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Overview
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Background
Ac-VEID-AFC is a fluorogenic substrate of caspase-6 (Km=30μM; Kcat/Km=168000 M-1sec-1) and related cysteine proteases. The sequence is based on the lamin A site of cleavage. During apoptosis, caspase-6 cleaves the substrate and release AFC which then can be quantified by fluorescent detection at Ex/Em = 400/505. Ac-IETD-pNA can be used to identify and quantify caspase-6 activity in apoptotic cell lysates and to study events downstream of caspase-6 activation.
1. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis: N.A. Thornberry, et al.; J. Biol. Chem. 272, 17907 (1997)
2. Substrate specificities of caspase family proteases: R.V. Talanian, et al.; J. Biol. Chem. 272, 9677 (1997)
3. The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32: S.M. Srinivasula, et al.; J. Biol. Chem. 271, 27099 (1996)
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- Properties
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Overview