The FAS Antibody from MyBioSource.com is a Mouse Monoclonal antibody. This antibody recognizes Human antigen. The FAS Antibody has been shown to work in the following applications: ELISA, Flow Cytometry, Immunocytochemistry, Immunofluorescence, and Western Blot.
Description
Description: The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contains a death domain. It has been shown to play a central role in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The interaction of this receptor with its ligand allows the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10. The autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, and leads to apoptosis. This receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is found to be involved in transducing the proliferating signals in normal diploid fibroblast and T cells. At least eight alternatively spliced transcript variants encoding seven distinct isoforms have been described. The isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform.
Function: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro).
Subunit Structure: Binds DAXX. Interacts with HIPK3. Part of a complex containing HIPK3 and FADD (By similarity). Binds RIPK1 and FAIM2 (PubMed:7538908, PubMed:10535980). Interacts with BABAM2 and FEM1B (PubMed:10542291, PubMed:15465831). Interacts with FADD (PubMed:21109225, PubMed:19118384). Interacts directly (via DED domain) with NOL3 (via CARD domain); inhibits death-inducing signaling complex (DISC) assembly by inhibiting the increase in FAS-FADD binding induced by FAS activation (By similarity). Interacts with CALM (PubMed:24914971).
Post-translational Modifications: N-and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.
Similarity: Contains a death domain involved in the binding of FADD, and maybe to other cytosolic adapter proteins