Background：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 MW of 50-70 kDa. This antibody can recognize p17, p19 and p32 of Caspase 3.
