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Western blot analysis of Jurkat cell extracts untreated or treated with cytochrome c in vitro, showing full length and/or cleaved caspase-3 (upper) and cleaved caspase-3 Asp175 (lower), using Caspase-3 Antibody #9662 and Cleaved Caspase-3 (Asp175) Antibody #9661.

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Product Description

Untreated Jurkat Control Cell Extracts: Untreated Jurkat cells are lysed in Chaps cell extract buffer and a cytoplasmic fraction is generated to serve as a negative control for caspase cleavage. Cytochrome c Treated Jurkat Cell Extracts: Untreated Jurkat cells are lysed in Chaps cell extract buffer and a cytoplasmic fraction is generated. Extracts are then treated with cytochrome c in vitro to generate a positive control for caspase cleavage.


Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).


1.  Fernandes-Alnemri, T. et al. (1994) J Biol Chem 269, 30761-4.

2.  Nicholson, D.W. et al. (1995) Nature 376, 37-43.



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