Anti-Pro Caspase-8 antibody [EPR162] - BSA and Azide free

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Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed : 23516580, PubMed : 35338844, PubMed : 35446120, PubMed : 8681376, PubMed : 8681377, PubMed : 8962078, PubMed : 9006941, PubMed : 9184224). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed : 23516580, PubMed : 35338844, PubMed : 35446120, PubMed : 8681376, PubMed : 8681377, PubMed : 8962078, PubMed : 9006941, PubMed : 9184224). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed : 16916640, PubMed : 8962078, PubMed : 9006941). Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed : 8681376, PubMed : 8681377). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed : 9184224). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed : 9184224). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed : 9184224). Also cleaves and activates BID, thereby promoting cytochrome C release from mitochrondria (By similarity). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis : acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed : 31827280, PubMed : 31827281). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively) : gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed : 32929201, PubMed : 34012073). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (PubMed : 8755496). Cleaves PARP1 and PARP2 (PubMed : 8681376). Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed : 18216014, PubMed : 27109099).. 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 (PubMed : 12010809).. Isoform 8. Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex.

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MCH5, CASP8, Caspase-8, CASP-8, Apoptotic cysteine protease, Apoptotic protease Mch-5, CAP4, FADD-homologous ICE/ced-3-like protease, FADD-like ICE, ICE-like apoptotic protease 5, MORT1-associated ced-3 homolog, FLICE, MACH