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Caspase-3 is a cysteinyl aspartic protease with roles in both extrinsic and intrinsic apoptosis.1,2 Upon apoptotic signaling via death receptors or mitochondrial assembly of pro-apoptotic factors, the zymogen procaspase-3 is cleaved into two subunits, p17 and p12, which form an active heterodimer that recognizes and cleaves proteins containing the canonical peptide sequence DEVD to drive apoptosis.3,4 Substrates for caspase-3 include the death substrate poly(ADP-ribose) polymerase (PARP), DNA-PK, actin, GAS2, and procaspase-6.5,6 The percentage of caspase-3-positive neurons is positively correlated with dopaminergic neuronal loss in the substantia nigra pars compacta of postmortem brains from patients with Parkinson’s disease, as well as several animal models of chronic neurodegenerative disorders.7 Cardiac levels of caspase-3 are increased in patients with ventricular arrhythmia, and activated caspase-3 is found in myocardium isolated from patients with end-stage heart failure.8 Cayman’s Caspase-3 Rabbit Monoclonal Antibody (Clone RM250) can be used for immunohistochemistry (IHC) and Western blot (WB) applications. The antibody recognizes the p17 subunit to detect caspase-3 in human samples.
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1. Apoptosis and cancer: Mutations within caspase genes. J. Med. Genet. 46(8), 497-510 (2009).
2. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-
3. Structural and kinetic analysis of caspase-
4. Caspases: Opening the boxes and interpreting the arrows. Cell Death Differ. 9(1), 3-5 (2002).
5. Yama/CPP32β, a mammalian homolog of CED-
6. Caspases and caspase inhibitors. Trends Biochem. Sci. 22(10), 388-393 (1997).
7. Caspase-
8. Caspase-