Used as a fluorogenic substrate in enzymatic assays, particularly for detecting protease activity. The compound is cleaved by target proteases, releasing the fluorescent 7-amino-4-methylcoumarin group, which emits measurable fluorescence upon excitation. This makes it valuable in high-throughput screening, drug discovery, and biochemical studies where real-time monitoring of enzyme kinetics is required. Commonly applied in assays involving trypsin-like proteases due to the arginine residue at the cleavage site. The Boc-protected tripeptide structure ensures specificity and stability prior to enzymatic reaction.