Widely used in enzymology, particularly as a substrate for studying trypsin-like proteases. Its structure mimics natural peptide bonds, allowing researchers to measure enzyme activity and inhibition kinetics. Commonly employed in colorimetric and fluorometric assays due to the ease of detecting product formation upon hydrolysis. Also utilized in the purification and characterization of serine proteases. Plays a role in drug development research by helping assess the efficacy of protease inhibitors. Frequently used in biochemical assays requiring high substrate specificity for arginine residues at the cleavage site.