CASP3, EnkiLife, AMRe06554

Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. Involved in the activation cascade of caspases responsible for apoptosis execution (PubMed: 7596430). At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216- Asp-|-Gly-217' bond (PubMed: 7774019). 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 (PubMed: 7596430). Involved in the cleavage of huntingtin (PubMed: 8696339). Triggers cell adhesion in sympathetic neurons through RET cleavage (PubMed: 21357690). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed: 23152800). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed: 23845944, PubMed: 33725486).