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Caspases, a family of endoproteases, are critical players in cell regulatory networks controlling inflammation and cell death. Initiator caspases (caspase-2, -8, -9, -10, -11, and -12) cleave and activate downstream effector caspases (caspase-3, -6, and -7), which in turn execute apoptosis by cleaving targeted cellular proteins. Caspase 3 (also named CPP32, SCA-1, and Apopain) proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at the beginning of apoptosis. Caspase 3 plays a key role in the activation of sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Caspase 3 can also form heterocomplex with other proteins and performs the molecular mass of 50-70 kDa(PMID:9747872). This antibody can recognize p17, p19 and p32 of Caspase 3.
