Leu-AMC HCl is a fluorogenic substrate for LAP3 (leucine aminopeptidase). Upon enzyme activity, a bright blue fluorescent dye, 7-amino-4-methylcoumarin, is released.
CAT No: R1916
CAS No:62480-44-8
Synonyms/Alias:62480-44-8;L-Leucine-7-amido-4-methylcoumarin hydrochloride;H-L-LEU-AMC HCL;L-Leucine 7-amido-4-methylcoumarin hydrochloride;(S)-2-amino-4-methyl-N-(4-methyl-2-oxo-2H-chromen-7-yl)pentanamide hydrochloride;(2S)-2-amino-4-methyl-N-(4-methyl-2-oxochromen-7-yl)pentanamide;hydrochloride;L-Leucine 7-amido-4-methylcoumarin hydrochloride salt;L-Leucine-7-amido-4-methylcoumarin (hydrochloride);Pentanamide,2-amino-4-methyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-,monohydrochloride, (2S)-;Leu-AMC;L-Leu-AMC (hydrochloride);L-Leucine-AMC.HCl;L-Leucin-7-amido-4-methylcoumarin-hydrochlorid;(2S)-2-amino-4-methyl-N-(4-methyl-2-oxo-chromen-7-yl)pentanamide Hydrochloride;MFCD00043262;L-Leu-AMC·HCl;H-L-Leu-amc hydrochloride;SCHEMBL381193;AKOS025295556;EL15997;AS-74553;HY-137844;CS-0142346;E78667;Leucine-7-amido-4-methylcoumarine hydrochloride;L-Leucine-7-amido-4-methylcoumarin hydrochloride;L-Leucine-7-amido-4-methylcouramin hydrochloride salt;(2S)-2-amino-4-methyl-N-(4-methyl-2-oxo-2H-chromen-7-yl)pentanamide hydrochloride;(S)-2-Amino-4-methyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-pentanamide Monohydrochloride; (2S)-2-Amino-4-methyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-pentanamide Monohydrochloride;;Pentanamide,2-amino-4-methyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-,monohydrochloride,(2S)-(9ci);
Chemical Name:(2S)-2-amino-4-methyl-N-(4-methyl-2-oxochromen-7-yl)pentanamide;hydrochloride
Leu-AMC HCl, also known as L-Leucine 7-amido-4-methylcoumarin hydrochloride, is a synthetic peptide substrate widely utilized in biochemical research, particularly in the study of protease activity. It consists of the amino acid leucine covalently linked to the fluorogenic moiety 7-amido-4-methylcoumarin (AMC), forming a molecule that emits fluorescence upon enzymatic cleavage. This property makes it a valuable tool for monitoring enzymatic reactions in real time, enabling precise quantification of proteolytic activity in complex biological samples. Its high specificity and sensitivity have established it as a standard substrate in enzymology, cell biology, and drug discovery workflows.
Enzyme Activity Assays: Leu-AMC HCl is frequently employed in the quantitative measurement of protease activity, especially for enzymes such as leucine aminopeptidase, trypsin, and related serine and cysteine proteases. Upon enzymatic hydrolysis, the AMC group is released, generating a fluorescent signal directly proportional to protease activity. This feature allows researchers to conduct kinetic analyses, determine enzyme specificity, and compare the efficacy of various protease preparations under controlled conditions. The use of this substrate streamlines high-throughput screening and facilitates the development of sensitive, reproducible assays for basic and applied research.
Inhibitor Screening: The substrate's fluorogenic properties make it particularly suitable for evaluating the potency of protease inhibitors in vitro. By monitoring the reduction in fluorescence signal in the presence of candidate compounds, scientists can efficiently assess inhibitor efficacy, determine IC50 values, and characterize inhibition mechanisms. This application is integral to pharmaceutical research, where identifying and optimizing protease inhibitors is critical for therapeutic target validation and lead compound selection.
Cellular Proteolysis Studies: Leu-AMC HCl serves as a functional probe for examining intracellular and extracellular protease activity in cell-based systems. Researchers can use it to monitor changes in proteolytic profiles in response to genetic modifications, environmental stimuli, or pharmacological interventions. The real-time detection of fluorescence enables dynamic studies of protease function, regulation, and localization within living cells or tissue extracts, providing insights into fundamental biological processes such as protein turnover, signal transduction, and apoptosis.
Biochemical Characterization: The compound is also valuable in the detailed characterization of novel proteases, including determination of substrate specificity, catalytic efficiency, and kinetic parameters such as Km and Vmax. By systematically varying substrate concentration and analyzing the resulting fluorescence, enzymologists can elucidate enzyme mechanisms and compare the properties of wild-type and mutant enzymes. This information supports protein engineering, functional annotation, and the exploration of enzyme evolution.
Analytical Method Development: Leu-AMC HCl is utilized in the optimization and validation of analytical protocols for protease quantification in complex matrices, such as biological fluids, cell lysates, or pharmaceutical formulations. Its robust and sensitive fluorescence readout enables the development of standardized, scalable methods compatible with microplate readers and automated platforms. These protocols are essential for quality control, biomarker discovery, and the assessment of protease-related processes in a variety of research and industrial settings.
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