H-Thr-AMC (L-Threonine 7-amido-4-methylcoumarin) is a fluorogenic peptide substrate. It consists of the amino acid L-threonine (Thr) conjugated to the fluorophore 7-amino-4-methylcoumarin (AMC) via an amide bond. This compound is typically supplied as a trifluoroacetate salt to enhance solubility and stability. Its primary application is in biochemical and enzymatic assays, particularly for the detection and quantification of protease activity. The AMC group is fluorescent only upon cleavage from the peptide backbone. Therefore, H-Thr-AMC serves as a specific substrate for proteases like thrombin, which cleave after arginine residues in certain contexts, or other serine or cysteine proteases that recognize threonine or adjacent sequences. The increase in fluorescence intensity is directly proportional to the enzymatic activity, making it a valuable tool in high-throughput screening, enzyme kinetics studies, and diagnostic research. This substrate is a key reagent in life science research for studying blood coagulation pathways, apoptosis (caspase assays), and general proteolytic processes. It is handled as a light-sensitive compound and typically stored desiccated at -20°C.