entitled “Wireless Power Receiver and Control Method Thereof”, which is a continuation of U.S. application Ser. No. 13/658,116, filed Oct. 23, 2012, now U.S. Pat. No. 9,461,364, issue... | <SOH> BACKGROUND <EOH>The embodiment relates to a wireless power receiver and a control method thereof. A wireless power transmission or a wireless energy transfer refers to a technology of wirelessly transferring electric energy to desired devices. In the 1800's, an electric motor or a transformer employing the princi... | <SOH> SUMMARY <EOH>The embodiment provides a wireless power receiver with a minimized thickness by suitably arranging a receiving coil, a short-range communication antenna and a printed circuit board. The embodiment provides a wireless power receiver with a reduced thickness by allowing a short-range communication ante... | H02J5012 | 20170810 | 20171123 | 97085.0 | H02J5012 | 1 | FLEMING, FRITZ M | Wireless Power Receiver and Control Method Thereof | UNDISCOUNTED | 1 | CONT-ACCEPTED | H02J | 2,017 | |
15,674,043 | ACCEPTED | 1-[2-(2,4-DIMETHYLPHENYLSULFANYL)-PHENYL]PIPERAZINE AS A COMPOUND With COMBINED SEROTONIN REUPTAKE, 5-HT3 AND 5-HT1A ACTIVITY FOR THE TREATMENT OF COGNITIVE IMPAIRMENT | 1-[2-(2,4-dimethylphenylsulphanyl)phenyl)]piperazine exhibits potent activity on SERT, 5-HT3 and 5-HT1A and may as such be useful for the treatment of cognitive impairment, especially in depressed patients. | 1. A method of alleviating a symptom or complication of depression or major depressive disorder, or delaying progression of depression or major depressive disorder, comprising: administering to a patient in need thereof a pharmaceutical composition comprising a hydrobromide salt of a 1-[2-(2,4-dimethylphenylsulfanyl)-p... | CROSS REFERENCE TO PRIOR APPLICATIONS This is a continuation application of U.S. application Ser. No. 14/948,775, filed Nov. 23, 2015, which is a continuation application of U.S. application Ser. No. 14/242,337, filed Apr. 1, 2014, which is a divisional application of U.S. application Ser. No. 12/301,061, filed Nov. 17... | <SOH> BACKGROUND OF THE INVENTION <EOH>Selective serotonin reuptake inhibitors (SSRI) have for years been the first choice therapeutics for the treatment of certain CNS related diseases, in particular depression, anxiety and social phobias because they are effective, well tolerated and have a favourable safety profile ... | <SOH> SUMMARY OF THE INVENTION <EOH>The present inventors have surprisingly found that 1-[2-(2,4-dimethylphenylsulfanyl)phenyl]piperazine exerts a combination of SERT inhibition, 5-HT 3 antagonism and 5-HT 1A partial agonism. Accordingly, in one embodiment the present invention provides compound I which is 1-[2-(2,4-di... | A61K31495 | 20170810 | 20180109 | 20171221 | 84397.0 | A61K31495 | 15 | POLANSKY, GREGG | 1-[2-(2,4-DIMETHYLPHENYLSULFANYL)-PHENYL]PIPERAZINE AS A COMPOUND With COMBINED SEROTONIN REUPTAKE, 5-HT3 AND 5-HT1A ACTIVITY FOR THE TREATMENT OF COGNITIVE IMPAIRMENT | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,674,122 | ACCEPTED | SEEDING MACHINE WITH SEED DELIVERY SYSTEM | A seed delivery system for use in a seeding or planting machine that removes the seed from a seed meter by capturing the seed therefrom. The delivery system then moves the seed down to a lower discharge point and accelerates the seed horizontally rearward to a speed approximately equal to the forward travel speed of th... | 1. A seeding machine, comprising: a seed metering system; a seed transfer device positioned adjacent to the seed metering system; a seed delivery system comprising a housing having a first opening and a second opening, the first opening located proximal to the seed transfer device through which seed is transferred from... | RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 14/616,877, filed Feb. 9, 2015, which is a continuation of U.S. patent application Ser. No. 14/504,801, filed Oct. 2, 2014 and issued as U.S. Pat. No. 9,686,905 on Jun. 27, 2017, which is a continuation of U.S. patent applicatio... | <SOH> BACKGROUND OF THE INVENTION <EOH>An agricultural seeding machine such as a row crop planter or grain drill places seeds at a desired depth within a plurality of parallel seed trenches formed in soil. In the case of a row crop planter, a plurality of row crop units is typically ground driven using wheels, shafts, ... | <SOH> SUMMARY OF THE INVENTION <EOH>The present invention provides a seed delivery system that removes the seed from the seed meter by capturing the seed. The delivery system then moves the seed down to a lower discharge point and accelerates the seed rearward to a horizontal velocity approximately equal to the forward... | A01C716 | 20170810 | 20180626 | 20171123 | 99684.0 | A01C716 | 1 | NOVOSAD, CHRISTOPHER J | SEEDING MACHINE WITH SEED DELIVERY SYSTEM | UNDISCOUNTED | 1 | CONT-ACCEPTED | A01C | 2,017 |
15,674,827 | PENDING | APPARATUS FOR SEPARATING USABLE CROP FROM INTERMIXED DEBRIS | An apparatus for separating usable crop from intermixed debris, the apparatus having: a movable support; a conveying system on the movable support to convey usable crop in a processing path from an upstream input location to a downstream output location; at least a first separating system on the movable support to caus... | 1. An apparatus for separating usable crop from intermixed debris, the apparatus comprising: a movable support; a conveying system on the movable support configured to convey usable crop in a processing path from an upstream input location to a downstream output location; at least a first separating system on the movab... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation-in-part of U.S. patent application Ser. No. 14/630,723 filed Feb. 25, 2015. BACKGROUND OF THE INVENTION Field of the Invention This invention relates to crop harvesting and, more particularly, to an apparatus through which usable crop can be sep... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>In one form, the invention is directed to an apparatus for separating usable crop from intermixed debris. The apparatus includes: a movable support; a conveying system on the movable support configured to convey usable crop in a processing path from an upstream input location to a do... | B07B902 | 20170811 | 20180201 | 71430.0 | B07B902 | 0 | FABIAN-KOVACS, ARPAD | APPARATUS FOR SEPARATING USABLE CROP FROM INTERMIXED DEBRIS | UNDISCOUNTED | 1 | CONT-ACCEPTED | B07B | 2,017 | |
15,675,361 | PENDING | INHIBITORS OF INDUCED MMP-1 PRODUCTION | The present invention provides methods and compositions of prophylaxis for, or for treating, chronic obstructive pulmonary disease (COPD), cancer, arthritis, skin damage, or atherosclerotic plaque rupture in a subject in need thereof, which comprise i) a statin or ii) selective serotonin reuptake inhibitor (SSRI). | 1. A method of prophylaxis for, or for treating, chronic obstructive pulmonary disease (COPD), cancer, arthritis, skin damage, or atherosclerotic plaque rupture in a subject in need thereof, which comprises administering to the subject i) a statin or ii) a selective serotonin reuptake inhibitor (SSRI) in an amount that... | This application is a continuation-in-part of PCT International Application No. PCT/US2016/017562, filed Feb. 11, 2016, claiming the benefit of U.S. Provisional Application No. 62/115,021, filed Feb. 11, 2015, the contents of each of which are hereby incorporated by reference into the application. This invention was ma... | <SOH> BACKGROUND OF INVENTION <EOH>Chronic obstructive pulmonary disease (COPD) is an enormous unmet medical need. Present therapies offer relief from its symptoms, but no drug treats the cause or slows progression of the disease. The most common cause of COPD is cigarette smoking, a behavior whose prevalence in the U.... | <SOH> SUMMARY OF THE INVENTION <EOH>The present invention provides a method of prophylaxis for, or for treating, chronic obstructive pulmonary disease (COPD), cancer, arthritis, skin damage, or atherosclerotic plaque rupture in a subject in need thereof, which comprises administering to the subject i) a statin or ii) a... | A61K31366 | 20170811 | 20180201 | 66987.0 | A61K31366 | 0 | THOMAS, TIMOTHY P | INHIBITORS OF INDUCED MMP-1 PRODUCTION | SMALL | 1 | CONT-REJECTED | A61K | 2,017 | |
15,675,368 | ACCEPTED | SHELVING SYSTEM | A shelving system includes a plurality of horizontal support members, each horizontal support member having a length; a plurality of wall supports, each wall support including a first surface on which at least a portion of a horizontal support member rests; a plurality of brackets, each bracket attachable to the horizo... | 1. A shelving system comprising: a support assembly comprising first and second support posts, each support post having a pair of mounting surfaces that face away from each other and a first abutment surface that is orthogonal to and between the mounting surfaces, and a plurality of support pins fixed to each of the fi... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 15/026,519 filed on Mar. 31, 2016, which is a U.S. National Phase entry of International Patent Application PCT/US14/58308 filed on Sep. 30, 2014, which claims priority to U.S. Provisional Patent Application N... | <SOH> FIELD <EOH>The present invention relates to shelves, racks, and workstations, and more particularly to shelves, racks, and workstations that are supported by a wall or ceiling and cantilevered for supporting items or for supporting work surfaces. | <SOH> SUMMARY <EOH>An important function of most shelving and rack systems and workstations is the ability to increase storage and working space. Limitations exist in the design and assembly of many conventional shelving systems, racks and workstations. These limitations are most apparent in highly competitive industri... | A47F508 | 20170811 | 20180206 | 20171130 | 73203.0 | A47F508 | 1 | NOVOSAD, JENNIFER ELEANORE | SHELVING SYSTEM | UNDISCOUNTED | 1 | CONT-ACCEPTED | A47F | 2,017 |
15,675,492 | PENDING | FRAUD PREVENTION BASED ON USER ACTIVITY DATA | A user conducts activities, such as researching a product online or visiting a store that sells the product. A user then utilizes a risk analysis system to receive and store user activity data for the user's activities. When a purchase attempt is made with the user's financial account, a merchant sends a transaction re... | 1.-20. (canceled) 21. A computer-implemented method to reduce fraud in online transactions by correlating shopping behaviors of users in physical merchant locations with product identification information associated with products being purchased in the online transactions, comprising: logging, by one or more computing ... | TECHNICAL FIELD The present disclosure relates generally to fraud prevention, and more particularly to methods and systems that rely on user-provided activity data, such as user search history, to detect possible fraudulent activity for purchase transactions involving a financial account of the user. BACKGROUND Electro... | <SOH> BACKGROUND <EOH>Electronic commerce, such as online shopping, has been increasingly common since the advent of the Internet. Online shopping websites generally provide a user interface for customers to select products to purchase. After the customer has selected products for purchase, the customer typically may c... | <SOH> SUMMARY <EOH>In certain example aspects described herein, a computer-implemented method for transaction risk analysis is provided. A risk analysis system receives a registration from a user that desires to have their purchase transactions monitored for possible fraudulent activity. The risk analysis system, for e... | G06Q204016 | 20170811 | 20171130 | 64483.0 | G06Q2040 | 0 | ZIMMERMAN, MATTHEW E | METHOD, MEDIUM, AND SYSTEM FOR ONLINE FRAUD PREVENTION | UNDISCOUNTED | 1 | CONT-ACCEPTED | G06Q | 2,017 | |
15,675,789 | ACCEPTED | CONCEALABLE BODY ARMOR AND COMBINATION BAG/VEST | Described herein are combination bag/vests which, in a bag configuration, serve as a functional bag and which, in a vest configuration, include a system for attaching one or more modular accessories to the vest in a desired configuration. Also described herein are such combination bag/vests wherein the vest configurati... | 1. A combination bag/vest comprising: a vest comprising: a chest covering portion and a back covering portion the chest covering portion and back covering portion each portion having a vest surface; a pair of separable shoulder straps each connecting an upper portion of the chest covering portion with an upper portion ... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation application claiming the benefit of U.S. patent application Ser. No. 14/153,687, filed Jan. 13, 2014, the disclosure of which is herein incorporated by reference. BACKGROUND 1. Field of the Invention The present invention relates generally to mu... | <SOH> BACKGROUND <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>It would be desirable to produce a combination bag/vest which, in a bag configuration, serves as a functional bag and which, in a vest configuration, includes a system for attaching one or more accessories in a desired configuration. It would also be desirable to produce such combina... | A41D1504 | 20170814 | 20180109 | 20171130 | 97819.0 | A41D1504 | 2 | QUINN, RICHALE LEE | CONCEALABLE BODY ARMOR AND COMBINATION BAG/VEST | SMALL | 1 | CONT-ACCEPTED | A41D | 2,017 |
15,675,895 | PENDING | Combinatory Score Having a Fitness Sub-Score and an Athleticism Sub-Score | Example embodiments may relate to a system, method, apparatus, and computer readable media configured for monitoring a user performing an athletic movement and/or exercise and generating a combinatory fitness athleticism score. The score may comprise a fitness sub-score and a fitness sub-score. The athletic movement ma... | 1. A computer-implemented method comprising: providing first instructions to a user to perform a first athletic movement; receiving, from a sensor, first activity data representing the first athletic movement; calculating with a processor, based on the first activity data, a first combinatory fitness-athleticism score;... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. application Ser. No. 15/074,682, filed Mar. 18, 2016, which is a continuation of U.S. application Ser. No. 13/909,832, filed Jun. 4, 2013, now U.S. Pat. No. 9,289,674, which claims the benefit of U.S. Provisional Patent Application No. 6... | <SOH> BACKGROUND <EOH>While most people appreciate the importance of physical fitness, many have difficulty finding the motivation required to maintain a regular exercise program. Some people find it particularly difficult to maintain an exercise regimen that involves continuously repetitive motions, such as running, w... | <SOH> SUMMARY <EOH>The following presents a simplified summary of the present disclosure in order to provide a basic understanding of some aspects of the invention. This summary is not an extensive overview of the invention. It is not intended to identify key or critical elements of the invention or to delineate the sc... | A63B7106 | 20170814 | 20180111 | 76440.0 | A63B7106 | 1 | ROWLAND, STEVE | Combinatory Score Having a Fitness Sub-Score and an Athleticism Sub-Score | UNDISCOUNTED | 1 | CONT-ACCEPTED | A63B | 2,017 | |
15,675,930 | PENDING | VIRTUAL 360-DEGREE VIEW OF A TELECOMMUNICATIONS SITE | Systems and method for creating and utilizing a virtual 360-degree view of a telecommunications site include capturing first data of a 360-degree view at multiple points around the telecommunications site; capturing second data of a 360-degree view at aerial points above the telecommunications site; capturing third dat... | 1. A method for creating and utilizing a virtual 360-degree view of a telecommunications site, the method comprising: capturing first data of a 360-degree view at multiple points around the telecommunications site; capturing second data of a 360-degree view at aerial points above the telecommunications site; capturing ... | CROSS-REFERENCE TO RELATED APPLICATION(S) The present patent/application is continuation-in-part of and the content of each are incorporated by reference herein: Filing Date Ser. No. Title Jul. 7, 2017 15/644,144 DETECTING CHANGES AT CELL SITES AND SURROUNDING AREAS USING UNMANNED AERIAL VEHICLES May 17, 2017 15/597,32... | <SOH> BACKGROUND OF THE DISCLOSURE <EOH>Due to the geographic coverage nature of wireless service, there are hundreds of thousands of cell towers in the United States. For example, in 2014, it was estimated that there were more than 310,000 cell towers in the United States. Cell towers can have heights up to 1,500 feet... | <SOH> BRIEF SUMMARY OF THE DISCLOSURE <EOH>In an exemplary embodiment, a method for creating and utilizing a virtual 360-degree view of a telecommunications site includes capturing first data of a 360-degree view at multiple points around the telecommunications site; capturing second data of a 360-degree view at aerial... | H04N523238 | 20170814 | 20171221 | 99058.0 | H04N5232 | 1 | LETT, THOMAS J | VIRTUAL 360-DEGREE VIEW OF A TELECOMMUNICATIONS SITE | SMALL | 1 | CONT-ACCEPTED | H04N | 2,017 | |
15,676,631 | PENDING | SELF-OPTIMIZING DISTRIBUTED ANTENNA SYSTEM USING SOFT FREQUENCY REUSE | A method of determining a carrier power in a communications system including a processor includes a) setting a power differential between a reference carrier and one or more carriers, b) measuring a number of satisfied users at the power differential, and c) measuring a capacity for the satisfied users at the power dif... | 1. (canceled) 2. A method of determining a transmission power of a digital remote unit (DRU) in a distributed antenna system (DAS), the method comprising: a) setting a transmission power level for the DRU; b) determining a key performance indicator related to a number of satisfied users at the transmission power; c) it... | CROSS-REFERENCES TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 15/154,073, filed May 13, 2016, which is a continuation of U.S. patent application Ser. No. 13/935,157, filed on Jul. 3, 2013, now U.S. Pat. No. 9,363,768, which claims priority to U.S. Provisional Patent App... | <SOH> SUMMARY OF THE INVENTION <EOH>According to an embodiment of the present invention, a method of determining a carrier power in a communications system including a processor is provided. The method includes a) setting a power differential between a reference carrier and one or more carriers, b) measuring a number o... | H04W52243 | 20170814 | 20180329 | 98936.0 | H04W5224 | 1 | KAMARA, MOHAMED A | SELF-OPTIMIZING DISTRIBUTED ANTENNA SYSTEM USING SOFT FREQUENCY REUSE | SMALL | 1 | CONT-ACCEPTED | H04W | 2,017 | ||
15,676,976 | PENDING | BODY LIMB PROTECTION SYSTEM | A body limb protection system includes an outer layer, an inner layer, and a force dampening and defusing structure. The outer layer includes a first material composition and has an exterior surface that includes a substantially planer area. The inner layer includes a second material composition and has a shape corresp... | 1. A body limb protection system comprises: an outer layer including a first material composition and having an exterior surface that includes a substantially planer area; an inner layer including a second material composition and having a shape corresponding to a body limb portion, wherein the inner layer is adjacent ... | CROSS REFERENCE TO RELATED PATENTS The present U.S. Utility Patent Application claims priority pursuant to 35 U.S.C. § 119(e) to U.S. Provisional Application No. 62/375,767, entitled “BODY IMPACT PROTECTION SYSTEM”, filed Aug. 16, 2016, which is hereby incorporated herein by reference in its entirety and made part of t... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> BRIEF DESCRIPTION OF THE SEVERAL VIEWS OF THE DRAWING(S) <EOH>FIG. 1 is a schematic diagram of an example of a conventional impact protection device receiving an impact force; FIG. 2 is a diagram of an example graph of the impact protection device of FIG. 1 that plots impact force versus impact area; FIG. 3 is a ... | A41D13015 | 20170814 | 20180222 | 94510.0 | A41D13015 | 0 | VANATTA, AMY B | BODY LIMB PROTECTION SYSTEM | SMALL | 0 | PENDING | A41D | 2,017 | |
15,677,081 | PENDING | STANDARD MOBILE COMMUNICATION DEVICE DISTRACTION PREVENTION AND SAFETY PROTOCOLS | Methods and systems for providing standardized mobile device distraction prevention and safety protocols are disclosed. In particular, an embodiment of a method for activating a distraction prevention or safety protocol behavior in a mobile device when the mobile device satisfies a specific condition is disclosed. The ... | 1. A method of activating a protocol behavior in a mobile device within a specified environment comprising: broadcasting, by a protocol activator, a first trigger signal in the specified environment; and including, by the protocol activator, a discovery information in the first trigger signal, wherein the discovery inf... | PRIORITY APPLICATIONS This application is a continuation application of and claims priority to U.S. patent application Ser. No. 15/368,856 filed on Dec. 5, 2016, which is a continuation of and claims priority to U.S. patent application Ser. No. 15/075,327 filed on Mar. 21, 2016, now issued as U.S. Pat. No. 9,584,652, w... | <SOH> BACKGROUND <EOH>Over the past few decades, the cellular/wireless industry has advanced by leaps and bounds. Throughout the world, mobile devices have become a ubiquitous part of everyday life. The enormous proliferation of the mobile device is nothing short of incredible. But, with it has surfaced a host of major... | <SOH> SUMMARY OF INVENTION <EOH>It is, therefore an object of the present invention, to provide a set of standard mobile communication device distraction prevention and safety protocols to be embedded in the mobile device firmware (system memory or system image) and to provide various applicable sensors to be adopted u... | H04M172577 | 20170815 | 20180111 | 61619.0 | H04M1725 | 0 | LEE, JOHN J | STANDARD MOBILE COMMUNICATION DEVICE DISTRACTION PREVENTION AND SAFETY PROTOCOLS | SMALL | 1 | CONT-ACCEPTED | H04M | 2,017 | |
15,677,143 | PENDING | SELF-CHECKOUT STATION AIR CIRCULATION | A self-checkout system comprises a cabinet housing, the cabinet including a ventilated region; a point of sale (POS) station at the cabinet housing, the POS station including heat-generating components, the ventilated region of the cabinet housing removing heat generated from the POS components from the cabinet housing... | 1. A self-checkout system, comprising: a cabinet housing, the cabinet including a ventilated region; a point of sale (POS) station at the cabinet housing, the POS station including heat-generating components, the ventilated region of the cabinet housing removing heat generated from the heat-generating components from t... | RELATED APPLICATIONS This application claims the benefit of U.S. Provisional Patent No. 62/377,305, filed Aug. 19, 2016, entitled “Self-Checkout Station Air Circulation,” the contents of which are incorporated by reference herein in their entirety. This application is related to Design Patent application Ser. No. 29/57... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY <EOH>In one aspect, provided is a self-checkout system, comprising: a cabinet housing, the cabinet including a ventilated region; a point of sale (POS) station at the cabinet housing, the POS station including heat-generating components, the ventilated region of the cabinet housing removing heat generated... | A47F9048 | 20170815 | 20180222 | 66102.0 | A47F904 | 0 | DANNEMAN, PAUL | SELF-CHECKOUT STATION AIR CIRCULATION | UNDISCOUNTED | 0 | ACCEPTED | A47F | 2,017 | |
15,677,957 | PENDING | METHODS FOR ANALYZING NUCLEIC ACIDS FROM SINGLE CELLS | Aspects of the present invention include analyzing nucleic acids from single cells using methods that include using tagged polynucleotides containing multiplex identifier sequences. | 1. A method of analyzing nucleic acids from a plurality of single cells, the method comprising: (a) providing a sample comprising a plurality of single cells, wherein each single cell of the plurality of single cells comprises a plurality of sample polynucleotides; (b) generating a plurality of tagged polynucleotides f... | BACKGROUND OF THE INVENTION We have previously described methods that enable tagging each of a population of fragmented genomes and then combining them together to create a ‘population library’ that can be processed and eventually sequenced as a mixture. The population tags enable analysis software to parse the sequenc... | <SOH> BACKGROUND OF THE INVENTION <EOH>We have previously described methods that enable tagging each of a population of fragmented genomes and then combining them together to create a ‘population library’ that can be processed and eventually sequenced as a mixture. The population tags enable analysis software to parse ... | <SOH> SUMMARY OF THE INVENTION <EOH>Aspects of the present invention are drawn to processes for moving a region of interest in a polynucleotide from a first position to a second position with regard to a domain within the polynucleotide, also referred to as a “reflex method” (or reflex process, reflex sequence process,... | C12Q16874 | 20170815 | 20180322 | 67988.0 | C12Q168 | 2 | DINES, KARLA A | METHODS FOR ANALYZING NUCLEIC ACIDS FROM SINGLE CELLS | SMALL | 1 | CONT-ACCEPTED | C12Q | 2,017 | |
15,679,054 | PENDING | System and Method for Real-Time Optimization and Industry Benchmarking for Campaign Management | A system for collecting brand awareness and advertising campaign performance results in real-time. Embodiments allow the system to adapt (e.g., machine learning) to target advertisements to users that are most likely to be influenced by exposure to a brand awareness advertising campaign, and present results, in real-ti... | 1. A method for real-time data optimization and campaign benchmarking, the method comprising: receiving a selected content request associated with a user identifier from a user device; retrieving a user profile associated with the user identifier from a profile store; determining whether to deliver a survey to the user... | CROSS-REFERENCE TO RELATED APPLICATIONS This application claims the benefit of U.S. Provisional Application No. 62/375,864, filed Aug. 16, 2016, which application is hereby incorporated herein by reference in its entirety and for all purposes. This application is also a continuation-in-part of U.S. patent application S... | <SOH> BACKGROUND <EOH>Consumers are inundated with various types of advertising content on television, mobile devices, and while accessing the internet, but typically lack the ability to actively control and interact with such advertising content. For example, consumers are conventionally served with advertising conten... | <SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>FIG. 1 is an exemplary top-level block diagram illustrating an embodiment of a content feedback, incentive, and reward system. FIG. 2 is an exemplary data flow diagram illustrating an embodiment of a data flow path between a user device, the list server and content server of... | G06Q300245 | 20170816 | 20180222 | 65555.0 | G06Q3002 | 0 | DAGNEW, SABA | System and Method for Real-Time Optimization and Industry Benchmarking for Campaign Management | SMALL | 0 | PENDING | G06Q | 2,017 | |
15,679,696 | ACCEPTED | ELEVATOR ROLLER INSERT SYSTEM | A device, system, and/or method for reducing friction required to rotate a tubular within an elevator during the process of running tubulars in an oil and gas well are provided. An elevator roller insert may be used in conjunction with an elevator, such as a single joint elevator. Such an insert may comprise upper and ... | 1. An elevator roller system for a drilling rig, comprising: a tubular having a first outer diameter and a second outer diameter, wherein the first outer diameter is smaller than the second outer diameter; an elevator having: a first arm having an interior surface; a second arm having an interior surface, the first and... | CROSS REFERENCE TO RELATED APPLICATION This application is a continuation application under 35 U.S.C. §111(a) of PCT Application No. PCT/US2016/023686 having an international filing date of Mar. 23, 2016, which designated the United States, which PCT application claims the benefit of U.S. Application Ser. No. 62/136,97... | <SOH> BACKGROUND AND SUMMARY OF THE INVENTION <EOH>In the oil and gas industry, wellbores are drilled into the earth using drilling rigs, where tubulars are threaded together to form long tubular strings that are inserted into the wellbore to extract the desired fluid. The tubing string is generally suspended in the bo... | <SOH> BACKGROUND AND SUMMARY OF THE INVENTION <EOH>In the oil and gas industry, wellbores are drilled into the earth using drilling rigs, where tubulars are threaded together to form long tubular strings that are inserted into the wellbore to extract the desired fluid. The tubing string is generally suspended in the bo... | E21B1906 | 20170817 | 20180605 | 20171130 | 59492.0 | E21B1906 | 2 | MALIKASIM, JONATHAN L | ELEVATOR ROLLER INSERT SYSTEM | SMALL | 1 | CONT-ACCEPTED | E21B | 2,017 |
15,679,748 | PENDING | SYSTEM AND METHOD FOR MANAGING GRATUITIES | A computer-implemented method for allocating gratuities is disclosed that includes employing at least one processor configured to execute computer-executable instructions stored in memory to perform the following acts: receiving transaction information from a point of sale, wherein the transaction information comprises... | 1-21. (canceled) 22. A computer-implemented system for managing gratuity allocations comprising: at least one processor coupled to at least one memory configured to execute the following computer-executable components stored in the at least one memory: a database configured to store transaction information and employee... | RELATED APPLICATION This application is a continuation application of and claims priority to and the benefit of U.S. patent application Ser. No. 13/834,466, filed Mar. 15, 2013, now U.S. Pat. No. 9,741,050, and to U.S. Patent Application No. 61/696,569, filed Sep. 4, 2012, the disclosures of which are incorporated here... | <SOH> BACKGROUND AND SUMMARY <EOH>The present disclosure is related to a system and method for managing gratuities, and more particularly to calculating, allocating, and distributing gratuities among service employees. In the hospitality industry and many other service based businesses, it is customary for customers to... | <SOH> BACKGROUND AND SUMMARY <EOH>The present disclosure is related to a system and method for managing gratuities, and more particularly to calculating, allocating, and distributing gratuities among service employees. In the hospitality industry and many other service based businesses, it is customary for customers to... | G06Q300214 | 20170817 | 20180510 | 93646.0 | G06Q3002 | 1 | WILDER, ANDREW H | SYSTEM AND METHOD FOR MANAGING GRATUITIES | SMALL | 1 | CONT-ACCEPTED | G06Q | 2,017 | |
15,680,300 | ACCEPTED | CONTROLLING FUNCTIONS OF A USER DEVICE UTILIZING AN ENVIRONMENT MAP | A system and method is provided for using information broadcast by devices and resources in the immediate vicinity of a mobile device, or by sensors located within the mobile device itself, to ascertain and make a determination of the immediate environment and state of the mobile device. This determination may be used ... | 1. A method for controlling access to a functionality of a user device, the method comprising: receiving a capabilities list (CL) from one or more external resources available to and in proximity with the user device, each CL specifying one or more attributes of the respective external resource from which it is receive... | BACKGROUND OF THE INVENTION Field of the Invention The present invention relates to the delivery, discovery, management and control of information to mobile consumers, and more particularly to consumers who have access to multiple devices, capabilities and networks, and to the efficient use and control of these resourc... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>These and other drawbacks in the prior art are overcome in large part by a system and method according to embodiments of the present invention. A telecommunications method in accordance with embodiments of the present invention includes receiving registry map information of network e... | H04W4001 | 20170818 | 20180306 | 20171207 | 78187.0 | H04W400 | 1 | LE, DANH C | CONTROLLING FUNCTIONS OF A USER DEVICE UTILIZING AN ENVIRONMENT MAP | SMALL | 1 | CONT-ACCEPTED | H04W | 2,017 |
15,683,359 | PENDING | SECURE AUTHENTICATION AND PAYMENT SYSTEM | A transaction and payment and processing system securely conducts transactions over the public telephone network. The transactions may be between and among entities of any type such as individuals, merchants, utilities, banks, etc. Nothing more than access to a telephone is required after initial registration of a user... | 1. A server comprising: a processor, the processor including one or more program modules configured to: send a message to a client device, wherein the message provides instructions for a target to access the server to receive payment; receive one or more messages from the client device, the one or more messages includi... | CROSS-REFERENCE TO RELATED APPLICATIONS The present application is a Continuation Application of U.S. patent application Ser. No. 13/689,308, filed Nov. 29, 2012, which is a Divisional of U.S. patent application Ser. No. 10/375,501 filed on Feb. 26, 2003, now U.S. Pat. No. 8,346,659, which is a continuation-in-part of ... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>Despite the widespread adoption of the internet and the significant commerce which already takes place over it, a substantial portion of the public still does not use the internet for commercial transactions. For some of these the non-use is attributable to unfamiliarity with, or acc... | G06Q203821 | 20170822 | 20171207 | 70763.0 | G06Q2038 | 3 | HAMILTON, LALITA M | SECURE AUTHENTICATION AND PAYMENT SYSTEM | SMALL | 1 | CONT-ACCEPTED | G06Q | 2,017 | |
15,683,623 | ACCEPTED | FASTER STATE TRANSITIONING FOR CONTINUOUS ADJUSTABLE 3DEEPS FILTER SPECTACLES USING MULTI-LAYERED VARIABLE TINT MATERIALS | An electrically controlled spectacle includes a spectacle frame and optoelectronic lenses housed in the frame. The lenses include a left lens and a right lens, each of the optoelectrical lenses having a plurality of states, wherein the state of the left lens is independent of the state of the right lens. The electrical... | 1. An apparatus comprising: a storage adapted to: store one or more image frames; a processor adapted to: obtain a first image frame and a second image frame from a first video stream; generate a first modified image frame by expanding the first image frame, wherein the first modified image frame is different from the ... | CROSS REFERENCE TO RELATED APPLICATIONS This application is a Continuation of U.S. patent application Ser. No. 15/606,850, filed May 26, 2017, which is (I) a Continuation-In-Part application of U.S. patent application Ser. No. 15/217,612, filed Jul. 22, 2016, now U.S. Pat. No. 9,699,444, which is a Continuation of U.S.... | <SOH> BACKGROUND <EOH>This invention is, in part, directed to Continuous Adjustable 3Deeps Filter spectacles for viewing 2D movies as 3D movies. 3Deeps Filter Spectacles provide a system by which ordinary 2-dimensional motion pictures can be viewed in part as a 3-dimensional motion pictures. They however were a sub-opt... | <SOH> SUMMARY OF THE INVENTION <EOH>A method has now been discovered for originating visual illusions of figures and spaces in continuous movement in any chosen direction using a finite number of pictures (as few as two pictures) that can be permanently stored and copied and displayed on motion picture film or electron... | H04N130431 | 20170822 | 20180417 | 20171228 | 67162.0 | H04N1304 | 10 | DANG, HUNG XUAN | FASTER STATE TRANSITIONING FOR CONTINUOUS ADJUSTABLE 3DEEPS FILTER SPECTACLES USING MULTI-LAYERED VARIABLE TINT MATERIALS | UNDISCOUNTED | 1 | CONT-ACCEPTED | H04N | 2,017 |
15,684,369 | ACCEPTED | SOUND VERIFICATION | In some examples, sound verification may include a speaker device that may be configured to transmit sound at a dynamic volume level and a listening device that may be configured to receive the sound and provide feedback to the speaker device based on the received sound. The primary transceiver device may be further co... | 1. A sound verification system, comprising: a plurality of speaker devices, wherein each of the plurality of speaker devices is configured to transmit sound at a dynamic volume level; and one or more listener devices configured to: receive the sound from the plurality of speaker devices; distinguish the received sound ... | CROSS-REFERENCE TO RELATED APPLICATIONS This Application is a continuation application under 35 U.S.C. §120 of U.S. application Ser. No. 14/440,236, filed on May 1, 2015, which is the U.S. National Stage filing under 35 U.S.C. §371 of International Application No. PCT/US14/33316, filed on Apr. 8, 2014. The disclosures ... | <SOH> BACKGROUND <EOH>Unless otherwise indicated herein, the approaches described in this section are not prior art to the claims in this application and are not admitted to be prior art by inclusion in this section. Acoustics in open forums may be unpredictable. For example, in an outdoor setting, weather conditions s... | <SOH> SUMMARY <EOH>In one example embodiment, a sound verification system may include: a speaker device that is configured to transmit sound at a dynamic volume level; and a listening device that is configured to receive the sound and provide feedback to the speaker device based on the received sound, wherein the speak... | G10L210364 | 20170823 | 20180529 | 20171207 | 70527.0 | G10L210364 | 1 | HUBER, PAUL W | SOUND VERIFICATION | UNDISCOUNTED | 1 | CONT-ACCEPTED | G10L | 2,017 |
15,685,566 | PENDING | Combination Therapy with Glutaminase Inhibitors | The invention relates to novel heterocyclic compounds and pharmaceutical preparations thereof. The invention further relates to methods of treating or preventing cancer using the novel heterocyclic compounds of the invention. | 1. A method of treating or preventing cancer in a subject, comprising administering a glutaminase inhibitor and a taxane to the subject, wherein the subject is refractory to at least one prior chemotherapy treatment. 2. The method of claim 1, wherein the glutaminase inhibitor is a compound of formula (I), or a pharmace... | BACKGROUND Glutamine supports cell survival, growth and proliferation through metabolic and non-metabolic mechanisms. In actively proliferating cells, the metabolism of glutamine to lactate, also referred to as “glutaminolysis” is a major source of energy in the form of NADPH. The first step in glutaminolysis is the de... | <SOH> BACKGROUND <EOH>Glutamine supports cell survival, growth and proliferation through metabolic and non-metabolic mechanisms. In actively proliferating cells, the metabolism of glutamine to lactate, also referred to as “glutaminolysis” is a major source of energy in the form of NADPH. The first step in glutaminolysi... | <SOH> SUMMARY OF INVENTION <EOH>The present invention provides a method of treating or preventing cancer, such as triple-negative breast cancer (TNBC), in a subject, comprising administering a compound of formula (I), or a pharmaceutically acceptable salt thereof, wherein: L represents CH 2 SCH 2 , CH 2 CH 2 , CH 2 CH ... | A61K31501 | 20170824 | 20180301 | 62726.0 | A61K31501 | 0 | WANG, SHENGJUN | COMBINATION THERAPY WITH GLUTAMINASE INHIBITORS | SMALL | 0 | ACCEPTED | A61K | 2,017 | |
15,686,198 | ACCEPTED | SHORT-WAVE INFRARED SUPER-CONTINUUM LASERS FOR EARLY DETECTION OF DENTAL CARIES | A wearable device for use with a smart phone or tablet includes LEDs for measuring physiological parameters by modulating the LEDs and generating a near-infrared multi-wavelength optical beam. At least one LED emits at a first wavelength having a first penetration depth and at least another LED emits at a second wavele... | 1. A wearable device for use with a smart phone or tablet, the wearable device comprising: a measurement device including a light source comprising a plurality of light emitting diodes (LEDs) for measuring one or more physiological parameters, the measurement device configured to generate, by modulating at least one of... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a Continuation of U.S. application Ser. No. 15/357,136 filed Nov. 21, 2016, which is a Continuation of U.S. application Ser. No. 14/651,367 filed Jun. 11, 2015, which is the U.S. national phase of PCT Application No. PCT/US2013/075736 filed Dec. 17, 2013, whic... | <SOH> BACKGROUND AND SUMMARY <EOH>Dental care and the prevention of dental decay or dental caries has changed in the United States over the past several decades, due to the introduction of fluoride to drinking water, the use of fluoride dentifrices and rinses, application of topical fluoride in the dental office, and i... | <SOH> BACKGROUND AND SUMMARY <EOH>Dental care and the prevention of dental decay or dental caries has changed in the United States over the past several decades, due to the introduction of fluoride to drinking water, the use of fluoride dentifrices and rinses, application of topical fluoride in the dental office, and i... | A61B50088 | 20170825 | 20180109 | 20171228 | 90729.0 | A61B500 | 2 | RAHMAN, MD M | SHORT-WAVE INFRARED SUPER-CONTINUUM LASERS FOR EARLY DETECTION OF DENTAL CARIES | SMALL | 1 | CONT-ACCEPTED | A61B | 2,017 |
15,686,268 | PENDING | STORAGE MEDIUM STORING GAME PROGRAM, GAME PROCESSING METHOD, AND INFORMATION PROCESSING APPARATUS | A non-transitory computer readable recording medium stores game program code instructions for a game in which a first user and a second user do battle, and when the game program code instructions are executed by a computer, the game program code instructions cause the computer to perform a data storage function of stor... | 1. A non-transitory computer readable recording medium storing game program code instructions for a game in which a first user and a second user do battle, and when the game program code instructions are executed by a computer, the game program code instructions cause the computer to perform: a data storage function of... | CROSS REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 15/391,123, filed Dec. 27, 2016, which is a continuation of U.S. patent application Ser. No. 15/253,964, filed Sep. 1, 2016, now U.S. Pat. No. 9,636,583, which is a continuation of U.S. patent application Ser.... | <SOH> BACKGROUND <EOH>In recent years, with the spread of electronic apparatuses such as smart phones and tablets, games played on these electronic apparatuses have been actively developed. As an example of such a game, there is a card game in which the user plays against other users or against the computer using cards... | <SOH> SUMMARY <EOH>I provide: (1) A non-transitory computer readable recording medium storing game program code instructions for a game in which a first user and a second user do battle, and when the game program code instructions are executed by a computer, the game program code instructions cause the computer to perf... | A63F1352 | 20170825 | 20171207 | 99434.0 | A63F1352 | 1 | ELISCA, PIERRE E | STORAGE MEDIUM STORING GAME PROGRAM, GAME PROCESSING METHOD, AND INFORMATION PROCESSING APPARATUS | UNDISCOUNTED | 1 | CONT-ACCEPTED | A63F | 2,017 | |
15,686,426 | PENDING | DIRECT INJECTION ENGINE AND CONTROL METHOD THEREOF | A direct injection engine includes a fuel injection valve configured to inject fuel into a cylinder, a water injection valve configured to inject water into the cylinder, and a valve variable mechanism configured to change an operation timing of each of an intake valve and an exhaust valve. During an operation in a low... | 1. A direct injection engine, comprising: a cylinder configured to accommodate a piston to be reciprocally movable; a fuel injection valve configured to inject fuel containing gasoline into the cylinder; a water injection valve configured to inject water into the cylinder; an intake valve configured to open and close a... | TECHNICAL FIELD The present invention relates to an engine configured to combust fuel containing gasoline after reforming the fuel. BACKGROUND ART As an engine configured to combust reformed fuel as described above, there is known an engine disclosed in Japanese Unexamined Patent Publication No. 2010-25031. The engine ... | <SOH> BACKGROUND ART <EOH>As an engine configured to combust reformed fuel as described above, there is known an engine disclosed in Japanese Unexamined Patent Publication No. 2010-25031. The engine disclosed in Japanese Unexamined Patent Publication No. 2010-25031 includes a cylinder, an intake passage and an exhaust ... | <SOH> SUMMARY OF INVENTION <EOH>In view of the above, an object of the present invention is to provide a direct injection engine and a control method thereof, which enable to improve fuel economy of the engine by using reformed fuel without waste. A direct injection engine according to an aspect of the present inventio... | F02D413094 | 20170825 | 20180308 | 64397.0 | F02D4130 | 0 | STAUBACH, CARL C | DIRECT INJECTION ENGINE AND CONTROL METHOD THEREOF | UNDISCOUNTED | 0 | ACCEPTED | F02D | 2,017 | |
15,686,875 | PENDING | EXERCISE SYSTEM AND METHOD | An exercise machine includes a processor, a first display, a deck, and a belt rotatable about the deck. The machine also includes a sensor operably connected to the processor and configured to detect a first performance parameter of a first user running on the belt of the exercise machine. The processor is configured t... | 1. A method, comprising: providing information about available exercise classes to a processor associated with a first exercise machine, the first exercise machine being located at a first remote location; receiving, from a first user of the first exercise machine and via the processor, a selection of one of the availa... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a nonprovisional of U.S. Provisional Application No. 62/380,412, filed Aug. 27, 2016, the entire disclosure of which is incorporated herein by reference. FIELD OF THE INVENTION This application relates generally to the field of exercise equipment and methods a... | <SOH> BACKGROUND <EOH>Humans are competitive by nature, striving to improve their performance both as compared to their own prior efforts and as compared to others. Humans are also drawn to games and other diversions, such that even tasks that a person may find difficult or annoying can become appealing if different ga... | <SOH> SUMMARY OF THE INVENTION <EOH>In an example embodiment of the present disclosure, a method includes providing information about available exercise classes to a processor associated with a first exercise machine, the first exercise machine being located at a first remote location, receiving, from a first user of t... | A63B240075 | 20170825 | 20180301 | 94831.0 | A63B2400 | 1 | ATKINSON, GARRETT K | EXERCISE SYSTEM AND METHOD | SMALL | 0 | ACCEPTED | A63B | 2,017 | |
15,687,132 | ACCEPTED | METHODS OF THERAPEUTIC MONITORING OF NITROGEN SCAVENGING DRUGS | The present disclosure provides methods for evaluating daily ammonia exposure based on a single fasting ammonia blood level measurement, as well as methods that utilize this technique to adjust the dosage of a nitrogen scavenging drug, determine whether to administer a nitrogen scavenging drug, and treat nitrogen reten... | 1-11. (canceled) 12. A method of treating a subject with a urea cycle disorder (UCD) who has a fasting morning plasma ammonia level less than the upper limit of normal, the method comprising: a) administering an initial dosage of glyceryl tri-[4-phenylbutyrate]; b) after a time period sufficient for the glyceryl tri-[4... | RELATED APPLICATIONS The present application is a divisional of U.S. patent application Ser. No. 13/417,137, filed Mar. 9, 2012 and now pending, which claims the benefit of U.S. Provisional Application No. 61/564,668, filed Nov. 29, 2011, and U.S. Provisional Application No. 61/542,100, filed Sep. 30, 2011, the disclos... | <SOH> BACKGROUND <EOH>Nitrogen retention disorders associated with elevated ammonia levels include urea cycle disorders (UCDs) and hepatic encephalopathy (HE). UCDs include several inherited deficiencies of enzymes or transporters necessary for the synthesis of urea from ammonia, including enzymes involved in the urea ... | <SOH> SUMMARY <EOH>Provided herein in certain embodiments are methods for determining whether to increase a dosage of a nitrogen scavenging drug in a subject with a nitrogen retention disorder by measuring a fasting blood ammonia level and comparing the fasting blood ammonia level to the upper limit of normal (ULN) for... | A61K31235 | 20170825 | 20180508 | 20180118 | 81418.0 | A61K31235 | 1 | RAO, SAVITHA M | METHODS OF THERAPEUTIC MONITORING OF NITROGEN SCAVENGING DRUGS | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,687,719 | PENDING | METHODS OF USING GAP JUNCTIONS AS THERAPEUTIC TARGETS FOR THE TREATMENT OF DEGENERATIVE DISORDERS OF THE RETINA | The disclosure provides methods of treating a condition of the retina by administering an inhibitor of connexin 36 and/or an inhibitor of connexin 45 to a subject with a retinal condition. This disclosure further provides compositions for the treatment of a retinal condition which include an inhibitor of connexin 36 an... | 1. A method of treating a condition of the retina comprising administering an inhibitor of connexin 36 and/or an inhibitor of connexin 45 to a subject in need thereof. 2. The method of claim 1, comprising administration of both an inhibitor of connexin 36 and an inhibitor of connexin 45. 3. The method of claims 1 or 2 ... | CROSS-REFERENCE TO RELATED APPLICATIONS The present application is a divisional of a co-pending application having U.S. Ser. No. 15/317,171, filed Dec. 8, 2016, which is a 371 of International application having Serial No. PCT/2015/035226, filed Jun. 11, 2015, which claims priority to U.S. provisional application 62/01... | <SOH> BACKGROUND OF THE DISCLOSURE <EOH>In addition to the intrinsic mechanisms underlying primary cell death, intercellular communication appears to play a major, but presently unclear, role in so-called secondary cell death (Andrade-Rozental A F, et al., Brain Res. Rev 32:308-315 (2000)). Damage in the central nervou... | <SOH> BRIEF SUMMARY OF THE DISCLOSURE <EOH>Disclosed herein are methods for treating a condition of the retina, by administering an inhibitor of connexin 36 and/or an inhibitor of connexin 45 to a subject with a retinal condition. In some embodiments, both an inhibitor of connexin 36 and an inhibitor of connexin 45 are... | A61K38177 | 20170828 | 20171214 | 57985.0 | A61K3817 | 0 | SHIN, DANA H | METHODS OF USING GAP JUNCTIONS AS THERAPEUTIC TARGETS FOR THE TREATMENT OF DEGENERATIVE DISORDERS OF THE RETINA | SMALL | 1 | CONT-PENDING | A61K | 2,017 | |
15,688,305 | ACCEPTED | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | Provided herein are peptide formulations comprising polymers as stabilizing agents. The peptide formulations can be more stable for prolonged periods of time at temperatures higher than room temperature when formulated with the polymers. The polymers used in the present invention can decrease the degradation of the con... | 1-15. (canceled) 16. A method of increasing blood pressure in a human in need thereof, the method comprising: administering to the human a pharmaceutical composition that comprises, in a unit dosage form: i) from about 0.1 μg/mL to about 2 μg/mL of vasopressin or a pharmaceutically-acceptable salt thereof; dextrose; ac... | CROSS REFERENCE This application is a continuation of U.S. application Ser. No. 15/612,649, filed Jun. 2, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/426,693, filed Feb. 7, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/289,640, filed Oct. 10, 2016, which is a continuati... | <SOH> BACKGROUND <EOH>Vasopressin is a potent endogenous hormone, responsible for maintaining plasma osmolality and volume in most mammals. Vasopressin can be used clinically in the treatment of sepsis and cardiac conditions, and in the elevation of patient's suffering from low blood pressure. Current formulations of v... | <SOH> SUMMARY OF THE INVENTION <EOH>In some embodiments, the invention provides a pharmaceutical composition comprising, in a unit dosage form: a) from about 0.01 mg/mL to about 0.07 mg/mL of vasopressin, or a pharmaceutically-acceptable salt thereof; and b) a polymeric pharmaceutically-acceptable excipient in an amoun... | A61K3811 | 20170828 | 20180529 | 20180104 | 67193.0 | A61K3811 | 1 | BRADLEY, CHRISTINA | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,688,314 | ACCEPTED | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | Provided herein are peptide formulations comprising polymers as stabilizing agents. The peptide formulations can be more stable for prolonged periods of time at temperatures higher than room temperature when formulated with the polymers. The polymers used in the present invention can decrease the degradation of the con... | 1-15. (canceled) 16. A method of increasing blood pressure in a human in need thereof, the method comprising: administering to the human a pharmaceutical composition that comprises, in a unit dosage form: i) from about 0.1 μg/mL to about 2 μg/mL of vasopressin or a pharmaceutically-acceptable salt thereof; dextrose; ac... | CROSS REFERENCE This application is a continuation of U.S. application Ser. No. 15/612,649, filed Jun. 2, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/426,693, filed Feb. 7, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/289,640, filed Oct. 10, 2016, which is a continuati... | <SOH> BACKGROUND <EOH>Vasopressin is a potent endogenous hormone, responsible for maintaining plasma osmolality and volume in most mammals. Vasopressin can be used clinically in the treatment of sepsis and cardiac conditions, and in the elevation of patient's suffering from low blood pressure. Current formulations of v... | <SOH> SUMMARY OF THE INVENTION <EOH>In some embodiments, the invention provides a pharmaceutical composition comprising, in a unit dosage form: a) from about 0.01 mg/mL to about 0.07 mg/mL of vasopressin, or a pharmaceutically-acceptable salt thereof; and b) a polymeric pharmaceutically-acceptable excipient in an amoun... | A61K3811 | 20170828 | 20180508 | 20180104 | 67193.0 | A61K3811 | 1 | BRADLEY, CHRISTINA | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,688,326 | ACCEPTED | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | Provided herein are peptide formulations comprising polymers as stabilizing agents. The peptide formulations can be more stable for prolonged periods of time at temperatures higher than room temperature when formulated with the polymers. The polymers used in the present invention can decrease the degradation of the con... | 1-15. (canceled) 16. A method of increasing blood pressure in a human in need thereof, the method comprising: administering to the human a pharmaceutical composition that comprises, in a unit dosage form: i) from about 0.1 μg/mL to about 2 μg/mL of vasopressin or a pharmaceutically-acceptable salt thereof; dextrose; ac... | CROSS REFERENCE This Application is a continuation of U.S. application Ser. No. 15/612,649, filed Jun. 2, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/426,693, filed Feb. 7, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/289,640, filed Oct. 10, 2016, which is a continuati... | <SOH> BACKGROUND <EOH>Vasopressin is a potent endogenous hormone, responsible for maintaining plasma osmolality and volume in most mammals. Vasopressin can be used clinically in the treatment of sepsis and cardiac conditions, and in the elevation of patient's suffering from low blood pressure. Current formulations of v... | <SOH> SUMMARY OF THE INVENTION <EOH>In some embodiments, the invention provides a pharmaceutical composition comprising, in a unit dosage form: a) from about 0.01 mg/mL to about 0.07 mg/mL of vasopressin, or a pharmaceutically-acceptable salt thereof; and b) a polymeric pharmaceutically-acceptable excipient in an amoun... | A61K3811 | 20170828 | 20180703 | 20180104 | 67193.0 | A61K3811 | 1 | BRADLEY, CHRISTINA | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,688,336 | ACCEPTED | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | Provided herein are peptide formulations comprising polymers as stabilizing agents. The peptide formulations can be more stable for prolonged periods of time at temperatures higher than room temperature when formulated with the polymers. The polymers used in the present invention can decrease the degradation of the con... | 1-15. (canceled) 16. A method of increasing blood pressure in a human in need thereof, the method comprising: administering to the human a unit dosage form, wherein the unit dosage form comprises from about 0.1 units/mL to about 1 unit/mL of vasopressin or the pharmaceutically-acceptable salt thereof, wherein the unit ... | CROSS REFERENCE This application is a continuation of U.S. application Ser. No. 15/612,649, filed Jun. 2, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/426,693, filed Feb. 7, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/289,640, filed Oct. 10, 2016, which is a continuati... | <SOH> BACKGROUND <EOH>Vasopressin is a potent endogenous hormone, responsible for maintaining plasma osmolality and volume in most mammals. Vasopressin can be used clinically in the treatment of sepsis and cardiac conditions, and in the elevation of patient's suffering from low blood pressure. Current formulations of v... | <SOH> SUMMARY OF THE INVENTION <EOH>In some embodiments, the invention provides a pharmaceutical composition comprising, in a unit dosage form: a) from about 0.01 mg/mL to about 0.07 mg/mL of vasopressin, or a pharmaceutically-acceptable salt thereof; and b) a polymeric pharmaceutically-acceptable excipient in an amoun... | A61K3811 | 20170828 | 20180515 | 20171221 | 67193.0 | A61K3811 | 1 | BRADLEY, CHRISTINA | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,688,338 | ACCEPTED | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | Provided herein are peptide formulations comprising polymers as stabilizing agents. The peptide formulations can be more stable for prolonged periods of time at temperatures higher than room temperature when formulated with the polymers. The polymers used in the present invention can decrease the degradation of the con... | 1-15. (canceled) 16. A pharmaceutical composition for intravenous administration comprising, in a unit dosage form: from about 0.01 mg/mL to about 0.07 mg/mL of vasopressin or a pharmaceutically-acceptable salt thereof; impurities that are present in an amount of 0.9% to 1.7%, wherein the impurities have from about 85%... | CROSS REFERENCE This application is a continuation of U.S. application Ser. No. 15/612,649, filed Jun. 2, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/426,693, filed Feb. 7, 2017, which is a continuation-in-part of U.S. application Ser. No. 15/289,640, filed Oct. 10, 2016, which is a continuati... | <SOH> BACKGROUND <EOH>Vasopressin is a potent endogenous hormone, responsible for maintaining plasma osmolality and volume in most mammals. Vasopressin can be used clinically in the treatment of sepsis and cardiac conditions, and in the elevation of patient's suffering from low blood pressure. Current formulations of v... | <SOH> SUMMARY OF THE INVENTION <EOH>In some embodiments, the invention provides a pharmaceutical composition comprising, in a unit dosage form: a) from about 0.01 mg/mL to about 0.07 mg/mL of vasopressin, or a pharmaceutically-acceptable salt thereof; and b) a polymeric pharmaceutically-acceptable excipient in an amoun... | A61K3811 | 20170828 | 20180320 | 20180118 | 67193.0 | A61K3811 | 1 | BRADLEY, CHRISTINA | VASOPRESSIN FORMULATIONS FOR USE IN TREATMENT OF HYPOTENSION | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,688,347 | PENDING | THIRD-PARTY PROVIDER METHOD AND SYSTEM | Methods and systems for processing negotiable economic credits through, or at the request of, a hand held device in association with a third-party provider communicative with the hand held device and/or a point of sale. At least one negotiable economic credit can be transferred from a third-party provider communicative... | 1.-20. (canceled) 21. A device comprising: a processor; a wireless controller configured to transmit and receive data through a wireless data communication network; and a memory having instructions stored thereon that are executable by the processor to cause the device to perform operations comprising: storing a data s... | CROSS-REFERENCE TO RELATED PATENT APPLICATIONS This application is a continuation of U.S. application Ser. No. 13/082,243, filed Apr. 7, 2011 which is a divisional of U.S. application Ser. No. 09/962,675, filed Sep. 25, 2001 which claims priority to Provisional Application U.S. Application 60/238,568, filed Oct. 6, 200... | <SOH> BACKGROUND <EOH> | <SOH> SUMMARY <EOH>It is therefore an aspect of the present invention to provide improved methods and systems for conducting E-commerce utilizing hand held devices. It is another aspect of the present invention to provide improved methods and systems for processing negotiable economic data (e.g., coupons, cash, credits... | G06Q3002 | 20170828 | 20180215 | 65555.0 | G06Q3002 | 3 | RUDY, ANDREW J | THIRD-PARTY PROVIDER METHOD AND SYSTEM | UNDISCOUNTED | 1 | CONT-ACCEPTED | G06Q | 2,017 | |
15,689,076 | PENDING | Process for Making Tablet Using Radiofrequency and Lossy Coated Particles | In one aspect the present invention features process for making a tablet comprising at least one pharmaceutically active agent, said method comprising the step of applying radiofrequency energy to a powder blend to sinter said powder blend into said tablet, wherein said powder blend comprises lossy coated particles and... | 1. A tablet comprising sintered lossy coated particles and at least one pharmaceutically active agent, wherein said lossy coated particles comprise a substrate that is at least partially coated with a lossy coating comprising at least one activator, wherein said substrate has a Q value of greater than 100 and said acti... | CROSS REFERENCE TO RELATED APPLICATIONS This application is a divisional application which claims the benefit U.S. patent application Ser. No. 14/592,176, filed Jan. 8, 2015, which also claims priority of the benefits of U.S. Provisional Application Ser. No. 61/925,713, filed Jan. 10, 2014. The complete disclosure of t... | <SOH> BACKGROUND OF THE INVENTION <EOH>Pharmaceuticals intended for oral administration are typically provided in tablet form. Tablets can be swallowed whole, chewed in the mouth, or disintegrated in the oral cavity. Soft tablets that either are chewed or dissolve in the mouth are often employed in the administration o... | <SOH> SUMMARY OF THE INVENTION <EOH>In one aspect, the present invention features a process for making a tablet comprising at least one pharmaceutically active agent, said method comprising the step of applying radiofrequency energy to a powder blend to sinter said powder blend into said tablet, wherein said powder ble... | A61K92095 | 20170829 | 20171214 | 80807.0 | A61K920 | 0 | VANHORN, ABIGAIL LOUISE | Process for Making Tablet Using Radiofrequency and Lossy Coated Particles | UNDISCOUNTED | 1 | CONT-REJECTED | A61K | 2,017 | |
15,689,491 | PENDING | BOOTSTRAPPED SWITCHING CIRCUIT | The trend in wireless communication receivers is to capture more and more bandwidth to support higher throughput, and to directly sample the radio frequency (RF) signal to enable re-configurability and lower cost. Other applications like instrumentation also demand the ability to digitize wide bandwidth RF signals. The... | 1. A bootstrapped switching circuit with accelerated turn on, comprising: a sampling switch receiving a voltage input signal and a gate voltage; a bootstrapped voltage generator comprising a positive feedback loop to generate the gate voltage for turning on the sampling switch, said positive feedback loop comprising an... | PRIORITY DATA AND RELATED APPLICATIONS This patent application receives benefit from and/or claim priority to U.S. Provisional Patent Application Ser. No. 62/393,529, filed on Sep. 12, 2016, entitled “INPUT BUFFER AND BOOTSTRAPPED SWITCHING CIRCUIT”. This U.S. Provisional Patent Application is incorporated by reference... | <SOH> BACKGROUND <EOH>In many electronics applications, an analog-to-digital converter (ADC) converts an analog input signal to a digital output signal, e.g., for further digital signal processing or storage by digital electronics. Broadly speaking, ADCs can translate analog electrical signals representing real-world p... | <SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>To provide a more complete understanding of the present disclosure and features and advantages thereof, reference is made to the following description, taken in conjunction with the accompanying figures, wherein like reference numerals represent like parts, in which: FIG. 1 ... | H03K1704123 | 20170829 | 20180315 | 68652.0 | H03K170412 | 1 | WELLS, KENNETH B | BOOTSTRAPPED SWITCHING CIRCUIT | UNDISCOUNTED | 0 | ACCEPTED | H03K | 2,017 | |
15,689,779 | PENDING | Selectively Locking Merchandising Member | A merchandising system includes an elongated mounting member having a wall with at least one tooth and a cooperating member having a front end receivable on the mounting member. The cooperating member can include a slot defined in the front end. A lock is received in the slot. The lock includes at least one tooth locat... | 1-20. (canceled) 21. A merchandising system comprising: a cooperating member including a front end defining a slot and a chamber accessible through the slot; a mounting member including a front wall at least partially defining a channel configured to receive the front end of the cooperating member, the front wall havin... | This application claims the benefit of Provisional Application Ser. No. 62/144,672 which was filed on Apr. 8, 2015. The entire content of that application is incorporated hereinto by reference. BACKGROUND The present disclosure pertains to a merchandising system. More specifically, the disclosure relates to a base and ... | <SOH> BACKGROUND <EOH>The present disclosure pertains to a merchandising system. More specifically, the disclosure relates to a base and divider assembly employed in a forward feeding display merchandising system for storing and displaying merchandise of a variety of shapes and sizes and automatically delivering the me... | <SOH> BRIEF SUMMARY OF THE DISCLOSURE <EOH>In accordance with one embodiment of the present disclosure, a merchandising system comprises an elongated mounting member including a wall, the wall comprising at least one tooth and a cooperating member including a front end. The front end is adapted to be received on the mo... | A47F1125 | 20170829 | 20180215 | 73203.0 | A47F112 | 0 | NOVOSAD, JENNIFER ELEANORE | Selectively Locking Merchandising Member | UNDISCOUNTED | 1 | CONT-ACCEPTED | A47F | 2,017 | |
15,689,947 | PENDING | LED LIGHT TUBE END CAP WITH SELF-DOCKING DRIVER COMM BOARD | An LED light tube assembly comprising an LED light tube with an LED array board in a tubular housing, and an end cap with a driver board removably secured to the end of the LED light tube. The driver board extends from a cap midpoint at a first level corresponding to an underside of the LED board in the tube, and the c... | 1. An LED light tube assembly comprising an LED light tube comprising an LED board mounted in a tubular housing including a translucent cover and a sidewall portion opposite the translucent cover, and a removable end cap assembly with external electrical connector terminals, wherein: the end cap assembly comprises an e... | RELATED APPLICATIONS/PRIORITY BENEFIT CLAIM This application claims the benefit of U.S. Provisional Application No. 62/381,111, filed Aug. 30, 2016 by the same inventor (Thiel), the entirety of which provisional application is hereby incorporated by reference. FIELD The subject matter of the present application is in t... | <SOH> BACKGROUND <EOH>Large scale lighting systems for businesses, industrial operations, educational institutions, hospitals and similar have traditionally used fluorescent light fixtures with replaceable fluorescent light tubes. These fluorescent tubes are increasingly being replaced with LED (light emitting diode) l... | <SOH> BRIEF SUMMARY <EOH>The present invention is an improved structure for replaceably assembling a separate LED driver and/or wireless communication board (hereafter driver board or driver comm board) to an LED light tube of the type used in large scale tube-lighting fixture environments. In a first aspect, the inven... | F21K9272 | 20170829 | 20180301 | 64415.0 | F21K9272 | 0 | GUDORF, LAURA A | LED LIGHT TUBE END CAP WITH SELF-DOCKING DRIVER COMM BOARD | SMALL | 0 | ACCEPTED | F21K | 2,017 | |
15,690,640 | PENDING | DIGITAL INFORMATION RECORDING APPARATUS, REPRODUCING APPARATUS AND TRANSMITTING APPARATUS | A digital information recording apparatus includes a recording circuit for recording information of a retention period included in the digital information and indicating a period for permitting the digital information to be held in the recording medium, starting with a time at which the digital information is recorded ... | 1. A digital information recording apparatus for recording digital information including video information and/or audio information on a first recording medium, comprising: a recording circuit for recording move permission information included in said digital information; said move permission information permitting sai... | CROSS REFERENCE TO RELATED APPLICATION This application is a Continuation of U.S. application Ser. No. 14/713,515, filed May 15, 2015, which is a Continuation of U.S. application Ser. No. 13/649,882, filed Oct. 11, 2012, now U.S. Pat. No. 9,083,942, issued Jul. 14, 2015, which is a Continuation of U.S. application Ser.... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>Various kinds of expedience disclosed in the above documents give a solution to the problems. But the problem involved in copyright cannot be solved satisfactorily by the conventional methods that inflict one-sided profit or loss to copyright holders, broadcasting or software develop... | G11B2000688 | 20170830 | 20171221 | 61391.0 | G11B2000 | 1 | ZHAO, DAQUAN | DIGITAL INFORMATION RECORDING APPARATUS, REPRODUCING APPARATUS AND TRANSMITTING APPARATUS | UNDISCOUNTED | 1 | CONT-ACCEPTED | G11B | 2,017 | |
15,691,134 | PENDING | ELECTRONIC EQUIPMENT DATA CENTER OR CO-LOCATION FACILITY DESIGNS AND METHODS OF MAKING AND USING THE SAME | The present invention relates to electronic equipment data center or co-location facility designs and methods of making and using the same in an environmentally aware manner, and generally provides apparatus and methods for using novel support bracket structures, and thermal panels associated with the same, that allow ... | 1. A structure for managing heat emitted by electronic equipment comprising: at least one cluster of cabinets disposed in two separated rows such that the rows of cabinets are positioned in a back-to-back configuration to establish a hot aisle enclosure area between the two separated rows and the front side of the cabi... | CROSS REFERENCE TO RELATED APPLICATIONS This application is a continuation of and claims priority to U.S. application Ser. No. 12/168,771 filed on Jun. 13, 2008, which claims priority to U.S. Provisional Appln. No. 60/944,082 filed Jun. 14, 2007 entitled “Electronic Equipment Data Center or Co-Location Facility Designs... | <SOH> BACKGROUND <EOH>Data centers and server co-location facilities are well-known. In such facilities, rows of electronics equipment, such as servers, typically owned by different entities, are stored. In many facilities, cabinets are used in which different electronics equipment is stored, so that only the owners of... | <SOH> SUMMARY OF THE INVENTION <EOH>The present invention relates to electronic equipment data center or co-location facility designs and methods of making and using the same in an environmentally aware manner. The present invention generally provides apparatus and methods for using novel support bracket structures, an... | H05K720 | 20170830 | 20180215 | 92371.0 | H05K720 | 2 | PROBST, SAMANTHA A | ELECTRONIC EQUIPMENT DATA CENTER OR CO-LOCATION FACILITY DESIGNS AND METHODS OF MAKING AND USING THE SAME | UNDISCOUNTED | 1 | CONT-ACCEPTED | H05K | 2,017 | |
15,691,144 | PENDING | COMMUNICATIVE WATER BOTTLE AND SYSTEM THEREOF | A communicative water bottle includes communication logic and wireless transmission logic technology electronically connected with a variety of sensors either on the water bottle or located remote from the water bottle. The sensors on the bottle create digital data associated with amount of fluid in the bottle and chan... | 1. A communicative sports water bottle system comprising: a bottle body having a base and an upwardly extending sidewall therein defining a fluid chamber and a first display coupled to the bottle body; a sensor determining one or more of the following an amount of fluid in the fluid chamber, an amount of fluid being di... | CROSS REFERENCE TO RELATED APPLICATION This is a continuation application from prior U.S. patent application Ser. No. 14/657,300 filed on Mar. 13, 2015; the entirety of which is herein incorporated by reference as if fully rewritten. BACKGROUND Technical Field The present disclosure relates generally to the field of he... | <SOH> BACKGROUND <EOH> | <SOH> SUMMARY <EOH>Issues continue to exist with activity trackers and health monitoring mobile applications inasmuch as they require the manual entry of hydration information. A need continues to exist for a water bottle having the ability to calculate an amount of water consumed therefrom to directly sync with a remo... | G06F193418 | 20170830 | 20171221 | 81456.0 | G06F1900 | 3 | GRANT, MICHAEL CHRISTOPHER | COMMUNICATIVE WATER BOTTLE AND SYSTEM THEREOF | SMALL | 1 | CONT-ACCEPTED | G06F | 2,017 | |
15,691,378 | ACCEPTED | UNIVERSAL SECURE REGISTRY | An authentication system and method of use are provided to enable a transaction involving a first party and a user, the system comprising an electronic device comprising a communications interface and one or more processors. The one or more processors are configured to receive biometric information of the user and gene... | 1. An authentication system to enable a transaction involving a first party and a user, the system comprising: an electronic device comprising a communications interface and one or more processors; wherein the one or more processors are configured to: receive biometric information of the user; and generate a one-time c... | RELATED APPLICATIONS This application is a continuation of and also claims priority under 35 U.S.C. §120 to co-pending U.S. patent application Ser. No. 15/040,873 filed on Feb. 10, 2016, entitled UNIVERSAL SECURE REGISTRY, which is a continuation of and also claims priority under 35 U.S.C. §120 to co-pending U.S. paten... | <SOH> BACKGROUND OF INVENTION <EOH> | <SOH> SUMMARY OF INVENTION <EOH>There is thus a need for an identification system that will enable a person to be identified or verified (“identification” sometimes being used hereinafter to mean either identified or verified) and/or authenticated without necessitating the provision of any personal information. Likewis... | G06Q20204 | 20170830 | 20180327 | 20171221 | 77435.0 | G06Q2020 | 1 | CRAWLEY, TALIA F | UNIVERSAL SECURE REGISTRY | SMALL | 1 | CONT-ACCEPTED | G06Q | 2,017 |
15,691,884 | PENDING | Portable vehicle battery jump start apparatus with safety protection | A handheld device for jump starting a vehicle engine includes a rechargeable lithium ion battery pack (32) and a microcontroller (1). The lithium ion battery is coupled to a power output port of the device through a power switch circuit (15) actuated by the microcontroller. A vehicle battery isolation sensor (12) conne... | 1. Apparatus for jump starting a vehicle engine, comprising: an internal power supply; an output port having positive and negative polarity outputs; a vehicle battery isolation sensor connected in circuit with said positive and negative polarity outputs, configured to detect presence of a vehicle battery connected betw... | FIELD OF THE INVENTION The present invention relates generally to apparatus for jump-starting a vehicle having a depleted or discharged battery. BACKGROUND TO THE INVENTION Prior art devices are known for jump-starting a vehicle, which provide either a pair of electrical connector cables that connect a fully-charged ba... | <SOH> BACKGROUND TO THE INVENTION <EOH>Prior art devices are known for jump-starting a vehicle, which provide either a pair of electrical connector cables that connect a fully-charged battery of another vehicle to the engine start circuit of the dead battery vehicle, or portable booster devices which include a fully-ch... | <SOH> SUMMARY OF THE INVENTION <EOH>In accordance with an aspect of the invention, an apparatus is provided for jump starting a vehicle engine, comprising: an internal power supply; an output port having positive and negative polarity outputs; a vehicle battery isolation sensor connected in circuit with said positive a... | B60L111816 | 20170831 | 20180426 | 60923.0 | B60L1118 | 2 | DIAO, M BAYE | Portable vehicle battery jump start apparatus with safety protection | SMALL | 1 | CONT-ACCEPTED | B60L | 2,017 | |
15,692,893 | PENDING | VEGF ANTAGONIST FORMULATIONS | Formulations of a vascular endothelial growth factor (VEGF)-specific fusion protein antagonist are provided including a pre-lyophilized formulation, a reconstituted lyophilized formulation, and a stable liquid formulation. Preferably, the fusion protein has the sequence of SEQ ID NO:4. | 1. A mammalian cell comprising a polynucleotide that encodes a fusion protein, wherein said fusion protein comprises an immunoglobulin-like (Ig) domain 2 of a first VEGF receptor, an Ig domain 3 of a second VEGF receptor, and a multimerizing component; wherein said fusion protein does not comprise a signal peptide and ... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 15/342,989, filed on Nov. 3, 2016, which is a continuation of U.S. patent application Ser. No. 15/064,343, filed on Mar. 8, 2016 and granted on Dec. 6, 2016 as U.S. Pat. No. 9,511,140, which is a continuation ... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> BRIEF SUMMARY OF THE INVENTION <EOH>Stable formulations of a VEGF-specific fusion protein antagonist are herein provided. The pharmaceutically acceptable formulations of the invention comprise the VEGF “trap” antagonist with a pharmaceutically acceptable carrier. In specific embodiments, liquid and freeze-dried, ... | A61K3939591 | 20170831 | 20171221 | 66200.0 | A61K39395 | 1 | STOICA, ELLY GERALD | METHOD OF MANUFACTURING VEGF ANTAGONIST FUSION PROTEINS | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 | |
15,693,163 | PENDING | SEEDING MACHINE WITH SEED DELIVERY SYSTEM | A seed delivery system for a seeding machine having a seed meter comprises a housing that defines an upper seed loading area and a lower seed discharge area. A drive pulley is mounted to rotate with respect to the housing. A belt is supported for rotation by the drive pulley within the housing. A loading wheel is mount... | 1. A seed delivery system for a seeding machine having a seed meter, the system comprising: a housing defining an upper seed loading area and a lower seed discharge area; a drive pulley mounted to rotate with respect to the housing; a belt having a base supported for rotation by the drive pulley within the housing; and... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a Continuation of U.S. patent application Ser. No. 14/616,877, filed Feb. 9, 2015, which is a Continuation of U.S. patent application Ser. No. 14/504,801, filed Oct. 2, 2014, now U.S. Pat. No. 9,686,905, which is a Continuation of U.S. patent application Ser. ... | <SOH> BACKGROUND OF THE INVENTION <EOH>An agricultural seeding machine such as a row crop planter or grain drill places seeds at a desired depth within a plurality of parallel seed trenches formed in soil. In the case of a row crop planter, a plurality of row crop units are typically ground driven using wheels, shafts,... | <SOH> SUMMARY OF THE INVENTION <EOH>A seed delivery system for a seeding machine having a seed meter comprises a housing that defines an upper seed loading area and a lower seed discharge area. A drive pulley is mounted to rotate with respect to the housing. A belt is supported for rotation by the drive pulley within t... | A01C716 | 20170831 | 20171221 | 99684.0 | A01C716 | 2 | NOVOSAD, CHRISTOPHER J | SEEDING MACHINE WITH SEED DELIVERY SYSTEM | UNDISCOUNTED | 1 | CONT-ACCEPTED | A01C | 2,017 | |
15,693,418 | PENDING | OPTICAL IMAGING SYSTEM | An optical imaging system includes, in order from an object side to an image side, a first lens element with positive refractive power, a second lens element, a third lens element, a fourth lens element, and a fifth lens element. Each of the fourth lens element and the fifth lens element includes at least one aspheric ... | 1. An optical imaging system comprising five lens elements, the five lens elements being, in order from an object side to an image side: a first lens element; a second lens element having an object-side surface being convex in a paraxial region thereof; a third lens element with negative refractive power having an imag... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation application of U.S. patent application Ser. No. 15/468,079 filed Mar. 23, 2017, entitled “OPTICAL IMAGING SYSTEM”, by Chun-Shan CHEN, Tsung-Han TSAI and Hsin-Hsuan HUANG, which is a continuation application of U.S. patent application Ser. No. 14... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>In response to the trend of development of miniature electronics and to solve the aforementioned problems, the present invention provides an optical imaging system designed for compact portable electronics and capable of improving the imaging quality of the optical imaging system. Ac... | G02B130045 | 20170831 | 20171221 | 76070.0 | G02B1300 | 1 | PICHLER, MARIN | OPTICAL IMAGING SYSTEM | UNDISCOUNTED | 1 | CONT-ACCEPTED | G02B | 2,017 | |
15,694,786 | PENDING | Exclusive Delivery of Content Within Geographic Areas | Application developers can request to have their applications registered for use with a content delivery platform. The operator of the content delivery platform establishes perimeters defining geographic areas, and maintains records reserving particular areas for delivery of content associated with particular sponsors.... | 1. A mobile device comprising: memory; at least one processor operably coupled to the memory; a location-determination component; and at least one module configured for execution by the at least one processor, wherein the at least one module comprises at least one instruction for: receiving, from an application program... | CROSS REFERENCE TO RELATED APPLICATIONS This continuation patent application claims priority from co-pending U.S. Non-provisional patent application having Ser. No. 15/009,961, filed 29 Jan. 2016, entitled “EXCLUSIVE DELIVERY OF CONTENT WITHIN GEOGRAPHIC AREAS”, which claims priority from co-pending U.S. Non-provisiona... | <SOH> BACKGROUND <EOH>Advertisements can be delivered to various devices, including mobile devices, within communications range of areas transmitters or other information providers. For example, advertisements can be delivered to cellular phones within range of a particular cellular phone provider's network area. Furth... | <SOH> SUMMARY <EOH>Various embodiments disclosed herein include registering an application program for use with a content delivery platform, establishing multiple perimeters defining respective geographic areas, and maintaining records associating sponsors with particular geographic areas. The content delivery platform... | G06Q300261 | 20170902 | 20171221 | 90633.0 | G06Q3002 | 2 | AJIBADE AKONAI, OLUMIDE | Exclusive Delivery of Content Within Geographic Areas | SMALL | 1 | CONT-ACCEPTED | G06Q | 2,017 | |
15,695,133 | PENDING | SYSTEMS AND METHODS OF MODIFYING TURBINE ENGINE OPERATING LIMITS | The present disclosure is directed to systems and methods of modifying turbine engine operating limits due to the intake of particulate matter. More specifically, the present disclosure is directed to the use of a sensor at the inlet of a turbine engine to measure the characteristics of particulate flow into the turbin... | 1. A method for modifying a life cycle schedule in a turbine engine, wherein the life cycle schedule is determined based on a predetermined operational profile of the turbine engine and empirical data, the method comprising detecting in real time the presence of particulate matter in fluid flow entering an inlet of the... | CROSS REFERENCE TO RELATED APPLICATION The present application claims priority to U.S. Provisional Patent Application No. 62/383,654, filed Sep. 6, 2016, the entirety of which is hereby incorporated by reference. FIELD OF THE DISCLOSURE The present disclosure relates generally to measuring particulate matter in fluid f... | <SOH> BACKGROUND <EOH>Turbine engines are generally operated based on a set of operating limits which can be both real-time (maximum temperature, pressure ranges, etc.) and long-term (maximum operating hours in engine lifespan). Operating limits can be adjusted based on turbine engine performance to ensure safe engine ... | <SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>The following will be apparent from elements of the figures, which are provided for illustrative purposes and are not necessarily to scale. FIG. 1 is a flow diagram of a method of modifying engine operational limits in accordance with some embodiments of the present disclosu... | G07C50808 | 20170905 | 20180308 | 75849.0 | G07C508 | 0 | BLOSS, STEPHANIE E | SYSTEMS AND METHODS OF MODIFYING TURBINE ENGINE OPERATING LIMITS | UNDISCOUNTED | 0 | REJECTED | G07C | 2,017 | |
15,695,692 | PENDING | Crimping Tool Locator and Crimping Tool | The invention relates to a crimping tool locator (12) for a crimping tool (1), especially crimping plier (2). The crimping tool locator (12) comprises an accommodating body (14) with at least one accommodation (21) for a workpiece (10), especially a plug (11). The accommodating body (14) comprises a securing device (24... | 1. A crimping tool locator for defining a position and/or orientation of a workpiece relative to a crimping tool, the crimping tool locator comprising an accommodating body with at least one accommodation for the workpiece, said accommodating body comprising a securing device by which the workpiece is securable in the ... | CROSS REFERENCE TO RELATED APPLICATIONS This application claims priority to co-pending European Patent Application No. EP 16 190 245.7 filed Sep. 22, 2016. FIELD OF THE INVENTION The invention relates to a crimping tool locator and a crimping tool with a crimping tool locator. A crimping by means of the crimping tool c... | <SOH> BACKGROUND OF THE INVENTION <EOH>During the crimping over a working stroke of crimping pliers, the plug is plastically deformed and pressed against the end of the cable arranged in the plug. In this way on one hand an electrical contact is established and on the other hand a mechanical connection between the plug... | <SOH> SUMMARY OF THE INVENTION <EOH>It is an object of the present invention to propose a crimping tool locator which is improved with respect to usage especially considering the demands of construction space. Furthermore, it is an object of the invention to propose a correspondingly improved crimping tool. The crimpin... | H01R43042 | 20170905 | 20180322 | 99929.0 | H01R43042 | 0 | ISLAM, AMER | Crimping Tool Locator and Crimping Tool | SMALL | 0 | PENDING | H01R | 2,017 | |
15,695,898 | PENDING | INDEPENDENTLY CONTROLLED METER ROLLERS AND AIR CONVEYANCE COMPONENTS SYSTEM AND METHOD | The present disclosure includes an agricultural system having first and second product meters configured to meter product to first and second lines, respectively. First and second motors are coupled to the first and second product meters and configured to drive them at first and second metering rates, respectively. An ... | 1. A method of operating a product distribution system of an agricultural implement, comprising: receiving, at a processor, a first signal indicative of a first number of first outlets fluidly coupled to a first meter that meters product from a product tank; receiving, at the processor, a second signal indicative of a ... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a divisional of U.S. patent application Ser. No. 14/932,817, entitled “INDEPENDENTLY CONTROLLED METER ROLLERS AND AIR CONVEYANCE COMPONENTS SYSTEM AND METHOD,” filed Nov. 4, 2015, which claims priority from and the benefit of U.S. Provisional Application Ser. ... | <SOH> BACKGROUND <EOH>The present disclosure relates generally to product distribution systems for agricultural implements and, more particularly, to independent control of meter rollers and air conveyance components of the product distribution system. Generally, agricultural implements (e.g., seeders) are configured t... | <SOH> BRIEF DESCRIPTION <EOH>Certain embodiments commensurate in scope with the present disclosure are summarized below. These embodiments are not intended to limit the scope of the disclosure, but rather these embodiments are intended only to provide a brief summary of possible forms of the disclosure. Indeed, the dis... | A01C7081 | 20170905 | 20171221 | 66662.0 | A01C708 | 0 | DILLON JR, JOSEPH A | INDEPENDENTLY CONTROLLED METER ROLLERS AND AIR CONVEYANCE COMPONENTS SYSTEM AND METHOD | UNDISCOUNTED | 1 | CONT-ACCEPTED | A01C | 2,017 | |
15,696,468 | PENDING | CONNECTOR | A connector includes a housing and a lock arm that extends from the housing and is engageable with a counterpart connector. The lock arm includes a first arm a has a shape of a cantilever beam and has a locking hole for being engaged with the counterpart connector at a free end side of the first arm, and a second arm t... | 1. A connector comprising: a housing; and a lock arm that extends from the housing and is engageable with a counterpart connector, wherein the lock arm includes: a first arm that has a shape of a cantilever beam and has a locking hole for being engaged with the counterpart connector at a free end side of the first arm;... | CROSS REFERENCE TO RELATED APPLICATION This application is based on Japanese Patent Application No. 2016-177773 filed on Sep. 12, 2016, the contents of which are incorporated herein by reference. BACKGROUND OF THE INVENTION 1. Technical Field The present invention relates to a connector including a housing and a lock a... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>In order to achieve the above object, a connector according to the invention is characterized as following (1) and (2) below. (1) A connector includes a housing and a lock arm that extends from the housing and is engageable with a counterpart connector. The lock arm includes a first ... | H01R1362966 | 20170906 | 20180315 | 76069.0 | H01R13629 | 0 | HARCUM, MARCUS E | CONNECTOR WITH A LOCK ARM | UNDISCOUNTED | 0 | ACCEPTED | H01R | 2,017 | |
15,696,581 | PENDING | METAL EXTRUSION PLATE AND DISPLAY STAND FORMED BY THE SAME | A metal extrusion plate for a display stand and the display stand are provided. The metal extrusion plate extends along a first direction and comprises N of flat plate sections and N−1 of connecting sections, wherein the flat plate sections are integrally formed with the connecting sections, and N is a positive integer... | 1. A metal extrusion plate for a display stand, the metal extrusion plate extending along a first direction and comprising N flat plate sections and N−1 connecting sections, wherein the flat plate sections are integrally formed with the connecting sections, N is a positive integer greater than 1, the flat plate section... | CROSS REFERENCE TO RELATED APPLICATION This application claims the benefit of U.S. Provisional Application Ser. No. 62/399,905 filed on Sep. 26, 2016, and the benefit of Taiwan Patent Application Serial No. 105216808 filed on Nov. 3, 2016. The entirety of each said application is incorporated herein by reference. BACKG... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>One objective of the present invention is to provide a display stand which has a slim structure and is capable of minimizing the unfavorable visual effect occupied by the stand from the view of the user. Another objective of the present invention is to provide a metal extrusion plate... | F16M11046 | 20170906 | 20180329 | 87489.0 | F16M1104 | 1 | STERLING, AMY JO | METAL EXTRUSION PLATE AND DISPLAY STAND FORMED BY THE SAME | UNDISCOUNTED | 0 | ACCEPTED | F16M | 2,017 | |
15,696,591 | PENDING | CODING/DECODING METHOD, APPARATUS, AND SYSTEM FOR AUDIO SIGNAL | Embodiments of the present application provide a coding/decoding method, apparatus, and system. According to the coding method, de-emphasis processing is performed on a full band signal by using a de-emphasis parameter determined according to a characteristic factor of an input audio signal, and then the full band sign... | 1. A coding method performed by a coder, comprising: obtaining an input audio signal; determining one or more characteristic factors of a low frequency band signal of the input audio signal; coding a high frequency band signal of the input audio signal to obtain a first full band signal; performing de-emphasis processi... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 15/391,339, filed on Dec. 27, 2016, which is a continuation of International Application No. PCT/CN2015/074704, filed on Mar. 20, 2015. The International Application claims priority to Chinese Patent Applicati... | <SOH> BACKGROUND <EOH>To save channel capacity and storage space, considering that human ears are less sensitive to high frequency information than to low frequency information of an audio signal, the high frequency information is usually cut, resulting in decreased audio quality. Therefore, a bandwidth extension techn... | <SOH> SUMMARY <EOH>Embodiments of the present application provide a coding/decoding method, apparatus, and system, so as to relieve or resolve a prior-art problem that an input audio signal restored by a decoder is apt to have relatively severe signal distortion. According to a first aspect, the present application pro... | G10L1912 | 20170906 | 20171228 | 74048.0 | G10L1912 | 1 | JACKSON, JAKIEDA R | CODING/DECODING METHOD, APPARATUS, AND SYSTEM FOR AUDIO SIGNAL | UNDISCOUNTED | 1 | CONT-ACCEPTED | G10L | 2,017 | |
15,696,662 | ACCEPTED | TOPICAL GEL COMPOSITIONS INCLUDING POLYCAPROLACTONE POLYMER AND METHODS FOR ENHANCING THE TOPICAL APPLICATION OF A BENEFIT AGENT | A composition comprising: a benefit agent; at least one polymer including a polycaprolactone polymer; at least one lower alcohol; and at least one co-solvent; and a method for enhancing topical delivery of a benefit agent is disclosed. | 1-23. (canceled) 24. method for enhancing the topical application of a benefit agent which comprises topically administering to a human or animal a gel composition comprising minoxidil in an amount from about 1% to about 5% by weight of the composition; polycaprolactone diol in an amount from about 1% to about 10% by w... | The present invention relates to compositions and methods for enhancing the topical application of a benefit agent. The compositions may be gels including a benefit agent, at least one polymer including a polycaprolactone polymer, at least one lower alcohol, and at least one co-solvent. The compositions are useful in t... | <SOH> BACKGROUND OF THE INVENTION <EOH>Liquid compositions for delivering benefit agents are well known. Typical formulations include solutions, emulsions, suspensions and gels. The viscosity may vary based on intended area for application, intended use (leave on or rinse off), or consumer preference. Liquids are typic... | <SOH> SUMMARY OF THE INVENTION <EOH>The invention provides a topical composition comprising at least one polycaprolactone polymer, at least one lower alcohol, and at least one co-solvent. The invention also provides a personal care composition comprising the above composition and a method for enhancing the topical appl... | A61K4734 | 20170906 | 20180717 | 20171221 | 58626.0 | A61K4734 | 0 | BARSKY, JARED | TOPICAL GEL COMPOSITIONS INCLUDING POLYCAPROLACTONE POLYMER AND METHODS FOR ENHANCING THE TOPICAL APPLICATION OF A BENEFIT AGENT | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,699,692 | PENDING | COMPOSITIONS AND METHODS FOR TREATING ROSACEA AND ACNE | Provided are compositions and methods for treating rosacea and acne. Specifically, a gel or foam composition having a tetracycline antibiotic and uses thereof for treating rosacea and acne are provided. | 1.-228. (canceled) 229. A method for treating acne vulgaris in a subject in need thereof, comprising administering to the subject a topical composition comprising an effective amount of a tetracycline antibiotic and a hydrophobic vehicle formulated such that the systemic plasma exposure to the tetracycline after repeat... | The present application claims the benefit of priority to U.S. Provisional Patent Application No. 62/385,189 filed Sep. 8, 2016; U.S. Provisional Patent Application No. 62/393,545 filed Sep. 12, 2016; U.S. Provisional Patent Application No. 62/444,960 filed Jan. 11, 2017; and U.S. Provisional Patent Application No. 62/... | <SOH> BACKGROUND <EOH>Rosacea is a chronic acneiform disorder affecting skin and potentially the eye. It is a syndrome of undetermined etiology characterized by both vascular and papulopustular components involving the face and occasionally the neck, scalp, ears and upper trunk. Clinical findings include mid facial ery... | <SOH> SUMMARY <EOH>In one aspect, provided is a method for treating rosacea or acne in a subject in need thereof, the method comprising: administering to said subject a topical composition comprising an effective amount of a tetracycline antibiotic. In another aspect, provided is a hydrophobic gel or foam composition c... | A61K90014 | 20170908 | 20180308 | 91396.0 | A61K900 | 1 | RAMACHANDRAN, UMAMAHESWARI | COMPOSITIONS AND METHODS FOR TREATING ROSACEA AND ACNE | SMALL | 0 | ACCEPTED | A61K | 2,017 | |
15,700,258 | PENDING | LEVOTHYROXINE LIQUID FORMULATIONS | The present invention is directed to a liquid formulation comprising levothyroxine or a pharmaceutically acceptable salt thereof. The formulation of the present invention includes tromethamine, sodium iodide, and water and has a pH of about 9.0 to about 11.5. The liquid formulation according to the invention is stable ... | 1. A liquid formulation comprising levothyroxine or a pharmaceutically acceptable salt thereof; a stabilizing agent; not more than 2% liothyronine (T3); and water; wherein the formulation is stable for at least 12 months at 25±2° C. 2. The formulation of claim 1, wherein levothyroxine or a pharmaceutically acceptable s... | CROSS-REFERENCE TO RELATED APPLICATIONS This patent application is a continuation of co-pending U.S. patent application Ser. No. 15/366,864, filed Dec. 1, 2016, the disclosure of which is incorporated herein by reference in its entirety for all purposes. BACKGROUND OF THE INVENTION Levothyroxine sodium for injection is... | <SOH> BACKGROUND OF THE INVENTION <EOH>Levothyroxine sodium for injection is a sterile lyophilized product for parenteral administration of levothyroxine sodium for thyroid replacement therapy. Levothyroxine sodium for injection is particularly useful when thyroid replacement is needed on an urgent basis, for short ter... | <SOH> BRIEF SUMMARY OF THE INVENTION <EOH>The invention provides a liquid formulation comprising levothyroxine or a pharmaceutically acceptable salt thereof, tromethamine, sodium iodide, and water, wherein the formulation has a pH of about 9.0 to about 11.5. The invention also provides a liquid formulation comprising (... | A61K31198 | 20170911 | 20180607 | 66080.0 | A61K31198 | 6 | HUI, SAN MING R | LEVOTHYROXINE LIQUID FORMULATIONS | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 | |
15,702,435 | PENDING | EZETIMIBE-ASSOCIATED APOA-I MIMETIC PEPTIDES SHOWING ENHANCED SYNERGISM | In various embodiments, ezetimibe-associated apoA-I mimetic peptide are provided that show improved synergistic activity between ezetimibe and the apoA-I peptide in vivo. In certain embodiments the peptide component is a transgenic 6F and the ezetimibe-associated apoA-I mimetic peptide is an Ez-T6F peptide. Methods of ... | 1: A method of preparing an ezetimibe-associated apoA-I mimetic peptide, said method comprising: incubating ezetimibe and said apoAI mimetic peptide in a solution comprising ethyl acetate and acetic acid or in a solution comprising ethyl lactate and lactic acid; and drying said solution to provide a dry ezetimibe-assoc... | CROSS-REFERENCE TO RELATED APPLICATIONS This application claims benefit of and priority to U.S. Ser. No. 62/401,102, filed on Sep. 28, 2016, which is incorporated herein by reference in its entirety for all purposes. STATEMENT OF GOVERNMENTAL SUPPORT This invention was made with Government support under HL030568, award... | <SOH> BACKGROUND <EOH>Mimetics of apolipoprotein A-I (apoA-I) containing only 18 amino acids showed promise in animal models of disease (Getz and Reardon (2011) J Inflamm. Res. 4: 83-92; Navab et al. (2012) Arterioscler. Thromb. Vasc. Biol. 32: 2553-2560), and improved HDL function in humans when given orally at high d... | <SOH> SUMMARY <EOH>In various embodiments, novel ezetimibe-associated apoA-I mimetic peptides are provided as well as uses thereof. It was surprising discovery that an ezetimibe-associated ApoA-I mimetic peptide (Ez-ApoA-I pepide) could be produced by incubating ezeimibe and Tg6F peptide together in a solution comprisi... | A61K3804 | 20170912 | 20180329 | 64641.0 | A61K3804 | 0 | DABKOWSKI, ERINNE R | EZETIMIBE-ASSOCIATED APOA-I MIMETIC PEPTIDES SHOWING ENHANCED SYNERGISM | SMALL | 0 | ACCEPTED | A61K | 2,017 | |
15,702,442 | PENDING | POLYAXIAL BONE SCREW WITH SHANK ARTICULATION PRESSURE INSERT AND METHOD | A polyaxial bone screw assembly includes a threaded shank body having an upper portion, a receiver member or head, a retaining and articulating structure, and a pressure insert disposed between the shank upper portion and a rod. The receiver has a U-shaped cradle defining a channel for receiving a spinal fixation rod a... | 1. A pivotal bone anchor assembly for securing an elongate rod to a bone, the pivotal bone anchor assembly comprising: a receiver having a longitudinal axis, a first pair of opposed upstanding arms extending upwardly from a lower body to define an upwardly open channel configured to receive the elongate rod, and a cavi... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 12/802,668 filed Jun. 11, 2010, which is a continuation of U.S. application Ser. No. 11/140,343 filed May 27, 2005, all of which are incorporated by reference herein. BACKGROUND OF THE INVENTION The present in... | <SOH> BACKGROUND OF THE INVENTION <EOH>The present invention is directed to polyaxial bone screws for use in bone surgery, particularly spinal surgery, and particularly to inserts for such screws. Bone screws are utilized in many types of spinal surgery, such as for osteosynthesis, in order to secure various implants t... | <SOH> SUMMARY OF THE INVENTION <EOH>A polyaxial bone screw assembly according to the invention includes a shank having an upper portion and a body for fixation to a bone; a head or receiver defining an open channel; and at least one compression or pressure insert. The shank is connected to the head or receiver at the u... | A61B177037 | 20170912 | 20180104 | 96981.0 | A61B1770 | 2 | YANG, ANDREW | PIVOTAL BONE ANCHOR ASSEMBLY WITH INTERFERENCE FIT INSERT | SMALL | 1 | CONT-ACCEPTED | A61B | 2,017 | |
15,702,837 | PENDING | MICROCONTROLLER-BASED MULTIFUNCTIONAL ELECTRONIC SWITCH AND LIGHTING APPARATUS HAVING THE SAME | A microcontroller-based multifunctional electronic switch for lighting control uses a detection design to sense and convert external control signals into message carrying sensing signals interpretable to a microcontroller. Based on signal format of message carrying sensing signal received, the microcontroller recognize... | 1. A microcontroller based electronic switch for controlling lighting performance of an LED lamp configured with a plurality of LED lighting loads comprising: a first controllable switching element, electrically connectable between a power source and a first LED lighting load for emitting light with a first color tempe... | CROSS-REFERENCE TO RELATED APPLICATIONS This Application is a continuation application of prior application Ser. No. 15/292,395 filed on Oct. 13, 2016, currently pending. The application Ser. No. 15/292,395 is a continuation application of prior application Ser. No. 15/095,540 filed on Apr. 11, 2016, now U.S. Pat. No. ... | <SOH> BACKGROUND <EOH> | <SOH> SUMMARY <EOH>An exemplary embodiment of the present disclosure provides a microcontroller based electronic switch for detecting an external motion signal. The microcontroller based electronic switch comprises a first controllable switching element, a second controllable switching element, a detection device and a... | H05B370227 | 20170913 | 20180308 | 72646.0 | H05B3702 | 2 | TRAN, THUY V | MICROCONTROLLER-BASED MULTIFUNCTIONAL ELECTRONIC SWITCH AND LIGHTING APPARATUS HAVING THE SAME | SMALL | 1 | CONT-ACCEPTED | H05B | 2,017 | |
15,703,285 | PENDING | MOBILE DISTRIBUTION STATION WITH FAIL-SAFES | A distribution station includes a mobile trailer, a pump on the mobile trailer, a manifold on the mobile trailer and connected with the pump, a plurality of hoses in communication with the manifold, and a plurality of valves on the mobile trailer. Each of the valves is situated between the manifold and a respective dif... | 1. A fuel distribution station comprising: a mobile trailer; a pump on the mobile trailer; a manifold on the mobile trailer and connected with the pump; a plurality of hoses in fluid communication with the manifold; a plurality of valves on the mobile trailer, each of the valves situated between the manifold and a resp... | CROSS-REFERENCE TO RELATED APPLICATION The present disclosure is a continuation of U.S. patent application Ser. No. 15/290,400 filed Oct. 11, 2016. BACKGROUND Hydraulic fracturing (also known as fracking) is a well-stimulation process that utilizes pressurized liquids to fracture rock formations. Pumps and other equipm... | <SOH> BACKGROUND <EOH>Hydraulic fracturing (also known as fracking) is a well-stimulation process that utilizes pressurized liquids to fracture rock formations. Pumps and other equipment used for hydraulic fracturing typically operate at the surface of the well site. The equipment may operate semi-continuously, until r... | <SOH> SUMMARY <EOH>A fuel distribution station according to an example of the present disclosure includes a mobile trailer, a pump on the mobile trailer, a manifold on the mobile trailer connected with the pump, a plurality of hoses in fluid communication with the manifold, and a plurality of valves on the mobile trail... | B67D73218 | 20170913 | 20180412 | 70409.0 | B67D732 | 1 | GRAY, PAUL J | MOBILE DISTRIBUTION STATION WITH FAIL-SAFES | UNDISCOUNTED | 1 | CONT-ACCEPTED | B67D | 2,017 | |
15,703,827 | PENDING | PNEUMATIC TIRE | A tire 2 includes a tie gum 24 between a carcass 12 and each chafer 22. In the tire 2, an inner liner 20 is formed from a thermoplastic elastomer composition including a styrene-isobutylene-styrene block copolymer. The inner liner 20 has a thickness of not greater than 1.5 mm. The tie gum 24 joins the inner liner 20 an... | 1. A pneumatic tire comprising a pair of beads, a carcass, an inner liner, a pair of chafers, and a pair of tie gums, wherein the carcass extends on and between one of the beads and the other of the beads, the inner liner is joined to an inner surface of the carcass, each chafer is turned up around the bead, each tie g... | This application claims priority on Patent Application No. 2016-211160 filed in JAPAN on Oct. 28, 2016. The entire contents of this Japanese Patent Application are hereby incorporated by reference. BACKGROUND OF THE INVENTION Field of the Invention The present invention relates to pneumatic tires. Description of the Re... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>A pneumatic tire according to the present invention includes a pair of beads, a carcass, an inner liner, a pair of chafers, and a pair of tie gums. The carcass extends on and between one of the beads and the other of the beads. The inner liner is joined to an inner surface of the car... | B60C150635 | 20170913 | 20180503 | 60315.0 | B60C1506 | 0 | BRADY, GEORGE WALKER | PNEUMATIC TIRE | UNDISCOUNTED | 0 | PENDING | B60C | 2,017 | |
15,703,964 | ACCEPTED | METHOD AND SYSTEM FOR DATA DEMULTIPLEXING | A method and system for demultiplexing packets of a message is provided. The demultiplexing system receives packets of a message, identifies a sequence of message handlers for processing the message, identifies state information associated with the message for each message handler, and invokes the message handlers pass... | 1-25. (canceled) 26. A method, comprising: receiving, at a computing device having a processing circuit, a packet of a message; determining, by the computing device, a key value for packet, wherein the key value is determined based on one or more headers in the packet; using, by the computing device, the key value to d... | CROSS REFERENCES TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 10/636,314, filed Aug. 6, 2003, titled Method and System for Data Demultiplexing, for all purposes including but not limited to the right of priority and benefit of earlier filing date, and expressly incorpor... | <SOH> BACKGROUND <EOH>Computer systems, which are becoming increasingly pervasive, generate data in a wide variety of formats. The Internet is an example of interconnected computer systems that generate data in many different formats. Indeed, when data is generated on one computer system and is transmitted to another c... | <SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>FIG. 1 is a block diagram illustrating example processing of a message by the conversion system. FIG. 2 is a block diagram illustrating a sequence of edges. FIG. 3 is a block diagram illustrating components of the conversion system in one embodiment. FIG. 4 is a block diagra... | H04L6908 | 20170913 | 20180717 | 20180111 | 70259.0 | H04L2906 | 6 | DUONG, DUC T | METHOD AND SYSTEM FOR DATA DEMULTIPLEXING | UNDISCOUNTED | 1 | CONT-ACCEPTED | H04L | 2,017 |
15,704,274 | PENDING | Crystalline Inhibitor of 4-Hydroxyphenylpyruvate Dioxygenase | The present invention relates to an improved synthesis and crystallization process of the 4-hydroxyphenylpyruvate dioxygenase (HPPD) inhibitor 2-(2-nitro-4-trifluoromethylbenzoyl)-1,3-cyclohexanedione, also known as nitisinone or NTBC. | 1-11. (canceled) 12. A method of inhibiting 4-hydroxyphenylpyruvate dioxygenase enzyme in a patient, the method comprising administering to a patient in need thereof a therapeutically effective amount of crystalline 2-(2-nitro-4-trifluoromethylbenzoyl)-1,3-cyclohexanedione having a X-ray powder diffraction pattern with... | FIELD OF THE INVENTION The present invention relates to an improved synthesis and crystallization process of 4-hydroxyphenylpyruvate dioxygenase (HPPD) inhibitor 2-(2-nitro-4-trifluoromethylbenzoyl)-1,3-cyclohexanedione, also known as nitisinone or NTBC. This new process of synthesis and crystallization gives rise to a... | <SOH> BACKGROUND OF THE INVENTION <EOH>NTBC is a drug marketed by Swedish Orphan Biovitrum International AB under the brand name Orfadin® and it is used to slow the effects of hereditary tyrosinemia type 1 (HT-1) in adult and pediatric patients. It has been approved by FDA and EMA in January 2002 and February 2005 resp... | C07C20546 | 20170914 | 20180531 | 65066.0 | C07C20546 | 1 | KATAKAM, SUDHAKAR | Crystalline Inhibitor of 4-Hydroxyphenylpyruvate Dioxygenase | UNDISCOUNTED | 1 | CONT-ACCEPTED | C07C | 2,017 | ||
15,704,922 | PENDING | Heat Dissipating Structures and Mobility Apparatus for Electronic Headset Frames | A heat sink for electronic devices, such as wearable displays, dissipates heat away from and electrical component, such as a microprocessor. An adjustable support assembly permits adjustment of a visual display relative to a user's field of view. | 1 A wearable display including a headset configured to be worn by a user, a visual display assembly including a support body supported by the headset and a visual display supported by the support body to be positioned forward of a user's eye wearing the headset, an electrical component in communication with the visual ... | CROSS REFERENCE TO RELATED APPLICATION The present application is a continuation of U.S. application Ser. No. 15/479,026, filed Apr. 4, 2017, and claims the benefit of U.S. Provisional Application No. 62/318,141, filed Apr. 4, 2016 and U.S. Provisional Application No. 62/318,554, filed Apr. 5, 2016, the disclosures of ... | <SOH> BACKGROUND OF THE DISCLOSURE <EOH>Electronic headset frames, such as Google® Glass Enterprise Edition visual display, serve as an optical display designed as a pair of glasses to be mounted to the head of a user. These electronic headset frames are capable of not only displaying images, but also recording the vis... | <SOH> BRIEF SUMMARY OF THE DISCLOSURE <EOH>According to one aspect of the present disclosure, a wearable display is provided. The wearable display includes a headset configured to be worn by a user and a visual display assembly including a support body supported by the headset and a visual display supported by the supp... | G06F1163 | 20170914 | 20180104 | 72063.0 | G06F116 | 1 | AUGUSTIN, CHRISTOPHER L | Heat Dissipating Structures and Mobility Apparatus for Electronic Headset Frames | UNDISCOUNTED | 1 | CONT-ACCEPTED | G06F | 2,017 | |
15,705,208 | ACCEPTED | EMULSION FORMULATIONS OF APREPITANT | Disclosed herein are novel pharmaceutical formulations of aprepitant suitable for parenteral administration including intravenous administration. Also included are formulations including both aprepitant and dexamethasone sodium phosphate. The pharmaceutical formulations are stable oil-in-water emulsions for non-oral tr... | 1. A physically stable pharmaceutical composition comprising: 0.4 wt/wt % to 1.0 wt/wt % aprepitant; 13 wt/wt % to 15 wt/wt % egg yolk lecithin; 9 wt/wt % to 10 wt/wt % soybean oil; and a pH modifier, wherein the pH modifier is sodium oleate; wherein the pH of the composition ranges from 7.5 to 9.0, wherein the ratio o... | CROSS-REFERENCE TO RELATED APPLICATIONS This application in a continuation of U.S. application Ser. No. 14/859,013, filed Sep. 18, 2015, which claims the benefit of U.S. Provisional Application No. 62/052,948 filed on Sep. 19, 2014, the disclosures of which are fully incorporated by reference in their entirety. TECHNIC... | <SOH> BACKGROUND <EOH>Aprepitant, having the chemical name 5-[[(2R,3S)-2-[(1R)-1-[3,5-bis(trifluoromethyl)phenyl]ethoxy]-3-(4-fluorophenyl)-4-morpholinyl]methyl]-1,2-dihydro-3H-1,2,4-triazol-3-one, has the structure: Aprepitant is indicated for the prevention of acute and delayed nausea and vomiting associated with ini... | <SOH> BRIEF SUMMARY <EOH>The following aspects and embodiments thereof described and illustrated below are meant to be exemplary and illustrative, not limiting in scope. In one aspect, a pharmaceutical composition suitable for intravenous administration is provided which comprises a stable emulsion comprising an oil ph... | A61K315377 | 20170914 | 20180522 | 20180104 | 58642.0 | A61K315377 | 1 | LEVIN, MIRIAM A | EMULSION FORMULATIONS OF APREPITANT | SMALL | 1 | CONT-ACCEPTED | A61K | 2,017 |
15,705,390 | PENDING | COVERING FOR A MEDICAL SCOPING DEVICE | The present invention relates to a cover having a plurality of moveable, external, angled projecting elements for use with flexible medical scoping devices such as endoscopes or enteroscopes. The invention includes the cover with an over cuff and use of the disposable removable covering in methods of medical scoping pr... | 1. (canceled) 2. A cover for a medical scoping device shaft, the cover comprising an elongate tubular member and being arranged for application over the medical scoping device with the cover extending along at least a part of a length of a distal end of the medical scoping device shaft, the tubular member comprising an... | The present invention relates to a covering or sheath or sleeve or cuff having external projections for use with a medical device and in particular for use with flexible medical scoping devices such as endoscopes or enteroscopes. The invention includes inter alia use of the disposable removable covering in methods of m... | <SOH> BACKGROUND <EOH>In endoscopic examinations/procedures, flexible instruments designed to view the gastro-intestinal tract are inserted along a body cavity to an internal part such as the stomach, duodenum, small intestine or large intestine. The instruments are provided with fibre-optic or charge-couple device (CC... | <SOH> BRIEF SUMMARY OF THE DISCLOSURE <EOH>According to a first aspect of the present invention there is provided a cover for a medical scoping device shaft, the cover comprising an elongate tubular member and being arranged for application over the medical scoping device shaft with the cover extending along at least a... | A61B100135 | 20170915 | 20180111 | 92216.0 | A61B100 | 1 | FAIRCHILD, AARON BENJAMIN | COVERING FOR A MEDICAL SCOPING DEVICE | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61B | 2,017 | |
15,705,703 | PENDING | EMBEDDING DIGITAL CONTENT WITHIN A DIGITAL PHOTOGRAPH DURING CAPTURE OF THE DIGITAL PHOTOGRAPH | A wireless communication device comprises position determining system, a digital imaging system and a photograph customization system coupled to the position locating system and the digital imaging system. The position determining system is configured to provide information indicating a current position of the wireless... | 1. (canceled) 2. (canceled) 3. (canceled) 4. (canceled) 5. (canceled) 6. (canceled) 7. (canceled) 8. (canceled) 9. (canceled) 10. (canceled) 11. (canceled) 12. (canceled) 13. (canceled) 14. (canceled) 15. (canceled) 16. (canceled) 17. A computer-implemented method performed by a wireless communication device, comprisin... | CROSS REFERENCE TO RELATED APPLICATIONS This continuation patent application claims priority from co-pending United States Non-provisional Patent Application having Ser. No. 14/251,707, filed 14, Apr. 2014, entitled “Embedding digital content within a digital photograph during capture of the digital photograph”, which ... | <SOH> BACKGROUND <EOH>Digital photography, like traditional film photography, is widely used for memorializing events and moments. With the advent of social media and wireless communication, it has become common place for people to use digital photographs as an integral part of their social networking endeavors such as... | <SOH> SUMMARY OF THE DISCLOSURE <EOH>Embodiments of the present invention are directed to a system-implemented solution (e.g., an internal process of a digital imaging device) for enabling personalization (e.g., via contextualization and/or customization) to be performed in combination with taking a photograph with a d... | G06T10021 | 20170915 | 20180308 | 83039.0 | G06T100 | 2 | YANG, WEI WEN | EMBEDDING DIGITAL CONTENT WITHIN A DIGITAL PHOTOGRAPH DURING CAPTURE OF THE DIGITAL PHOTOGRAPH | MICRO | 1 | CONT-ACCEPTED | G06T | 2,017 | |
15,706,139 | PENDING | Accessory Cart | In the specification and drawings an accessory cart is described and shown with a base, a housing element that is connected to the base and extends upward from the base, and a platform, which is connected to the housing element with the height of the platform being automatically adjustable. | 1. An accessory cart, comprising: a base; an adjustable housing element connected to the base, the housing element extending upward from the base; a work platform connected to the housing element, the cart further comprising an input device, the input device configured to receive a user identifier, the user identifier ... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. application Ser. No. 14/714,994, filed on May 18, 2015, which application was a continuation of U.S. application Ser. No. 13/763,395, filed on Feb. 8, 2013, which claims the benefit of U.S. Provisional Application No. 61/596,635, filed F... | <SOH> BACKGROUND OF THE INVENTION <EOH>Mobile accessory carts that carry computers are commonly used in healthcare and other industries to provide portable workstations. Similar to a computer workstation in an ordinary office setting, ergonomic features are important for mobile accessory carts as well. For example, the... | <SOH> SUMMARY OF THE INVENTION <EOH>An embodiment of the present invention is directed to an accessory cart that comprises a base, a housing element, which is connected to the base, extending upward from the base and a work platform that is connected to the housing element with the height of the work platform being aut... | A47B2104 | 20170915 | 20180125 | 96764.0 | A47B2104 | 1 | TO, TOAN C | Accessory Cart | UNDISCOUNTED | 1 | CONT-ACCEPTED | A47B | 2,017 | |
15,707,891 | PENDING | BONE PLATE WITH A TRANSFIXATION SCREW HOLE | A system for securing bones together across a joint includes a transfixation screw and a plate. The plate includes an elongate spine having a transfixation screw hole disposed along the spine. The transfixation screw hole includes an inner surface configured to direct the transfixation screw through the transfixation s... | 1. A system for securing bones together across a joint, comprising a transfixation screw and a plate wherein: the plate comprises: an elongate spine having a first end comprising at least one attachment point for attaching the first end to a first bone on a first side of a joint, a second end comprising at least one at... | CROSS-REFERENCE TO RELATED APPLICATIONS The present application is a continuation of co-pending, commonly assigned, patent application Ser. No. 15/147,828 entitled “BONE PLATE WITH A TRANSFIXATION SCREW HOLE,” filed May 5, 2016, which is a continuation of patent application Ser. No. 14/015,900 entitled “BONE PLATE WITH... | <SOH> BACKGROUND OF THE INVENTION <EOH>When performing certain medical procedures, such as reconstructing a joint that has been damaged due to bone or soft tissue trauma, a surgeon may need to fuse the bones of the joint together in a configuration that approximates the natural geometry of the joint. One way to achieve... | <SOH> BRIEF SUMMARY OF THE INVENTION <EOH>The present disclosure relates generally to orthopedic devices. More specifically, the present disclosure relates to a bone plate with a transfixation screw hole for securing the bones of a joint together and a method for using the same. In particular embodiments, a system for ... | A61B178057 | 20170918 | 20180104 | 58291.0 | A61B1780 | 2 | WOODALL, NICHOLAS W | BONE PLATE WITH A TRANSFIXATION SCREW HOLE | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61B | 2,017 | |
15,710,604 | PENDING | COMBINED ORTHODONTIC MOVEMENT OF TEETH WITH AIRWAY DEVELOPMENT THERAPY | Systems, devices and methods are disclosed for reshaping airways concurrently with dental and/or orthodontic treatment. The systems can have a series of two or more oral appliances configured to progressively reposition the maxillary and mandibular teeth in two or more successive steps. Each oral appliance in the serie... | 1. An oral appliance for the treatment of sleep breathing disorders, comprising: one or more maxillary blocks; one or more mandibular blocks; a maxillary oral tray, wherein the one or more maxillary blocks are attached to or integrated with the maxillary oral tray; and a mandibular oral tray, wherein the one or more ma... | CROSS-REFERENCE TO RELATED APPLICATION This application claims priority to U.S. Provisional Application No. 62/397,749 filed Sep. 21, 2016, which is herein incorporated by reference in its entirety for all purposes. BACKGROUND 1. Technical Field Systems, devices and methods for reshaping airways are disclosed. More spe... | <SOH> BACKGROUND <EOH> | <SOH> BRIEF SUMMARY OF THE INVENTION <EOH>This disclosure relates generally to the combined orthodontic movement and/or dental treatment of teeth, airway development and treatment of sleep breathing disorders. More specifically, orthodontic and/or dental airway development systems, apparatuses and methods of using the ... | A61C736 | 20170920 | 20180322 | 67703.0 | A61C736 | 0 | CARREIRO, CAITLIN ANN | COMBINED ORTHODONTIC MOVEMENT OF TEETH WITH AIRWAY DEVELOPMENT THERAPY | SMALL | 0 | PENDING | A61C | 2,017 | |
15,710,711 | PENDING | INFORMATION APPARATUS AND SOFTWARE APPLICATIONS SUPPORTING PRINTING OF DIGITAL CONTENT OVER A NETWORK TO A REGISTERED PRINTER | Software applications and information apparatus supporting output of digital content over a network (e.g., Internet) to an output device (e.g., printer) are herein disclosed and enabled. To output digital content, an application for accessing a service provided over the network is installed, the information apparatus i... | 1. A method for outputting digital content from an information apparatus to an output device by using one or more application software executable at the information apparatus, the information apparatus includes: one or more processors; a user interface for interacting with a user; wireless communication circuitry for w... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 10/053,765 filed Jan. 18, 2002, which claims priority to U.S. Provisional Patent Application Ser. No. 60/262,764, filed Jan. 19, 2001. Additionally, this application is a continuation-in-part of U.S. patent ap... | <SOH> BACKGROUND OF THE DISCLOSURE <EOH>The present invention relates to universal data output and, in particular, to providing a new data output method and a new raster image process for information apparatuses and output devices. As described herein, information apparatuses refer generally to computing devices, which... | <SOH> SUMMARY OF THE INVENTION <EOH>Accordingly, this invention provides a convenient universal data output method in which an information apparatus and an output device or system share the raster image processing operations. Moreover, the new data output method eliminates the need to install a plurality of device-depe... | G06F31236 | 20170920 | 20180125 | 66411.0 | G06F312 | 1 | RILEY, MARCUS T | INFORMATION APPARATUS AND SOFTWARE APPLICATIONS SUPPORTING OUTPUT OF DIGITAL CONTENT OVER A NETWORK TO A REGISTERED OUTPUT DEVICE | UNDISCOUNTED | 1 | CONT-ACCEPTED | G06F | 2,017 | |
15,710,804 | ACCEPTED | SYSTEM AND METHOD FOR VOICE CONTROL OF MEASUREMENT APPARATUS | Measurement apparatus includes sensors configured to generate signals associated with physiological parameters and adapted to be coupled to tissue comprising blood and to communicate signals associated with the parameters to feedback control circuitry capable of generating physiological information from the signals. A ... | 1. A measurement apparatus comprising: one or more sensors configured to generate signals associated with one or more physiological parameters, wherein at least one of the one or more sensors is adapted to be coupled to tissue comprising blood and to communicate to feedback control circuitry at least a portion of the s... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 15/258,133 filed Sep. 7, 2016, which is a continuation of U.S. patent application Ser. No. 14/734,069 filed Jun. 9, 2015, now U.S. Pat. No. 9,456,751, issued Oct. 4, 2016, which is a continuation of U.S. paten... | <SOH> TECHNICAL FIELD <EOH>This disclosure relates generally to medical diagnostic systems. | <SOH> SUMMARY OF EXAMPLE EMBODIMENTS <EOH>In one embodiment, a measurement apparatus comprises one or more sensors configured to generate signals associated with one or more physiological parameters, wherein at least one of the one or more sensors is adapted to be coupled to tissue comprising blood and to communicate t... | A61B50075 | 20170920 | 20180626 | 20180201 | 61148.0 | A61B500 | 1 | HELLNER, MARK | MEASUREMENT APPARATUS FOR PHYSIOLOGICAL PARAMETERS | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61B | 2,017 |
15,712,074 | ACCEPTED | Biosynthesis Of Human Milk Oligosaccharides In Engineered Bacteria | The invention provides compositions and methods for engineering bacteria to produce fucosylated oligosaccharides, and the use thereof in the prevention or treatment of infection. | 1. A method for producing a fucosylated oligosaccharide in a bacterium, comprising providing a bacterium, said bacterium comprising a functional β-galactosidase gene, an exogenous fucosyltransferase gene, a GDP-fucose synthesis pathway, a functional lactose permease gene; culturing said bacterium in the presence of lac... | RELATED APPLICATIONS This application is a continuation of U.S. Ser. No. 15/442,131, filed Feb. 24, 2017, which is a continuation of U.S. Ser. No. 14/033,664 filed Sep. 23, 2013, now U.S. Pat. No. 9,587,241 issued Feb. 15, 2017, which is a divisional of U.S. Ser. No. 13/398,526 filed Feb. 16, 2012, now U.S. Pat. No. 9,... | <SOH> BACKGROUND OF THE INVENTION <EOH>Human milk contains a diverse and abundant set of neutral and acidic oligosaccharides (human milk oligosaccharides, HMOS). Many of these molecules are not utilized directly by infants for nutrition, but they nevertheless serve critical roles in the establishment of a healthy gut m... | <SOH> SUMMARY OF THE INVENTION <EOH>The invention described herein features efficient and economical methods for producing fucosylated and sialylated oligosaccharides. The method for producing a fucosylated oligosaccharide in a bacterium comprises the following steps: providing a bacterium that comprises a functional β... | C12N1570 | 20170921 | 20180515 | 20180322 | 69611.0 | C12N1570 | 2 | PROUTY, REBECCA E | Biosynthesis Of Human Milk Oligosaccharides In Engineered Bacteria | UNDISCOUNTED | 1 | CONT-ACCEPTED | C12N | 2,017 |
15,712,780 | PENDING | APPARATUS, METHOD AND SYSTEM FOR A TUNNELING CLIENT ACCESS POINT | The disclosure details the implementation of an apparatus, method, and system comprising a portable device configured to communicate with a terminal and a network server, and execute stored program code in response to user interaction with an interactive user interface. The portable device contains stored program code ... | 1. A portable device configured to communicate with a communications network, the communication network comprising (i) a communications network node, and (ii) a terminal, the terminal comprising a processor, an output component, and a memory configured to store executable program code, including first program code whic... | This application is a continuation of U.S. application Ser. No. 14/721,540, filed May 26, 2015, which is a continuation of U.S. application Ser. No. 13/960,514, filed Aug. 6, 2013, now U.S. Pat. No. 9,059,969, which is a continuation of U.S. application Ser. No. 12/950,321, filed Nov. 19, 2010, now U.S. Pat. No. 8,539,... | <SOH> BACKGROUND <EOH> | <SOH> SUMMARY <EOH>Although all of the aforementioned portable computing systems exist, no effective solution to securely access, execute, and process data is available in an extremely compact form. Currently, PDAs, which are considered among the smallest portable computing solution, are bulky, provide uncomfortably sm... | H04L6742 | 20170922 | 20180111 | 57313.0 | H04L2906 | 1 | BOUTAH, ALINA A | APPARATUS, METHOD AND SYSTEM FOR A TUNNELING CLIENT ACCESS POINT | SMALL | 1 | CONT-ACCEPTED | H04L | 2,017 | |
15,713,324 | PENDING | FLUORESCENT COMPOUND COMPRISING A FLUOROPHORE CONJUGATED TO A pH-TRIGGERED POLYPEPTIDE | The present subject matter provides compounds, compositions, and methods for identifying, monitoring, treating, and removing diseased tissue. Compounds, compositions, and methods for identifying, monitoring, and detecting circulating fluids such as blood are also provided. | 1. A pHLIP-fluorophore compound comprising (a) a pH-triggered polypeptide (pHLIP peptide); and (b) a fluorophore, wherein the fluorophore is a near-infrared (NIR) fluorophore, a cyanine fluorophore, or an optoacoustic contrast imaging agent. 2. The compound of claim 1, having the structure: 3. The compound of claim 1, ... | RELATED APPLICATION This application claims the benefit of priority under 35 U.S.C. § 119(e) to U.S. Provisional Application No. 62/398,448, filed Sep. 22, 2016, the entire content of which is incorporated herein by reference. STATEMENT AS TO FEDERALLY SPONSORED RESEARCH This invention was made with government support ... | <SOH> BACKGROUND <EOH>Bladder cancer is the fifth most common cancer, constituting 4.5% of all new cancer cases in the United States. 76,960 new cases were estimated in 2016 and the death rate currently expected from bladder cancer is 21% (16,390). Approximately 2.4 percent of men and women will be diagnosed with bladd... | <SOH> SUMMARY OF THE INVENTION <EOH>The present subject matter provides, inter alia, fluorescent compounds comprising, consisting essentially of, or consisting of a pH-triggered polypeptide (a “pHLIP peptide”) and a fluorophore. Such compounds may be referred to herein as “pHLIP-fluorophore compounds.” Methods and comp... | A61K490056 | 20170922 | 20180503 | 63697.0 | A61K4900 | 0 | NIEBAUER, RONALD T | FLUORESCENT COMPOUND COMPRISING A FLUOROPHORE CONJUGATED TO A pH-TRIGGERED POLYPEPTIDE | SMALL | 0 | PENDING | A61K | 2,017 | |
15,713,546 | PENDING | PRINTING DEVICES SUPPORTING PRINTING OVER AIR OR PRINTING OVER A WIRELESS NETWORK | Printing devices (including controllers) supporting printing in a wireless local area network, printing over air, or network printing by registering the printing device with a service over a network are herein disclosed and enabled. The printing device may include wireless communication circuitry that supports part of ... | 1. A method for a printing device to wirelessly provide printing services, the printing device includes wireless communication circuitry for establishing a wireless local area network connection to a wireless local area network, the method comprises: (1) wirelessly connecting, using the wireless communication circuitry... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 10/053,765 filed Jan. 18, 2002, which claims priority to U.S. Provisional Patent Application Ser. No. 60/262,764, filed Jan. 19, 2001. Additionally, this application is a continuation-in-part of U.S. patent ap... | <SOH> BACKGROUND OF THE DISCLOSURE <EOH>The present invention relates to universal data output and, in particular, to providing a new data output method and a new raster image process for information apparatuses and output devices. As described herein, information apparatuses refer generally to computing devices, which... | <SOH> SUMMARY OF THE INVENTION <EOH>Accordingly, this invention provides a convenient universal data output method in which an information apparatus and an output device or system share the raster image processing operations. Moreover, the new data output method eliminates the need to install a plurality of device-depe... | G06F31236 | 20170922 | 20180125 | 66411.0 | G06F312 | 3 | RILEY, MARCUS T | PRINTING DEVICES SUPPORTING PRINTING OVER AIR OR PRINTING OVER A WIRELESS NETWORK | UNDISCOUNTED | 1 | CONT-ACCEPTED | G06F | 2,017 | |
15,713,743 | PENDING | ELECTRONIC CIGARETTE | An electronic cigarette includes a housing, a sleeve, an atomizer, a latch assembly and a control assembly. The sleeve includes a first limiting position and a second limiting position. The atomizer includes a mouthpiece. The atomizer is capable of being inserted into the sleeve and telescoping relative to the sleeve a... | 1. An electronic cigarette, comprising: a housing; a sleeve received in the housing, the sleeve comprising a first limiting position and a second limiting position; an atomizer comprising a mouthpiece, the atomizer capable of being inserted into the sleeve and telescoping relative to the sleeve along an axial direction... | CROSS-REFERENCE TO RELATED APPLICATIONS The present disclosure claims priority to Chinese Patent Application No. 201621082925.6, filed with the Chinese Patent Office on Sep. 26, 2016, titled “ELECTRONIC CIGARETTE,” the entire contents of which are incorporated herein by reference. TECHNICAL FIELD The present disclosure... | <SOH> BACKGROUND <EOH>In current market, suction nozzles of atomizers of electronic cigarettes are fixed. The suction nozzles of the atomizers are always exposed outside, which is unsanitary in use. Protection for the suction nozzles of the atomizers depends on package boxes, and thus the atomizers are inconvenient to ... | <SOH> SUMMARY <EOH>An embodiment of the present disclosure provides an electronic cigarette. The electronic cigarette includes: a housing; a sleeve received in the housing, the sleeve including a first limiting position and a second limiting position; an atomizer including a mouthpiece, the atomizer capable of being in... | A24F47008 | 20170925 | 20180329 | 97260.0 | A24F4700 | 0 | HYEON, HAE M | ELECTRONIC CIGARETTE HAVING PROTECTION FOR A SUCTION NOZZLE | SMALL | 0 | ACCEPTED | A24F | 2,017 | |
15,714,103 | PENDING | PROGRAM, CONTROL METHOD, AND INFORMATION PROCESSING APPARATUS | Provided are a program, a control method, and an information processing apparatus which may provide an improved user interface on which a user may easily and efficiently execute various processes on a game content. The information processing apparatus may be caused to execute a game content specifying step of specifyin... | 1. A non-transitory computer-readable storage medium comprising program code that, when executed, causes an information processing apparatus including: a display unit configured to display a game content; an operation unit configured to receive a first input operation of a user, the first input operation of the user co... | BACKGROUND OF THE INVENTION Field of the Invention The present invention relates to a program, a control method, and an information processing apparatus. Description of the Related Art A user playing a role-playing game or the like may acquire a game content such as a card, an item, equipment, a character, or the like ... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>The invention is to provide a program, a control method, and an information processing apparatus that realize a user interface capable of easily and efficiently executing various processes on a game content. According to an exemplary embodiment, there may be provided a program causin... | A63F1340 | 20170925 | 20180405 | 65883.0 | A63F1340 | 0 | ROWLAND, STEVE | PROGRAM, CONTROL METHOD, AND INFORMATION PROCESSING APPARATUS | UNDISCOUNTED | 0 | ACCEPTED | A63F | 2,017 | |
15,714,558 | PENDING | METHOD AND APPARATUS TO CORRECT BLUR IN ALL OR PART OF A DIGITAL IMAGE BY COMBINING PLURALITY OF IMAGES | A method and apparatus for use in a digital imaging device for correcting image blur in digital images by combining plurality of images. The plurality of images that are combined include a main subject that can be selected by user input or automatically by the digital imaging device. Blur correction can be performed to... | 1. A method for use in an imaging device, the method comprising: displaying an image in a user interface of the device; receiving a user input in the user interface, wherein the user input designates a first subject in the image; capturing a plurality of images using an image sensor of the device, wherein the plurality... | CROSS REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 14/875,204, filed Oct. 5, 2015, which is a continuation of U.S. patent application Ser. No. 14/586,297, filed on Dec. 30, 2014, which issued as U.S. Pat. No. 9,154,699 on Oct. 6, 2015, which is a continuation ... | <SOH> BACKGROUND <EOH>When capturing images, as with a camera, it is desirable to capture images without unwanted distortion. In general, sources of unwanted distortion can be characterized as equipment errors and user errors. Examples of common equipment errors include inadequate or flawed optical equipment, and undes... | <SOH> SUMMARY <EOH>The present invention processes image data in order to correct an image for distortion caused by imager movement or by movement of the subject being imaged. In another embodiment, the present invention can prevent image distortion due to motion of the imaging device or subject at relatively slow shut... | H04N523287 | 20170925 | 20180125 | 70224.0 | H04N5232 | 1 | MONK, MARK T | METHOD AND APPARATUS TO CORRECT BLUR IN ALL OR PART OF A DIGITAL IMAGE BY COMBINING PLURALITY OF IMAGES | SMALL | 1 | CONT-ACCEPTED | H04N | 2,017 | |
15,715,065 | PENDING | ELECTRONIC PERCUSSION INSTRUMENT AND METHOD FOR CONTROLLING SOUND GENERATION | An electronic percussion instrument to control generated sound in accordance with operation to the striking surface includes: a first sensor configured to detect a slapping operation on the striking surface; a second sensor configured to detect a contact operation to the striking surface; and a processor configured to ... | 1. An electronic percussion instrument having a surface, comprising: a first sensor configured to detect a striking operation on the surface; a second sensor configured to detect a contact operation to the surface; and a processor configured to control sound generated in response to detection of a striking operation by... | BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to electronic percussion instruments, such as an electronic cajon. 2. Description of the Related Art Conventionally known percussion instruments include an acoustic percussion instrument not having a function of amplifying the sound ele... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF THE INVENTION <EOH>One aspect of the present invention relates to an electronic percussion instrument having a surface. The electronic percussion instrument includes: a first sensor configured to detect a striking operation on the surface; a second sensor configured to detect a contact operation to the... | G10H322 | 20170925 | 20180329 | 84267.0 | G10H322 | 0 | DONELS, JEFFREY | ELECTRONIC PERCUSSION INSTRUMENT AND METHOD FOR CONTROLLING SOUND GENERATION | UNDISCOUNTED | 0 | ACCEPTED | G10H | 2,017 | |
15,715,351 | PENDING | 6-Alkynyl-pyridine Derivatives | 6-Alkynyl-pyridine of general formula (I) their use as SMAC mimetics, pharmaceutical compositions containing them, and their use as a medicaments for the treatment and/or prevention of diseases characterized by excessive or abnormal cell proliferation and associated conditions such as cancer. An exemplary compound is | 1. A compound of formula I wherein R1 is selected from the group consisting of hydrogen, —C1-3alkyl and halogen; R2 is selected from the group consisting of hydrogen, —C1-3alkyl and halogen; R3 is selected from the group consisting of phenyl or a 9- to 14-membered heteroaryl wherein each of these groups is optionally s... | This invention relates to compounds of the general formula (I) wherein the groups R1 to R4 have the meanings given in the claims and in the specification. The compounds of the invention are suitable for the treatment of diseases characterized by excessive or abnormal cell proliferation, pharmaceutical preparations cont... | <SOH> BACKGROUND OF THE INVENTION <EOH>Apoptosis, a form of programmed cell death, typically occurs in the normal development and maintenance of healthy tissues in multicellular organisms. It is a complex process, which results in the removal of damaged, diseased or developmentally redundant cells, without signs of inf... | A61K314709 | 20170926 | 20180118 | 59270.0 | A61K314709 | 0 | NORTHINGTON DAVI, ZINNA | 6-Alkynyl-pyridine Derivatives | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 | ||
15,716,675 | PENDING | FUEL MANAGEMENT SYSTEM FOR VARIABLE ETHANOL OCTANE ENHANCEMENT OF GASOLINE ENGINES | Fuel management system for efficient operation of a spark ignition gasoline engine. Injectors inject an anti-knock agent such as ethanol directly into a cylinder of the engine. A fuel management microprocessor system controls injection of the anti-knock agent so as to control knock and minimize that amount of the anti-... | 1. A fuel management system for a spark ignition engine that has a first fueling system that uses direct injection and also has a second fueling system that uses port fuel injection; and where the fueling is such that there is a first torque range where both the first and second fueling system are used throughout the r... | This application is a continuation of U.S. patent application Ser. No. 15/463,425 filed on Mar. 20, 2017, which is a continuation of U.S. patent application Ser. No. 14/982,086 filed on Dec. 29, 2015, which is a continuation of U.S. patent application Ser. No. 14/478,069 filed on Sep. 5, 2014, which is a continuation o... | <SOH> BACKGROUND <EOH>This invention relates to spark ignition gasoline engines utilizing an antiknock agent which is a liquid fuel with a higher octane number than gasoline such as ethanol to improve engine efficiency. It is known that the efficiency of spark ignition (SI) gasoline engines can be increased by high com... | <SOH> SUMMARY <EOH>In one aspect, the invention is a fuel management system for efficient operation of a spark ignition gasoline engine including a source of an antiknock agent such as ethanol. An injector directly injects the ethanol into a cylinder of the engine and a fuel management system controls injection of the ... | F02D410025 | 20170927 | 20180118 | 63491.0 | F02D4100 | 1 | HUYNH, HAI H | FUEL MANAGEMENT SYSTEM FOR VARIABLE ETHANOL OCTANE ENHANCEMENT OF GASOLINE ENGINES | UNDISCOUNTED | 1 | CONT-ACCEPTED | F02D | 2,017 | |
15,716,838 | PENDING | STEROID COMPOUND FOR USE IN THE TREATMENT OF HEPATIC ENCEPHALOPATHY | The present invention provides the steroidal compound 3α-ethynyl-3β-hydroxyandrostan-17-one oxime, or a pharmaceutically acceptable salt thereof, for use in treatment of hepatic encephalopathy. | 1. A method of treating hepatic encephalopathy, comprising administering a pharmaceutically effective amount of 3α-ethynyl-3β-hydroxyandrostan-17-one oxime or a pharmaceutically acceptable salt thereof, to a patient in need thereof, wherein said hepatic encephalopathy is selected from the group consisting of minimal he... | RELATED APPLICATIONS This application is a continuation of U.S. Ser. No. 15/352,035, filed Nov. 15, 2016, which is a continuation of U.S. application Ser. No. 15/114,972, filed on Jul. 28, 2016. U.S. application Ser. No. 15/114,972 is the 35 U.S.C. §371 national stage filing of International Application No. PCT/GB2015/... | <SOH> BACKGROUND OF THE INVENTION <EOH>Hepatic encephalopathy (HE) is a serious neuropsychiatric and neurocognitive complication in acute and chronic liver disease. HE is a significant and increasing health care problem due to the large and increasing prevalence of chronic liver disease. HE is characterized by impairme... | <SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>FIG. 1 shows that 3α-ethynyl-3β-hydroxyandrostan-17-one oxime does not affect blood ammonia levels. Values are the mean±SEM of 12 rats per group, values significantly different from controls are indicated by asterisks; ***, p<0.001. CV=control rats treated with vehicle; HAV=... | A61K31568 | 20170927 | 20180118 | 96712.0 | A61K31568 | 0 | BERRY, LAYLA D | STEROID COMPOUND FOR USE IN THE TREATMENT OF HEPATIC ENCEPHALOPATHY | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 | |
15,716,893 | PENDING | METASTATIC CANCER DECOY TRAP | A method of treating or preventing cancer metastasis in a subject is described. The method includes implanting a decoy trap within the subject, the decoy trap comprising an implantable trap device including a metastatic cancer attractant. Methods of diagnosing cancer metastasis in a subject using the decoy traps are al... | 1. A method of treating or preventing cancer metastasis in a subject, comprising implanting a decoy trap within the subject, the decoy trap comprising an implantable trap device including a metastatic cancer attractant. 2. The method of claim 1, wherein the cancer metastasis is bone metastasis, and the metastatic cance... | This application is a continuation-in-part of U.S. patent application Ser. No. 15/327,332, filed on Jan. 18, 2017, which was a national stage application claiming the benefit of International Patent Application No. PCT/US2015/041061, filed on Jul. 20, 2015, which claimed the benefit of the benefit of U.S. Provisional A... | <SOH> BACKGROUND <EOH>Mesenchymal Stem Cells (MSC) have long been described as cellular progenitors of mesenchymal lineages including bone, cartilage, fat, muscle and other connective tissues. In addition, a secretory capacity has been identified with both immunomodulatory and trophic activities, exerted at sites of in... | <SOH> SUMMARY <EOH>With the notion of BM-MSC as pericytes, the inventors propose taking advantage of the physical interaction of invading cancer cells and resident BM-MSC occurring at the abluminal space of BM sinusoids as a determinant step in the initiation and fate of skeletal metastasis. The inventors have shown th... | A61K3544 | 20170927 | 20180222 | 67892.0 | A61K3544 | 0 | SGAGIAS, MAGDALENE K | METASTATIC CANCER DECOY TRAP | SMALL | 1 | CONT-REJECTED | A61K | 2,017 | |
15,717,056 | ACCEPTED | Elastomeric Coating Composition | An elastomeric coating composition to enhance or alter the aesthetic appearance of an automobile. The coating composition can be applied by spraying onto either a vehicle paint job or clear coat and is semi-permanent upon drying. The coating composition can be manually removed from the vehicle by peeling without damagi... | 1. A coating composition, comprising: a composite film comprising: a polymer; a tackifier; a hydrocarbon resin; a solvent; and a UV stabilizer; and at least one pigment additive. 2. The coating composition according to claim 1, wherein the hydrocarbon resin has a softening point of at least 140 degrees Celsius. 3. The ... | CROSS REFERENCE TO RELATED APPLICATIONS This application is a continuation of application No. 15/056,052 filed on Feb. 29, 2016 entitled “Elastomeric Coating Composition and Method of Applying Same” which claims priority to Provisional Application No. 62/126,587 filed on Feb. 28, 2015 and entitled “Elastomeric Coating ... | <SOH> BACKGROUND OF THE INVENTION <EOH>This invention relates to an elastomeric coating specifically engineered to enhance or alter the aesthetic appearance of an automobile. In traditional settings, automobile paint shops change the color and finish of trucks, cars, and other vehicles by applying permanent paint to th... | <SOH> SUMMARY OF THE INVENTION <EOH>A coating composition for vehicles, comprises a polymer, a tackifier, a hydrocarbon resin; and a solvent. In another embodiment, the coating composition includes a styrene/ethylene/butylene/styrene liner triblock copolymer in an amount by weight of 6.51 percent; a hydrocarbon resin i... | C09D520 | 20170927 | 20180306 | 20180118 | 75225.0 | C09D520 | 2 | HARLAN, ROBERT D | Elastomeric Coating Composition | SMALL | 1 | CONT-ACCEPTED | C09D | 2,017 |
15,717,138 | ACCEPTED | INTERNET QUERIED DIRECTIONAL NAVIGATION SYSTEM WITH MOBILE AND FIXED ORIGINATING LOCATION DETERMINATION | A mobile wireless network and a method of operation provide directional assistance in response to an Internet query. The directional assistance is provided from a location of the querying device to a destination that may be selectively prompted based on whether the destination is a nearby business, a type of business, ... | 1. A method of providing navigation assistance to a user of a communications device, the method comprising: receiving, by a directional assistance service, an Internet query initiated at the communications device and directed via the Internet to initiate a request for navigational assistance to a destination; responsiv... | The present Application is a Continuation of U.S. patent application Ser. No. 15/468,265 filed on Mar. 24, 2017 and published as U.S. Patent Publication No. 20170195847 on Jul. 6, 2017, which is a Continuation of U.S. patent application Ser. No. 15/297,222, filed on Oct. 19, 2016, and issued as U.S. Pat. No. 9,642,024 ... | <SOH> BACKGROUND OF THE INVENTION <EOH>Wireless networks 100 are becoming increasingly important worldwide. Wireless networks 100 are rapidly replacing conventional wire-based telecommunications systems in many applications. Cellular radio telephone networks (“CRT”), and specialized mobile radio and mobile data radio n... | <SOH> Summary of Factors Affecting Rf Propagation <EOH>The physical radio propagation channel perturbs signal strength, causing rate changes, phase delay, low signal to noise ratios (e.g., ell for the analog case, or E b /no, RF energy per bit, over average noise density ratio for the digital case) and doppler-shift. S... | H04W4023 | 20170927 | 20180313 | 20180208 | 67921.0 | H04W402 | 5 | PATEL, AJIT | INTERNET QUERIED DIRECTIONAL NAVIGATION SYSTEM WITH MOBILE AND FIXED ORIGINATING LOCATION DETERMINATION | UNDISCOUNTED | 1 | CONT-ACCEPTED | H04W | 2,017 |
15,717,359 | ACCEPTED | PROTOCOL FOR LIGHTING CONTROL VIA A WIRELESS NETWORK | A monitor lighting control device receives a state change event message that includes a payload specifying: (i) a state change event of an occupancy, audio, or daylight sensor, or a switch to turn lighting on/off, dim up/down, set scene or the like; (ii) an identifier of a member lighting control device that detected t... | 1. A lighting control system comprising: a lighting control group, including a group monitor, a member lighting control device, and a luminaire; wherein the group monitor comprises: a wireless radio communication interface system configured for wireless communication over a wireless lighting control network communicati... | CROSS-REFERENCE TO RELATED APPLICATION This application is a continuation of U.S. patent application Ser. No. 15/214,962, filed on Jul. 20, 2016, the entire disclosure of which is incorporated herein by reference. BACKGROUND Traditional luminaires can be turned ON and OFF, and in some cases may be dimmed, usually in re... | <SOH> BACKGROUND <EOH>Traditional luminaires can be turned ON and OFF, and in some cases may be dimmed, usually in response to user activation of a relatively simple input device. Often traditional luminaires are controlled individually or as relatively small groups at separate locations. More sophisticated lighting co... | <SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>The drawing figures depict one or more implementations in accord with the present teachings, by way of example only, not by way of limitation. In the figures, like reference numerals refer to the same or similar elements. FIG. 1A is a high-level functional block diagram of a... | H05B370272 | 20170927 | 20180626 | 20180201 | 57220.0 | H05B3702 | 0 | LE, TUNG X | PROTOCOL FOR LIGHTING CONTROL VIA A WIRELESS NETWORK | UNDISCOUNTED | 1 | CONT-ACCEPTED | H05B | 2,017 |
15,717,502 | PENDING | Novel Reagents for Directed Biomarker Signal Amplification | Described herein are methods, compositions and articles of manufacture involving neutral conjugated polymers including methods for synthesis of neutral conjugated water-soluble polymers with linkers along the polymer main chain structure and terminal end capping units. Such polymers may serve in the fabrication of nove... | 1-40. (canceled) 41. A water soluble conjugated polymer having the structure of the formula: wherein: Ar is an aryl or heteroaryl unit substituted with a non-ionic side group capable of imparting solubility in water; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distributed along ... | CROSS-REFERENCE This application is a continuation of application Ser. No. 15/239,713, filed Aug. 17, 2016; which application is a continuation of application Ser. No. 14/821,386, filed Aug. 7, 2015 and issued as U.S. Pat. No. 9,547,008; which application is a continuation of application Ser. No. 14/018,985, filed Sep.... | <SOH> BACKGROUND OF THE INVENTION <EOH>Fluorescent hybridization probes have developed into an important tool in the sequence-specific detection of DNA and RNA. The signals generated by the appended fluorescent labels (or dyes) can be monitored in real time and provide simple, rapid, and robust methods for the detectio... | <SOH> SUMMARY OF THE INVENTION <EOH>Provided herein are water soluble conjugated polymers of Formula (I): wherein: each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distribut... | G01N3358 | 20170927 | 20180315 | 86750.0 | G01N3358 | 1 | TRUONG, DUC | Novel Reagents for Directed Biomarker Signal Amplification | UNDISCOUNTED | 1 | CONT-ACCEPTED | G01N | 2,017 | |
15,717,580 | PENDING | Novel Reagents for Directed Biomarker Signal Amplification | Described herein are methods, compositions and articles of manufacture involving neutral conjugated polymers including methods for synthesis of neutral conjugated water-soluble polymers with linkers along the polymer main chain structure and terminal end capping units. Such polymers may serve in the fabrication of nove... | 1.-40. (canceled) 41. A method of determining whether a target is present in a sample, the method comprising: contacting the sample with a conjugated polymer complex comprising a sensor for the target conjugated to a water soluble conjugated polymer having the structure of the formula: wherein: Ar is an aryl or heteroa... | CROSS-REFERENCE This application is a continuation of application Ser. No. 15/239,713, filed Aug. 17, 2016; which application is a continuation of application Ser. No. 14/821,386, filed Aug. 7, 2015 and issued as U.S. Pat. No. 9,547,008; which application is a continuation of application Ser. No. 14/018,985, filed Sep.... | <SOH> BACKGROUND OF THE INVENTION <EOH>Fluorescent hybridization probes have developed into an important tool in the sequence-specific detection of DNA and RNA. The signals generated by the appended fluorescent labels (or dyes) can be monitored in real time and provide simple, rapid, and robust methods for the detectio... | <SOH> SUMMARY OF THE INVENTION <EOH>Provided herein are water soluble conjugated polymers of Formula (I): wherein: each R is independently a non-ionic side group capable of imparting solubility in water in excess of 10 mg/mL; MU is a polymer modifying unit or band gap modifying unit that is evenly or randomly distribut... | G01N3358 | 20170927 | 20180315 | 86750.0 | G01N3358 | 1 | TRUONG, DUC | NOVEL REAGENTS FOR DIRECTED BIOMARKER SIGNAL AMPLIFICATION | UNDISCOUNTED | 1 | CONT-ACCEPTED | G01N | 2,017 | |
15,719,560 | ACCEPTED | FLOOR DRAIN FOR SAME FLOOR DRAINAGE WITHOUT DESCENDING FLOOR OF BUILDING | A floor drain for same floor drainage of a building consists of a floor drain body and a floor drain cover The floor drain body consists of a lower accumulated water collection tank, a lateral accumulated water collection tank and an accumulated water discharge port. A bottom of the lower accumulated water collection t... | 1. A floor drain for same floor drainage without descending floor of a building, consisting of a floor drain body (1) and a floor drain cover (2), wherein the floor drain cover (2) and the floor drain body (1) are separable; the floor drain body (1) consists of a lower accumulated water collection tank (3), a lateral a... | TECHNICAL FIELD The present invention relates to a floor drain for same floor drainage, and more specifically, to a floor drain for same floor drainage without descending floor of a building. BACKGROUND Currently, if same floor drainage needs to be realized in a building toilet, a floor of the toilet is required to be ... | <SOH> BACKGROUND <EOH>Currently, if same floor drainage needs to be realized in a building toilet, a floor of the toilet is required to be descended entirely or locally. To reduce the height of descending the floor, the width of a flow path of a floor drain and an area of a drainage section are also reduced, thereby ea... | <SOH> SUMMARY <EOH>The purpose of the present invention is to overcome existing technical defects, so as to provide a floor drain for same floor drainage used in the same floor drainage without descending floor of a building, thereby improving the unobstruction and difficult blocking of the drainage, being easy to main... | E03F50407 | 20170929 | 20180605 | 20180125 | 80742.0 | E03F504 | 0 | SCHNEIDER, CRAIG M | FLOOR DRAIN FOR SAME FLOOR DRAINAGE WITHOUT DESCENDING FLOOR OF BUILDING | SMALL | 1 | CONT-ACCEPTED | E03F | 2,017 |
15,721,589 | PENDING | OUTLET BOX | A utility box for mounting at least in part within a wall for use with a fluid carrying supply pipe, the box comprising, a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom, f... | 1. A utility box for mounting at least in part within a wall for use with a fluid carrying supply pipe, the box comprising: a housing including a top wall, a bottom wall, a first side wall and a second side wall, a back wall and a front opening providing access into an interior of the housing defined by the top, bottom... | RELATED APPLICATIONS This application claims benefit of U.S. Provisional Application No. 62/402,896, filed on Sep. 30, 2016, the entire disclosures and content of which are hereby incorporated by reference in their entirety. FIELD OF INVENTION The invention relates to outlet boxes for mounting in a wall, and more parti... | <SOH> BACKGROUND <EOH>Utility outlet boxes may be installed in building walls to provide access and/or disposal points for utilities, such as water. In one application, outlet boxes may be installed within building walls during the construction or renovation, and pipes and/or fixtures may be connected to the outlet box... | <SOH> BRIEF DESCRIPTION OF THE DRAWINGS <EOH>FIG. 1 illustrates a perspective view of a utility box according to a first embodiment. FIG. 2 illustrates a first exploded view of the utility box of FIG. 1 . FIG. 3 illustrates a second exploded view of the utility box of FIG. 1 . FIG. 4 illustrates a third exploded view o... | E03C1021 | 20170929 | 20180405 | 97595.0 | E03C102 | 0 | MURPHY, KEVIN F | OUTLET BOX | SMALL | 0 | ACCEPTED | E03C | 2,017 | |
15,722,239 | PENDING | INFORMATION PROCESSING APPARATUS CAPABLE OF ACHIEVING IMPROVED USABILITY, METHOD OF CONTROLLING INFORMATION PROCESSING APPARATUS, NON-TRANSITORY STORAGE MEDIUM ENCODED WITH PROGRAM READABLE BY COMPUTER OF INFORMATION PROCESSING APPARATUS, AND INFORMATION PROCESSING SYSTEM | An information processing system includes an operation apparatus and a main body apparatus which is capable of communicating with the operation apparatus. The operation apparatus includes a first transceiver which transmits operation data to the main body apparatus. The main body apparatus includes a memory in which an... | 1. An information processing system comprising: an operation apparatus; and a main body apparatus which is capable of communicating with the operation apparatus, the operation apparatus including a first transceiver which transmits operation data representing an operation by a user to the main body apparatus, the main ... | Information Processing Apparatus Capable of Achieving Improved Usability, Method of Controlling Information Processing Apparatus, Non-Transitory Storage Medium Encoded With Program Readable by Computer of Information Processing Apparatus, and Information Processing System This nonprovisional application is based on Jap... | <SOH> BACKGROUND AND SUMMARY <EOH>In a game system representing one example of a conventional information processing system, when a game controller representing an operation apparatus is registered in correspondence with a player number, the game controller may be registered by successively performing the same prescrib... | <SOH> BACKGROUND AND SUMMARY <EOH>In a game system representing one example of a conventional information processing system, when a game controller representing an operation apparatus is registered in correspondence with a player number, the game controller may be registered by successively performing the same prescrib... | A63F1322 | 20171002 | 20180510 | 65883.0 | A63F1322 | 0 | WILLIAMS, ROSS A | INFORMATION PROCESSING APPARATUS CAPABLE OF ACHIEVING IMPROVED USABILITY, METHOD OF CONTROLLING INFORMATION PROCESSING APPARATUS, NON-TRANSITORY STORAGE MEDIUM ENCODED WITH PROGRAM READABLE BY COMPUTER OF INFORMATION PROCESSING APPARATUS, AND INFORMATION PROCESSING SYSTEM | UNDISCOUNTED | 0 | ACCEPTED | A63F | 2,017 | |
15,724,732 | ACCEPTED | MASK SYSTEM WITH SNAP-FIT SHROUD | A shroud (1020) for a mask system includes a retaining portion structured to retain a frame (1040), a pair of upper headgear connectors (1024) each including an elongated arm (1026) and a slot (1027) at the free end of the arm adapted to receive a headgear strap, and a pair of lower headgear connectors (1025) each adap... | 1. A mask system, comprising: a frame defining a breathing chamber; a cushion provided to the frame and adapted to form a seal with the patient's face; and a shroud provided to the frame, wherein the shroud and the frame are co-molded with one another, the frame being constructed of a first, relatively soft, elastomeri... | CROSS-REFERENCE TO APPLICATION This application is a continuation of U.S. patent application Ser. No. 15/682,117, filed Aug. 21, 2017, pending, which is a continuation of U.S. patent application Ser. No. 15/440,972, filed Feb. 23, 2017, now U.S. Pat. No. 9,770,568, which is a continuation of U.S. patent application Ser... | <SOH> BACKGROUND OF THE INVENTION <EOH>Patient interfaces, such as a full-face or nasal mask systems, for use with blowers and flow generators in the treatment of sleep disordered breathing (SDB), typically include a soft face-contacting portion, such as a cushion, and a rigid or semi-rigid shell or frame. In use, the ... | <SOH> SUMMARY OF THE INVENTION <EOH>One aspect of the invention relates to a mask system provided without a forehead support adapted to engage the patient's forehead. Another aspect of the invention relates to a mask system including a frame and a shroud removably connected to the frame and adapted to attach headgear. ... | A61M160622 | 20171004 | 20180508 | 20180125 | 65185.0 | A61M1606 | 1 | DITMER, KATHRYN ELIZABETH | MASK SYSTEM WITH SNAP-FIT SHROUD | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61M | 2,017 |
15,725,437 | PENDING | MACHINE LEARNING DEVICE AND MACHINE LEARNING METHOD FOR LEARNING CORRELATION BETWEEN SHIPMENT INSPECTION INFORMATION AND OPERATION ALARM INFORMATION FOR OBJECT | A machine learning device which learns a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, includes a state observation unit which observes the shipment inspection information and the operation ... | 1. A machine learning device which learns a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object, comprising: a state observation unit which observes the shipment inspection information and the oper... | BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a machine learning device and a machine learning method for learning the correlation between shipment inspection information and operation alarm information for an object. 2. Description of the Related Art Conventionally, electric mo... | <SOH> BACKGROUND OF THE INVENTION <EOH> | <SOH> SUMMARY OF INVENTION <EOH>According to a first aspect of the present invention, there is provided a machine learning device which learns a correlation between shipment inspection information obtained by inspecting an object in shipment thereof and operation alarm information issued during operation of the object,... | G06Q5028 | 20171005 | 20180412 | 58717.0 | G06Q5028 | 0 | SECK, ABABACAR | MACHINE LEARNING DEVICE AND MACHINE LEARNING METHOD FOR LEARNING CORRELATION BETWEEN SHIPMENT INSPECTION INFORMATION AND OPERATION ALARM INFORMATION FOR OBJECT | UNDISCOUNTED | 0 | PENDING | G06Q | 2,017 | |
15,725,505 | PENDING | CONSIGNMENT BOOKING APPARATUSES, METHODS, AND SYSTEMS | Implementations for consignment booking include actions of providing a user interface including a plurality of consignment data entry fields that include a pickup location entry field configured to receive data identifying a pickup location for a consignment, a delivery destination entry field configured to receive dat... | 1. A computing system for consignment booking, the system comprising: a user interface module configured to cause a display of a plurality of consignment data entry fields on a computer display, the consignment data entry fields comprising: a pickup location entry field configured to receive data identifying a pickup l... | CROSS-REFERENCE TO RELATED APPLICATION This application claims priority to Indian Patent Application No. 201641034044, filed on Oct. 5, 2016, entitled “Consignment Booking Apparatuses, Methods, And Systems,” the entirety of which is hereby incorporated by reference. TECHNICAL FIELD The present application is related to... | <SOH> BACKGROUND <EOH>Present systems for booking consignments involve customers traveling to consignment agency locations to book the consignment. The customer fills out a hand written form at the booking agency location and provides it to an agency associate to book the consignment. The agency associate uses written ... | <SOH> SUMMARY <EOH>The inventors have appreciated that computer implemented systems and methods can improve the accuracy and efficiency of booking and delivering consignments. Accordingly, various implementations of the present disclosure are directed to methods, systems, and apparatuses, for booking and delivering con... | G06Q100835 | 20171005 | 20180405 | 63528.0 | G06Q1008 | 0 | WALSH, EMMETT K | CONSIGNMENT BOOKING APPARATUSES, METHODS, AND SYSTEMS | UNDISCOUNTED | 0 | PENDING | G06Q | 2,017 | |
15,726,165 | PENDING | Stable Aqueous Formulations of Adalimumab | The invention provides aqueous pharmaceutical adalimumab compositions suitable for long-term storage of adalimumab, methods of manufacture of these compositions, methods of administration, and kits containing same. | 1. A stable aqueous pharmaceutical composition comprising: i) adalimumab; ii) a buffer; and iii) a stabilizer; wherein the composition is free of polyol and has a pH of about 5 to about 6. 2. The composition of claim 1, wherein the composition is free of citrate buffer. 3. The composition of claim 1, wherein the compos... | FIELD OF THE INVENTION The present invention relates to aqueous pharmaceutical compositions suitable for long-term storage of adalimumab (including antibody proteins considered or intended as “biosimilar” or “bio-better” variants of commercially available adalimumab), methods of manufacture of the compositions, methods... | <SOH> BACKGROUND OF THE INVENTION <EOH>Tumor necrosis factor alpha (TNFα) is a naturally occurring mammalian cytokine produced by various cell types, including monocytes and macrophages in response to endotoxin or other stimuli. TNFα is a major mediator of inflammatory, immunological, and pathophysiological reactions (... | <SOH> SUMMARY OF THE INVENTION <EOH>The invention provides stable aqueous formulations comprising adalimumab that allow its long term storage. In a first embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab; a stabilizer comprising at least one member selected from the gr... | A61K3939591 | 20171005 | 20180215 | 72243.0 | A61K39395 | 1 | KIM, YUNSOO | Stable Aqueous Formulations of Adalimumab | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 | |
15,726,215 | PENDING | Stable Aqueous Formulations of Adalimumab | The invention provides aqueous pharmaceutical adalimumab compositions suitable for long-term storage of adalimumab, methods of manufacture of these compositions, methods of administration, and kits containing same. | 1. A stable aqueous pharmaceutical composition comprising: i) adalimumab; ii) a single buffer; iii) a surfactant; and iv) a sugar, wherein the composition is free of polyol and has a pH of about 5 to about 6. 2. The composition of claim 1, wherein the composition is free of citrate buffer. 3. The composition of claim 2... | FIELD OF THE INVENTION The present invention relates to aqueous pharmaceutical compositions suitable for long-term storage of adalimumab (including antibody proteins considered or intended as “biosimilar” or “bio-better” variants of commercially available adalimumab), methods of manufacture of the compositions, methods... | <SOH> BACKGROUND OF THE INVENTION <EOH>Tumor necrosis factor alpha (TNFα) is a naturally occurring mammalian cytokine produced by various cell types, including monocytes and macrophages in response to endotoxin or other stimuli. TNFα is a major mediator of inflammatory, immunological, and pathophysiological reactions (... | <SOH> SUMMARY OF THE INVENTION <EOH>The invention provides stable aqueous formulations comprising adalimumab that allow its long term storage. In a first embodiment, the invention provides a stable aqueous pharmaceutical composition comprising adalimumab; a stabilizer comprising at least one member selected from the gr... | A61K3939591 | 20171005 | 20180215 | 72243.0 | A61K39395 | 1 | KIM, YUNSOO | Stable Aqueous Formulations of Adalimumab | UNDISCOUNTED | 1 | CONT-ACCEPTED | A61K | 2,017 | |
15,726,899 | PENDING | WIRELESS PRINTING DEVICES THAT PROVIDE PRINTING SERVICES OVER A NETWORK WITHOUT A PRINTER SPECIFIC PRINTER DRIVER AFTER HAVING REGISTERED THE PRINTING DEVICE WITH A SERVICE OVER THE NETWORK | Wireless printing devices that are configured to register with a service over a network (e.g., Internet) for providing printing services for one or more client devices without printer drivers are herein disclosed and enabled. The printing device may include a touch sensitive screen interface to receive security informa... | 1. A printing device that is a wireless printing device for wirelessly providing printing services to one or more client devices over a network without the need for the one or more client devices to install a device specific printer driver that is device specific to the printing device, the printing device includes: an... | CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation of U.S. patent application Ser. No. 10/053,765 filed Jan. 18, 2002, which claims priority to U.S. Provisional Patent Application Ser. No. 60/262,764, filed Jan. 19, 2001. Additionally, this application is a continuation-in-part of U.S. patent ap... | <SOH> BACKGROUND OF THE DISCLOSURE <EOH>The present invention relates to universal data output and, in particular, to providing a new data output method and a new raster image process for information apparatuses and output devices. As described herein, information apparatuses refer generally to computing devices, which... | <SOH> SUMMARY OF THE INVENTION <EOH>Accordingly, this invention provides a convenient universal data output method in which an information apparatus and an output device or system share the raster image processing operations. Moreover, the new data output method eliminates the need to install a plurality of device-depe... | G06F31236 | 20171006 | 20180208 | 66411.0 | G06F312 | 6 | RILEY, MARCUS T | WIRELESS PRINTING DEVICES THAT PROVIDE PRINTING SERVICES OVER A NETWORK WITHOUT A NEED FOR A CLIENT DEVICE OF THE PRINTING DEVICE TO USE, AT THE CLIENT DEVICE, A PRINTER SPECIFIC PRINTER DRIVER | UNDISCOUNTED | 1 | CONT-ACCEPTED | G06F | 2,017 | |
15,726,901 | PENDING | AMLODIPINE FORMULATIONS | Provided herein are stable amlodipine oral liquid formulations. Also provided herein are methods of using amlodipine oral liquid formulations for the treatment of certain diseases including hypertension and Coronary Artery Disease (CAD). | 1. An oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (v) about 7.5 mg/ml of hydroxypropyl methylcellulose; ... | CROSS-REFERENCE This application claims the benefit of U.S. Application Ser. No. 62/405,455 filed Oct. 7, 2016, which is hereby incorporated by reference in its entirety. BACKGROUND OF THE INVENTION Hypertension, or high blood pressure, is a serious health issue in many countries. According to the National Heart Blood ... | <SOH> BACKGROUND OF THE INVENTION <EOH>Hypertension, or high blood pressure, is a serious health issue in many countries. According to the National Heart Blood and Lung Institute, it is thought that about 1 in 3 adults in the United States alone have hypertension. Left unchecked, hypertension is considered a substantia... | <SOH> SUMMARY OF THE INVENTION <EOH>Disclosed herein is an oral liquid formulation, comprising: (i) amlodipine benzoate in an amount corresponding to 1.0 mg/ml amlodipine freebase; (ii) about 3 mM of a citrate buffer; (iii) about 0.2 mg/ml to about 10 mg/ml of sodium benzoate; (iv) about 0.5 mg/ml of silicon dioxide; (... | A61K314422 | 20171006 | 20180412 | 96348.0 | A61K314422 | 1 | SOROUSH, LAYLA | AMLODIPINE FORMULATIONS | UNDISCOUNTED | 0 | ACCEPTED | A61K | 2,017 |
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