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|GT15045||50 ul||$190.00||Buy Now | Add to Cart|
|GT15045||100 ul||$345.00||Buy Now | Add to Cart|
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 intereacts with BIRC7 and has been shown to cleave PARP and vimentin.
Image: Immunoblots of extracts from 2 x 105 human Jurkat cells treated with staurosporine (STS, 1 μg/mL) for the indicated times. Samples were electrophoresed on 15% gels and immunoblotting was with 1.0 μg/mL goat anti-Caspase-9 that detects the precursor and 34 and 37 kDa forms of pro + LSU.
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