Mammalian Expression Vector Construction and the Coordinated Expression of Proteins
{'Code': '15030000', 'Directorate': {'Abbreviation': 'TIP', 'LongName': 'Dir for Tech, Innovation, & Partnerships'}, 'Division': {'Abbreviation': 'TI', 'LongName': 'Translational Impacts'}}
{'SignBlockName': 'Ritchie B. Coryell', 'PO_EMAI': None, 'PO_PHON': None}
A need exists for a source of biologically active human proteins,               particularly those with complex tertiary or quaternary structure which          require modification for full biological activity.  Current production          of recombinant molecules by bacteria has limited ability to satisfy             this need.  Cultured mammalian cells provide greater promise as                 production systems.  Cell lines, such as Chinese hamster ovary (CHO),           have been shown capable of expressing and properly processing a                 variety of human recombinant proteins, and are adaptable to large-              scale cultivation in serum free media.  This work addresses the need            for an improved expression system to facilitate the production of               proteins that are composed of two different subunits.  The system               proposed will utilize a plasmid vector containing transcription                 promoters from SV40 and the mouse mammary tumor virus, which is                 integrated into the genome of Chinese hamster ovary cells (CHO).  In            this construction, both promoters will be capable of directing high             levels of production, and the ratio of synthesis of the two proteins            produced can be adjusted to achieve the proper ratio of precursor               proteins for efficient folding and final assembly.  The plasmid will            be constructed and tested for expression using bacterial reporter               genes.  Growth and expression in serum free media will be optimized in          the production of human Insulin-like Growth Factor-1 (1GF-1), a small           biologically important peptide currently produced by this laboratory            using a recombinant                                                             bacterial system.                                                                                                                                               The medical use of peptides and proteins is an immature                         pharmaceutical market.  However, clinical usage is expected to                  grow substantially during the next five years.  Data indicates                  the current annual market for medically important                               peptides/proteins exceeds $175.6 million.  However, peptides                    world markets associated with the mammalian cell technology                     addressed in this proposal could reach $3.04 billion by 1991.
{'FirstName': 'Gopalam', 'LastName': 'Somasekhar', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Gopalam Somasekhar', 'EmailAddress': None, 'PI_PHON': None, 'NSF_ID': '000341791', 'StartDate': '01/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Incell Corporation', 'CityName': 'Milwaukee', 'ZipCode': '532242411', 'PhoneNumber': '4142634111', 'StreetAddress': '9075 West Heather Avenue', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Wisconsin', 'StateCode': 'WI', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'WI04', 'ORG_UEI_NUM': None, 'ORG_LGL_BUS_NAME': None, 'ORG_PRNT_UEI_NUM': None}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '5371', 'Text': 'SBIR Phase I'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8860905.xml'}