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Antigen:
human caspase-9 amino acids 299-318 (ASTSPEDESPGSNPEPDATP)
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Host:
rabbit
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Application(s):
WB
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Apoptosis is related to many diseases and is induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf3.1,2,3 Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation.3 Caspase-9 is also activated by granzyme B and CPP32.1,2 Activated caspase-9 cleaves and activates caspase-3, one of the key proteases responsible for the proteolytic cleavage of many key proteins in apoptosis.3 Caspase-9 plays a central role in cell death induced by a wide variety of apoptosis inducers including TNFα, TRAIL, anti-CD-95, FADD, and TRADD.4 Caspase-9 is expressed in a variety of human tissues.1,2
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1
Srinivasula, S.M., Fernandes-Alnemri, T., Zangrilli, J., et al. The Ced-3/interleukin 1β converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2α are substrates for the apoptotic mediator CPP32. J Biol Chem 271 27099-27106 (1996).
2
Duan, H., Orth, K., Chinnaiyan, A.M., 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 271 16720-16724 (1996).
3
Li, P., Nijhawan, D., Budihardjo, I., et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 479-489 (1997).
4
Pan, G., O'Rourke, K., Dixit, V.M. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J Biol Chem 273 5841-5845 (1998).
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