Initiator caspases, which include caspase-8, activate effector caspases by cleaving inactive forms of effector caspases. In the activation cascade responsible for apoptosis induced by TNFRSF1A and mediated by TNFRSF6/FAS, caspase-8 is the most upstream protease. Caspase-8 binds to adaptor molecule FADD, forming an aggregate referred to as death-inducing signaling complex (DISC), which activates caspase-8. The actived protein is released from the complex and further activates downstream apoptotic proteases. Caspase-8, which is a heterodimer consisting of two subunits (p18 and p10), is widely expressed, but is detected at highest levels in peripheral blood leukocytes (PBLs), thymus, liver and spleen. Defects in CASP8, the gene encoding for caspase-8, may cause CASP8D (caspase-8 deficiency disorder), which is characterized by splenomegaly and CD95-induced apoptosis of PBLs, may lead to immunodeficiency due to defects in T lymphocyte, NK cell and B lymphocyte activation.
Immunogen
peptide
Key Feature
Clonality
Monoclonal
Isotype
IgG1
Host Species
Mouse
Tested Applications
WBIPIFIHC-P
WB:1:100-1:1,000 IP:1-2 μg per 100-500 μg of total protein(1 ml of cell lysate) IF:1:50-500 IHC:1:50-500