Used extensively in biochemical assays to study protease enzyme activity, particularly for enzymes like thrombin, trypsin, and other serine proteases. The compound acts as a fluorogenic substrate—when the enzyme cleaves the AMC (7-amino-4-methylcoumarin) group from the peptide chain, a fluorescent signal is released that can be measured quantitatively. This allows researchers to monitor enzyme kinetics, inhibition, and activation in real time. Commonly employed in high-throughput screening for drug discovery, especially in developing anticoagulants and anti-inflammatory agents. Also used in cell-based assays to assess proteolytic activity in lysates or live cells. Its specificity makes it valuable for detecting subtle changes in enzyme function under various experimental conditions.