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 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 form heterocomplex with other proteins. This antibody is specific for cleaved caspase 3, and does not recognize full length caspase-3. The cleaved P17 and P19 fragment might form complex and shows at around 30-35 kDa by western blot (PMID: 25501826).