l-arg

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)

Z-Val-Val-Arg-AMC serves as a fluorescent peptide substrate utilized for assessing the activity of cathepsins [1].

Evans blue (C.I. 23860) is an effective inhibitor of glutamate uptake by synaptic vesicles and also acts as an antagonist of AMPA/kainate receptors. As an azo dye, Evans blue binds to serum albumin, enabling detection of blood-brain barrier integrity and permeability.

Mca-RPPGFSAFK(Dnp)-OH, a fluorogenic substrate specifically designed for endothelin-converting enzyme-1 (ECE-1), enables the quantification of ECE-1 activity through its distinctive fluorescence signal. When ECE-1 cleaves this substrate, it releases 7-methoxycoumarin-4-acetyl (Mca), which exhibits excitation and emission maxima at 328 nm and 420 nm, respectively, allowing for the direct measurement of enzyme activity.

Mca-KPLGL-Dap(Dnp)-AR-NH2 serves as a fluorogenic substrate specifically designed for matrix metalloproteinases (MMPs). This compound facilitates the quantification of MMP activity by releasing 7-methoxycoumarin-4-acetyl (Mca) upon enzymatic cleavage by MMPs, which exhibits fluorescence with excitation and emission maxima at 328 nm and 420 nm, respectively.