Caspase-8 is an initiator caspase with roles in cell death, including induction of apoptosis and pyroptosis and inhibition of necroptosis.1 It is widely expressed during development and adulthood with high levels of expression in the heart and limb buds, as well as other tissues, in development and in leukocytes in adulthood.2 It localizes to the cytosol and can be found in the lamella of migrating cells.3 Caspase-8 is produced as an inactive proenzyme containing a prodomain, which is composed of two N-terminal death-effector domains (DEDs), and two C-terminal catalytic subunits: p18 and p10.4,1 Activation of the proenzyme occurs when it binds to the death-inducing signaling complex (DISC), which is composed of CD95, a Fas-associated death domain (FADD) protein, and cellular FLICE-like inhibitory protein (c-FLIP). Upon DISC binding, procaspase-8 is cleaved to release the p10 subunit then the p18 subunit. Together, two of each subunit form an activated and stabilized heterotetramer, which cleaves other procaspases, including procaspase-3 and procaspase-7, to initiate the extrinsic apoptosis pathway. Caspase-8 also has a role in the innate immune response via its activation by toll-like receptor 4 (TLR4) signaling and its initiation of the pyroptosis pathway through the NOD-like receptor protein 3 (NLRP3) inflammasome.1 Mutations in CASP8, the gene encoding caspase-8, or dysfunctional caspase-8 activity are associated with a variety of conditions, including autoimmune disorders, immunodeficiencies, and an increased risk of cancer. Cayman’s Caspase-8 Monoclonal Antibody (Clone 90A992) can be used for flow cytometry (FC), immunohistochemistry (IHC), and Western blot applications.WARNING This product is not for human or veterinary use.
