Caspase-9 is a cytoplasmic proenzyme that associates with both pro-apoptotic and anti-apoptotic proteins. It is a key regulator of apoptosis and also functions in embryonic development.
Also known as ICE like apoptotic protease 6 (ICE LAP6), apoptotic protease Mch6, and apoptotic protease activating factor 3 (Apaf3)) 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. ProCaspase 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, BclXL, cIAP1, cIAP2, XIAP, and Livin. This caspase becomes activated when recruited to Apaf1/cytochrome c complex, and following cleavage by Apaf1, 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.
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Name Catalog # Cathepsin D GT15042 Caspase-3 GT15044 Cathepsin B (Human) GT15046 Cathepsin B (Mouse) GT15047 Cathepsin L (Human) GT15048 Cathepsin L (Mouse) GT15049 Cathepsin O GT15197 Cathepsin S GT15198 Cathepsin V GT15199 Cathepsin F MO15096 Cathepsin G MO20021 Caspase-7 MO25036 Caspase-3, active RA15046 Caspase-10/b-Flice 2 RA15047 Caspase-12 RA15048 Caspase-14 RA30061 CARD8 RA30062 CARD9 RA30063