Human CASP8 (Caspase 8) ELISA Kit

Caspase-8; Casp-8; Apoptotic Cysteine Protease; Apoptotic Protease Mch-5; Cap4; Fadd-Homologous Ice/Ced-3-Like Protease; Fadd-Like Ice; Flice; Ice-Like Apoptotic Protease 5; Mort1-Associated Ced-3 Homolog; Mach Cleaved Into - Caspase-8 Subunit P18 - Caspase-8 Subunit P10

Uniprot ID: MBP_HUMAN ; Reactome: R-HSA-111465 ; Gene ID: 841

Tissue Specificity: Isoform 1, isoform 5 and isoform 7 are expressed in a wide variety of tissues. Highest expression in peripheral blood leukocytes, spleen, thymus and liver. Barely detectable in brain, testis and skeletal muscle.

Function: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the Granzyme B (GZMB) apoptotic pathways. Cleaves PARP1. Cleaves RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response. Isoform 5: Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex. Isoform 6: Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex. Isoform 7: Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex (Probable). Acts as an inhibitor of the caspase cascade. Isoform 8: Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.