Antigen: human caspase-3 amino acids 166-183 (TELDSGIETDSGVDDDMA) · Host: rabbit · Application(s): WB and IHC; other applications not tested · Apoptosis is associated with 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. Caspase-3 (CPP32, Yama, Apopain, ICE3) is a key effector caspase in the apoptosis cascade.^1,2 The enzyme is efficiently activated by caspase-8, caspase-9, and granzyme B resulting in 17 and 12 kDa active subunits formed from the 34 kDa proenzyme.^3,1 The substrates of caspase-3 are numerous and include pro- and anti-apoptotic proteins, downstream components of the apoptotic machinery (for example, ICAD), as well as structural and homeostatic proteins.^1,2 DNA fragmentation and the morphological changes associated with this final stage of apoptosis appears to be dependent upon caspase-3.⁴ Caspase-3 is expressed in a variety of tissues and cells.^3,5

1 Wolf, B.B., and Green, D.R. Suicidal tendencies: Apoptotic cell death by caspase family proteinases. J Biol Chem 274 20049-20052 (1999).

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

3 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).

4 Jänicke, R.U., Sprengart, M.L., Wati, M.R., et al. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J Biol Chem 273 9357-9360 (1998).

5 Juan, T.S., McNiece, I.K., Jenkins, N.A., et al. Molecular characterization of mouse and rat CPP32β gene encoding a cysteine protease resembling interleukin-1β converting enzyme and CED-3. Oncogene 13 749-755 (1996).

Jänicke, R.U., Sprengart, M.L., Wati, M.R., et al. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J Biol Chem 273 9357-9360 (1998).

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

Juan, T.S., McNiece, I.K., Jenkins, N.A., et al. Molecular characterization of mouse and rat CPP32β gene encoding a cysteine protease resembling interleukin-1β converting enzyme and CED-3. Oncogene 13 749-755 (1996).

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).

Wolf, B.B., and Green, D.R. Suicidal tendencies: Apoptotic cell death by caspase family proteinases. J Biol Chem 274 20049-20052 (1999).

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