Caspase-9 (Pro)

GWB-5D0729

Caspase-9 (ICE-LAP6 Mch-6 Apaf-3) is a member of the cysteine aspartic acid protease or caspase family. Pro-Caspase-9 exists as a 46 kDa isomer that is cleaved by apoptotic stimulation and functions as the major initiator caspase in programmed cell death or apoptosis (1-4). Upon stimulation cytochrome c is released from mitochondria and associates with the Pro-Caspase-9/Apaf 1 complex. This complex in turn activates Pro-Caspase-9 by cleaving it into an active 35 kDa fragment and a small 10 kDa fragment (1 2). Activated Caspase-9 cleaves Caspase-3 as well as poly (ADP-ribose) polymerase (PARP) to initiate a caspase cascade and apoptosis (3 4).

WB: 1:100-500IHC: 1:50-100ICC: 1:50FC: 1:100IP: 1:100. A synthetic peptide corresponding to C-terminus of human Caspase-9 p35 subunit was used as immunogen. The antibody should recognize only pro-form (46kDa) . 1. Kuida K. et al. Reduced Apoptosis and Cytochrome c2. Li P. et al. Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade. Cell 91: 4793. 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. 271: 167204. Srinivasula S. M. 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. 271: 270995. Manufactured under U. S. Patents No. 5 675 063 and 7 429 487