Antigen: recombinant full-length human caspase-3 · Clone designation: 31A1067 · Host: mouse · Isotype: IgG1κ · Application(s): IHC (frozen and paraffin-embedded sections) and WB · Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis.¹ The precursor form of all caspases is composed of a prodomain and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation, and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into a tetramer to form the active enzyme. The gene for caspase-3 also known as Yama, CPP32, and apopain codes for a 32 kDa protein.^2,3,4 Caspase-3 cleaves the death substrate poly(ADP-ribose) polymerase (PARP) to a specific 85 kDa form observed during apoptosis and is inhibitable by the CrmA protein. Other caspase-3 substrates include DNA-PK, actin, GAS2, and pro-caspase-6.⁵ Caspase-3 is activated by cleavage events at Asp28/Ser²⁹ (between N-terminal pro-domain) and Asp175/Ser¹⁷⁶ (between large and small subunits) to generate a large subunit of 17 kDa and a small subunit of 12 kDa.³

1 Cohen, G.M. Caspases: The executioners of apoptosis. Biochem J 326 1-16 (1997).

2 Fernandes-Alnemri, T., Litwack, G., and Alnemri, E.S. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1β-converting enzyme. J Biol Chem 269 30761-30764 (1994).

3 Tewari, M., Quan, L.T., O'Rourke, K., et al. Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81 801-809 (1995).

4 Shi, L., Chen, G., Macdonald, G., et al. Activation of an interleukin 1 converting enzyme-dependent apoptosis pathway by granzyme B. Proc Natl Acad Sci USA 93 11002-11007 (1996).

5 Villa, P., Kaufman, S.H., and Earnshaw, W.C. Caspases and caspase inhibitors. Trends Biochem Sci 22 388-393 (1997).

Villa, P., Kaufman, S.H., and Earnshaw, W.C. Caspases and caspase inhibitors. Trends Biochem Sci 22 388-393 (1997).

Shi, L., Chen, G., Macdonald, G., et al. Activation of an interleukin 1 converting enzyme-dependent apoptosis pathway by granzyme B. Proc Natl Acad Sci USA 93 11002-11007 (1996).

Tewari, M., Quan, L.T., O'Rourke, K., et al. Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81 801-809 (1995).

Fernandes-Alnemri, T., Litwack, G., and Alnemri, E.S. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1β-converting enzyme. J Biol Chem 269 30761-30764 (1994).

Cohen, G.M. Caspases: The executioners of apoptosis. Biochem J 326 1-16 (1997).

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