FAF1 Anticuerpo(A-16): sc-1886

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In contrast to growth factors which promote cell proliferation, FAS ligand (FAS-L) and the tumor necrosis factors (TNFs) rapidly induce apoptosis (1,2). Cellular response to FAS-L and TNF is mediated by structurally related receptors containing a conserved "death domain" and belonging to the TNF receptor superfamily (1-4). TRADD, FADD and RIP are FAS/TNF-RI interacting proteins that contain a death domain homologous region (DDH) (5-7). TRADD (TNF-RI-associated death domain) and FADD (FAS-associated death domain) associate with the death domains of both FAS and TNF-RI via their DDH regions (5,6), while RIP associates exclusively with FAS (7). An additional FAS interacting protein designated FAF1, for FAS-associated protein factor-1, binds with the cytoplasmic tail of wild type but not lpr mutant FAS (8). When overexpressed in cells, FAF1 enhances the efficiency of FAS-mediated apoptosis (8). In contrast to TRADD, FADD and RIP, FAF1 lacks a DDH and cannot induce apoptosis independently of FAS activation (8).