|Other Names||Transcription factor E2F1, E2F-1, PBR3, Retinoblastoma-associated protein 1, RBAP-1, Retinoblastoma-binding protein 3, RBBP-3, pRB-binding protein E2F-1, E2F1, RBBP3|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC- 3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:20176812).|
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E2F1 is a member of the E2Ffamily of transcription factors. The E2F family plays a crucialrole in the control of cell cycle and action of tumor suppressorproteins and is also a target of the transforming proteins of smallDNA tumor viruses. The E2F proteins contain several evolutionallyconserved domains found in most members of the family. Thesedomains include a DNA binding domain, a dimerization domain whichdetermines interaction with the differentiation regulatedtranscription factor proteins (DP), a transactivation domainenriched in acidic amino acids, and a tumor suppressor proteinassociation domain which is embedded within the transactivationdomain. This protein and another 2 members, E2F2 and E2F3, have anadditional cyclin binding domain. This protein binds preferentiallyto retinoblastoma protein pRB in a cell-cycle dependent manner. Itcan mediate both cell proliferation and p53-dependent/independentapoptosis.
Pulikkan, J.A., et al. Blood 115(9):1768-1778(2010)Paik, J.C., et al. J. Biol. Chem. 285(9):6348-6363(2010)Alla, V., et al. J. Natl. Cancer Inst. 102(2):127-133(2010)Helin, K., et al. Cell 70(2):337-350(1992)
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