Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis.1 The precursor form of all caspases is composed of a prodomain and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation, and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into an a2b2 tetramer to form the active enzyme. The gene for caspase-3, also known as yama, CPP32, and apopain, codes for a 32 kDa protein.2,3,4 Caspase-3 cleaves the death substrate poly(ADP-ribose) polymerase (PARP) to a specific 85 kDa form observed during apoptosis and is inhibitable by the CrmA protein. Other caspase-3 substrates include DNA-PK, actin, GAS2, procaspase-6, etc.5 Caspase-3 is activated by cleavage events at Asp28/Ser29 (between N-terminal pro-domain) and Asp175/Ser176 (between large and small subunits) to generate a large subunit of 17 kDa and a small subunit of 12 kDa.3WARNING This product is not for human or veterinary use.
