Anti-Caspase-3, Pro and Active, clone CAS3836

0.5 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide. Caspases, or cysteine-aspartic proteases, are a family of cysteine proteases that play essential roles in inflammation, apoptosis and necrosis. They are often referred to as the 'executioners of apoptosis.' Caspases are synthesized as inactive proenzymes comprising an N-terminal peptide (prodomain) together with one large and one small subunit. Active caspase-1 and -3 are heterodimers, containing two small and two large subunits. Active Caspase-3 subunits are 17kD (p17) and 12kD (p12). Pro Caspase-3 is inactive and has virtually no activity until it is cleaved by an initiator caspase. It is activated by Caspases -8, -9 and -10 ('initiator caspases') and then effects apoptosis by cleaving targeted cellular proteins. 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]