CGI-03, FAS-associated factor 1, HFAF1s, UBX domain-containing protein 12, UBX domain-containing protein 3A
In contrast to growth factors which promote cell proliferation, FAS ligand (FAS-L) and the tumor necrosis factors (TNFs) rapidly induce apoptosis. 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. TRADD, FADD and RIP are FAS/TNF-alphaI interacting proteins that contain a death domain homologous region (DDH). TRADD (TNF-alphaI-associated death domain) and FADD (FAS-associated death domain) associate with the death domains of both FAS and TNF-alphaI via their DDH regions, while RIP associates exclusively with FAS. An additional FAS interacting protein designated FAF1, for FAS-associated protein factor-1, binds with the cytoplasmic tail of wildtype but not LPR mutant FAS. When overexpressed in cells, FAF1 enhances the efficiency of FAS-mediated apoptosis. In contrast to TRADD, FADD and RIP, FAF1 lacks a DDH and cannot induce apoptosis independently of FAS activation.
Western Blot (1-2ug/ml),Immunohistochemistry (Formalin-fixed) (1-2ug/ml for 30 min at RT)(Staining of formalin-fixed tissues requires heating tissue sections in 10mM Tris with 1mM EDTA, pH 9.0, for 45 min at 95&degC followed by cooling at RT for 20 mi
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