Background: Caspase-9 exists as a pro-form (mw ~46 kDa) that is cleaved by the activity of Apaf-1 in the presence of cytosolic cytochrome c (Apaf-2) and dATP. The processing of pro-caspase-9 into a heterodimer consisting of a 35kDa and a 10 kDa chain activates the protease and induces the cascade leading to cleavage of caspase-3 and other apoptotic targets. The processing of caspase-9 may be blocked by the activity of bcl-x which physically interacts with the caspase-/Apaf-1 complex.
Immunogen: Synthetic peptide corresponding to amino acids 301-313 of human caspase-9
Purification Method: Ammonium Sulfate Precipitation
Concentration: See vial for concentration
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide
References: 1. Duan H, et al., ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B. J. Biol. Chem. 1996, 271, 16720-167242. Srinivasula SM, et al., The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. J. Biol. Chem. 1996, 271, 27099-271063. Li P, et al., Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997, 91, 479-4894. Pan G, et al., Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J. Biol. Chem. 1998, 273, 5841-5845
UniProt: P55211
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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