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Caspase-8 (FLICE/MACH-1) is a 55kDa cytosolic protein with homology to the CD95/Fas-associated signal transducer, FADD/MORT-1, as well as to other caspase (ICE/Ced-3) cysteine proteases. The N-terminal region of caspase-8 contains an amino acid sequence, termed the death domain, that facilitates caspase-8-FADD direct interaction. FADD therefore acts as an adapter molecule, allowing caspase-8 to become recruited to the cytoplasmic region of Fas following receptor activation. Viral proteins (v-FLIPS) which inhibit recruitment and activation of caspase-8 have been isolated. Caspase-8 is produced as a proenzyme (55/50kDa doublet) which upon receptor aggregation is proteolytically cleaved into smaller subunits of 40/36 (doublet), and 23kDa. Overexpression of caspase-8 is sufficient to induce apoptosis in certain cell lines (e.g., MCF-7) and this phenotype is blocked by overexpression of the caspase-3 protease inhibitor, CrmA. The antibody recognizes both the proform of human caspase-8 (55/50kDa doublet) as well as the cleaved forms which migrate at 40/36 (doublet) and 23kDa in SDS/PAGE. It also immunoprecipitates the full-length human caspase-8. Full-length recombinant human caspase-8 protein was used as immunogen.Host Species: MouseClone: 3-1-9Isotype: IgG1 κSpecies Reactivity: HumanImmunogen: Human Caspase-8 full-length recombinant proteinImmunoprecipitation, Western Blotting
