Widely used in biochemical and enzymatic assays as a fluorogenic substrate. It is particularly valuable in the study of protease enzyme activity, where cleavage of the amide bond releases the fluorescent 7-amino-4-methylcoumarin (AMC) group. This release allows real-time monitoring of enzyme kinetics by measuring fluorescence intensity. Commonly employed in assays for caspases, cathepsins, and other hydrolases involved in cellular signaling and apoptosis. Its high sensitivity and low background fluorescence make it ideal for high-throughput screening in drug discovery and diagnostic applications. Also used in research settings to evaluate enzyme inhibition and to detect proteolytic activity in cell lysates or purified enzyme preparations.