Gly-Arg-AMC is a fluorogenic substrate for cathepsin C.1 Upon enzymatic cleavage by cathepsin C, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify cathepsin C activity. AMC displays excitation/emission maxima of 340-360/440-460 nm, respectively. |1. Rubach, J.K., Cui, G., Schneck, J.L., et al. The amino-acid substituents of dipeptide substrates of cathepsin C can determine the rate-limiting steps of catalysis. Biochemistry 51(38), 7551-7568 (2012).
Ac-RGK(Ac)-AMC, fluorogenic substrate for assaying histone deacetylase (HDAC) activity in a two-step enzymatic reaction. The assay consists of the initial lysine deacetylation by HDAC followed by the release of the fluorescent group by trypsin.
Boc-Ile-Glu-Gly-Arg-AMC (IEGR-AMC) is a specific, highly fluorogenic substrate for clotting enzyme factor Xa (coagulation factor Xa) and is also hydrolyzed by acrosin from the ascidian Halocynthia roretzi.
Z-Gly-Gly-Arg-AMC acetate is a thrombase-specific fluorescent matrix used to detect thrombin production in platelet-rich plasma (PRP) and poor platelet plasma (PPP).
Z-Gly-Gly-Arg-AMC is a specific fluorogenic substrate utilized for assessing thrombin generation in Platelet-Rich Plasma (PRP) and Platelet-Poor Plasma (PPP), with a particular focus on thrombin activity.