H-Gly-Arg-AMC links a minimal dipeptide recognition element to an AMC fluorophore, forming a sensitive substrate for trypsin-like proteases. The arginine residue defines cleavage specificity, while glycine provides flexibility. Researchers quantify fluorescence increase to monitor catalytic turnover. Applications include high-throughput screening, kinetic analysis, and protease-mechanism research.
CAT No: R2570
CAS No:65147-19-5
Synonyms/Alias:H-Gly-Arg-AMC;Gly-Arg-AMC;65147-19-5;(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)-N-(4-methyl-2-oxochromen-7-yl)pentanamide;Gly-Arg-7-Amino-4-Methylcoumarin;glycyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-argininamide, hydrochloride;70274-78-1;(S)-2-(2-Aminoacetamido)-5-guanidino-N-(4-methyl-2-oxo-2H-chromen-7-yl)pentanamide;H-Gly-Arg-AMC hydrochloride salt;Gly-Arg-AMC (hydrochloride);CHEMBL65584;SCHEMBL7574189;HY-P4342;FG110503;CS-0653705;(2S)-2-[(2-aminoacetyl)amino]-5-guanidino-N-(4-methyl-2-oxo-chromen-7-yl)pentanamide;
H-Gly-Arg-AMC, also known as Glycyl-Arginyl-7-amido-4-methylcoumarin, is a synthetic fluorogenic peptide substrate widely utilized in biochemical and molecular biology research. Featuring a peptide sequence conjugated to the AMC (7-amido-4-methylcoumarin) fluorophore, this compound enables sensitive detection of protease activity through fluorescence emission upon enzymatic cleavage. Its design allows for highly specific monitoring of enzyme-substrate interactions, providing researchers with a powerful tool for kinetic studies and functional assays. The substrate's stability in aqueous solutions and its compatibility with a range of assay conditions make it a versatile choice for laboratories investigating proteolytic processes.
Enzyme Activity Assays: H-Gly-Arg-AMC serves as an essential substrate for quantifying the activity of serine proteases, particularly trypsin-like enzymes, in vitro. Upon cleavage by target proteases, the AMC moiety is released, resulting in a measurable increase in fluorescence intensity. This property enables researchers to perform continuous or endpoint assays to monitor enzyme kinetics, inhibitor screening, and substrate specificity under various experimental conditions. The high sensitivity and real-time detection capabilities provided by this substrate facilitate detailed mechanistic studies of protease function and regulation.
Drug Discovery Research: Gly-Arg-AMC is frequently employed in high-throughput screening platforms designed to identify novel protease inhibitors. Its robust fluorescent signal allows for rapid evaluation of compound libraries, supporting the discovery and optimization of small molecules that modulate protease activity. By offering a reliable readout of enzymatic inhibition, the substrate accelerates the lead identification process and aids in the characterization of inhibitor potency and selectivity, which are crucial for the development of targeted therapeutics.
Biochemical Characterization: The substrate is instrumental in characterizing the enzymatic properties of newly discovered or engineered proteases. Researchers utilize Glycyl-Arginyl-AMC to determine substrate preferences, catalytic efficiency, and the influence of cofactors or mutations on enzyme performance. Its fluorogenic nature allows for precise quantification of reaction rates and detailed comparison of enzyme variants, supporting protein engineering efforts and the elucidation of structure-function relationships in proteolytic enzymes.
Cellular and Molecular Biology: In cellular assays, Gly-Arg-AMC is used to monitor protease activity in cell lysates or tissue extracts, providing insights into physiological and pathological processes involving proteolysis. The substrate's compatibility with various buffer systems and detection platforms ensures its utility in diverse experimental setups, including microplate-based assays and flow cytometry. By enabling the assessment of protease function in complex biological samples, it contributes to studies on cell signaling, apoptosis, and protein turnover.
Educational and Training Applications: The straightforward and visually demonstrable nature of the fluorescence-based assay using H-Gly-Arg-AMC makes it a valuable tool for teaching laboratory techniques in enzymology and molecular biology. Students and trainees can gain hands-on experience with kinetic measurements, data analysis, and assay optimization, fostering a deeper understanding of enzyme-substrate interactions and the principles of fluorescence detection. Its use in educational settings supports practical learning and the development of essential laboratory skills in the next generation of researchers.
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