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|7237||Cleaved Caspase-9 (Asp330) (D2D4) Rabbit mAb||
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Cleaved Caspase-9 (Asp330) Antibody (Human Specific) detects endogenous levels of the large fragment (37 kDa with prodomain/17 kDa) of caspase-9 following cleavage at aspartic acid 330. The antibody does not recognize the uncleaved procaspase-9.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino terminus residues surrounding to Asp330 of human caspase-9. Antibodies are purified by protein A and peptide affinity chromatography.
Caspase-9 (ICE-LAP6, Mch6) is an important member of the cysteine aspartic acid protease (caspase) family (1,2). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with the 47 kDa procaspase-9/Apaf-1. Apaf-1 mediated activation of caspase-9 involves intrinsic proteolytic processing resulting in cleavage at Asp315 and producing a p35 subunit. Another cleavage occurs at Asp330 producing a p37 subunit that can serve to amplify the apoptotic response (3-6). Cleaved caspase-9 further processes other caspase members, including caspase-3 and caspase-7, to initiate a caspase cascade, which leads to apoptosis (7-10).
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
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