Anti-Recombinant Caspase 9, clone R09-4C4

Caspase 9,apoptosis-related cysteine protease (CASP9,synonyms: MCH6,APAF3,APAF-3,ICE-LAP6,CASPASE-9c)is a member of the cysteine-aspartic acid protease (caspase) family. 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. Capase 9 is processed by caspase APAF1, this step is thought to be one of the earliest in the caspase activation cascade. Protein function: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates effector caspases caspase-3 (CASP3) or caspase-7 (CASP7). Promotes DNA damage- induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). [The UniProt Consortium]