Anti-Caspase-3 (Pro and Active) (Clone: ABM1C12)

Caspases are a member of the cysteine-aspartic acid protease family. Caspase-3 (31 kDa) is an executionary caspase which directly cleaves and activates poly(ADP-ribose) polymerase (PARP), sterol regulatory element binding proteins (SREBPs) or it can also interact with other caspases like caspase-6, -7 and -9. Increased levels of caspase-3 are involved in Huntington Disease-associated cell death. Caspase-3 is the principal caspase in mediating the cleavage of amyloid-beta 4A precursor protein (APP), which is related with neuronal death in Alzheimer's disease. Like other caspases, caspase-3 is also synthesized as a zymogen procaspase which is activated by specific proteolytic cleavage. High levels of caspase-3 are observed in lung, spleen, heart, liver and kidney, moderate levels in brain and skeletal muscle, and low in testis. 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. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. [The UniProt Consortium]