Purified anti-Caspase-9

Caspase 9 (also known as ICE-like apoptotic protease 6 (ICE-LAP6), apoptotic protease Mch-6, and apoptotic protease activating factor 3 (Apaf-3)) is a member of the peptidase family C14 that contains a CARD domain. This caspase is active as a heterotetramer and has been reported to have two isoforms. Pro-Caspase 9 has been reported to be approximately 47 kD. This caspase is present in the cytosol and, upon activation, translocates to the mitochondria. Caspase 9 is involved in the caspase activation cascade responsible for apoptosis execution and cleaves/activates Caspase 3 and Caspase 6. Caspase 9 is inhibited by the dominant negative isoform, Bcl-XL, c-IAP1, c-IAP2, XIAP, and Livin. This caspase becomes activated when recruited to Apaf-1/cytochrome c complex, and following cleavage by Apaf-1, granzyme B, Caspase 3, possibly Caspase 8 and Caspase 10 into large p37 and small p10 subunits. Caspase 9 interacts with BIRC7 and has been shown to cleave PARP and vimentin. The 96-2-22 monoclonal antibody has been shown to be useful for Western blotting of human caspase 9 (46 kD pro-caspase 9 as well as the 34 kD cleaved caspase 9).