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Members of the ICE/CED-3 cysteine protease family have key roles in inflammation and mammalian apoptosis. The ICE family member Caspase-3 (also known as CPP32, Yama, apopain) is activated early in apoptosis and appears to be involved in the proteolysis of several important molecules, including poly (ADP ribose) polymerase (PARP). Activated Caspase-3 cleaves PARP from its 116 kD to an 85 kD residual fragment. The cleavage site in PARP is C-terminal to Asp-216. The upstream sequence of the cleavage site, DEVD (Asp-Glu-Val-Asp), is utilized as a basis for the highly specific Caspase-3 substrate, Ac-DEVD-AMC and Caspase-3 inhibitor, Ac-DEVD-CHO.
Ac-DEVD-CHO is a synthetic tetrapeptide inhibitor for Caspase-3 (CPP32) and contains the amino acid sequence of the PARP cleavage site. The tetrapeptide inhibitor can be used to identify and quantify the Caspase-3 activity in apoptotic cells, and to study events downstream of Caspase-3 activation.
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