Ac-DNLD-AMC is a fluorogenic caspase-3 substrate. Upon enzymatic cleavage by caspase-3, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify caspase-3 activity. AMC displays excitation/emission maxima of 340-360 and 440-460 nm, respectively.
Z-(L-Arg)-AMC is a fluorogenic substrate for trypsin, cathepsin B, and cathepsin H.1,2Upon enzymatic cleavage by trypsin, cathepsin B, or cathepsin H, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify trypsin, cathepsin B, and cathepsin H activity. AMC displays excitation/emission maxima of 340-360/440-460 nm, respectively.
1.Zimmerman, M., Ashe, B., Yurewicz, E.C., et al.Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substratesAnal. Biochem.78(1)47-51(1977) 2.Brindley, P.J., Kalinna, B.H., Dalton, J.P., et al.Proteolytic degradation of host hemoglobin by schistosomesMol. Biochem. Parasitol.89(1)1-9(1997)
L-Leu-AMC is a fluorogenic substrate for leucine aminopeptidase.1Upon enzymatic cleavage by leucine aminopeptidase, AMC is released and its fluorescence can be used to quantify leucine aminopeptidase activity. AMC displays excitation/emission maxima of 340-360/440-460 nm, respectively.
1.Izquierdo, M., Lin, D., O’Neill, S., et al.Development of a high-throughput screening assay to identify inhibitors of the major M17-leucyl aminopeptidase from Trypanosoma cruzi using rapidfire mass spectrometrySLAS Discov.25(9)1064-1071(2020)