Anti-Gfi-1: Mouse Gfi-1 Antibody

Gfi-1 functions mainly as a repressor of transcription. It represses its target genes by binding to consensus DNA elements containing the AATC core sequence. The Gfi-1 protein consists of an N-terminal SNAG domain required for nuclear localization, a central region and 6 C-terminal zinc fingers (ZFs) involved in DNA binding. The SNAG domain is important for transcriptional repression; however, Gfi-1 may repress transcription through both SNAG domain-dependent and independent mechanisms. The different domains of Gfi-1 have been implicated in recruiting corepressors and histone modifying enzymes, including eight-twenty-one (ETO), CoREST, histone demethylase LSD1, histone deacetylases (HDACs) 1 and 2, and the histone lysine methyltransferase G9a. The mechanisms by which Gfi-1 controls cell proliferation and survival are still poorly understood. It has been shown that Gfi-1 binds to and represses CDKN1A encoding the cyclin-dependent kinase inhibitor (CDKI) ^p21Cip, and the proapoptotic Bcl2 family member Bax. Myc-interacting zinc finger protein-1 (Miz-1) is a POZ-ZF transcription factor originally identified as a binding partner of c-Myc. Miz-1 possesses a potent anti-growth activity and has been shown to activate transcription by directly binding to the initiator (Inr) elements in its target genes, including Mad4, CDKN1A, and CDKN2B encoding the CDKI ^p15INK4B. It was shown that Gfi-1 interacts with Miz-1 and is recruited to the core promoter of CDKN2B via Miz-1, leading to transcriptional repression.³ In addition, Gfi1 functions as an antagonist of NF-kappaB activity at the level of promoter binding. This suggested a new function of Gfi1 as a general negative regulator of the endotoxin-initiated innate immune responses, including septic shock and possibly other severe inflammatory diseases.⁴