Background |
Caspases are cysteine proteases, expressed as inactive precursors, that mediate apoptosis by proteolysis of specific substrates. Caspases have the ability to cleave after aspartic acid residues. There are two classes of caspases involved in apoptosis, initiators (activation by receptor cluster) and effectors (activation by mitochondrial permeability transition). Proapoptotic signals autocatalytically activate initiator caspases, such as Caspase 8 and Caspase 9. Activated initiator caspases then process effector caspases, such as Caspase 3 and Caspase 7, which in turn cause cell collapse. |
WB |
Western blot (WB) analysis of p-Caspase-8 (Y380) pAb at 1:500 dilution Lane1:HEK293T cell lysate treated with PMA(100nM, 15mins) Lane2:Hela cell lysate treated with PMA(100nM, 15mins) Lane3:H9C2 cell lysate treated with PMA(100nM, 15mins) |
Alternative Name |
Caspase-8, Caspase8, 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, Caspase-8 subunit p18, Caspase-8 subunit p10, CASP8, MCH5 |