Caspase-8 binds to the death effector domain (DED) of FADD through an analogous DED domain present in tandem in the proform of the caspase-8 protein. Recruitment of caspase-8 to the Fas receptor results in oligomerization of the caspase-8 protein, which in turn drives its autoactivation through "self-cleavage". Activated caspase-8 then activates other downstream caspases including caspase-9, thereby commiting the cell to undergo apoptosis. This antibody also detects the processed forms (42/44kDa, 25kDA, and 14kDa) of caspase-8.
Apoptotic cysteine protease; Apoptotic protease Mch-5; CAP4; CASP-8; caspase 8, apoptosis-related cysteine peptidase; caspase 8, apoptosis-related cysteine protease; Caspase-8; Caspase-8 precursor; EC 3.4.22.-; EC 22.214.171.124; FADD-homologous ICE/CED-3- like protease; FADD-homologous ICE/CED-3-like protease; FADD-like ICE; FLICE; ICE-like apoptotic protease 5; ICE8; MACH; MACH-alpha-1/2/3 protein; MACH-beta-1/2/3/4 protein; MCH5; MORT1-associated CED-3 homolog
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