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Antigen:
human caspase-3 amino acids 166-183 (TELDSGIETDSGVDDDMA)
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Host:
rabbit
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Application(s):
WB and IHC; other applications not tested
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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
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1
Wolf, B.B., 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., Earnshaw, W.C. Caspases and caspase inhibitors. Trends Biochem Sci 22 388-393 (1997).
3
Fernandes-Alnemri, T., Litwack, G., 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).
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