Anti-CASP3

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. Protein function: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-, -Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage. Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. [The UniProt Consortium]