AMC (7-amino-4-methylcoumarin)-derived caspase substrates are widely used for the fluorimetric detection of various caspase activities. Cleavage of AMC peptides by caspases generates strongly fluorescent AMC that is monitored fluorimetrically at 440-460 nm with excitation of 340-350 nm. Caspase-3 substrate with Km = 9.7 µM; Caspase-7 substrate with Km = 11 µM
Koeplinger KA, et al. (2000). Caspase 8: an efficient method for large-scale autoactivation of recombinant procaspase 8 by matrix adsorption and characterization of the active enzyme. Protein Expr Purif 18, 378-87; Garcia-Calvo M, et al. (1998). Inhibition of human caspases by peptide-based and macromolecular inhibitors. J Biol Chem 273, 32608-13; Thornberry NA, et al. (1997). A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem 272, 17907-11; Rano TA, et al. (1997). A combinatorial approach for determining protease specificities: application to interleukin-1 beta converting enzyme (ICE). Chem Biol 4, 149-55; Margolin N, et al. (1997). Substrate and inhibitor specificity of interleukin-1 ?-converting enzyme and related caspases. J Biol Chem 272, 7223-8; Mizushima N, et al. (1996). Ceramide induces apoptosis via CPP32 activation. FEBS Lett 395, 267-71; Faubion WA, et al. (1999). Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas. J Clin Invest 103, 137-45.