Boc-Leu-Lys-Arg-AMC Hydrochloride Salt combines a protected tripeptide with an AMC fluorophore for trypsin-like protease assays. Leucine provides hydrophobic contacts, while lysine and arginine define strong basic recognition features. The hydrochloride salt enhances aqueous solubility and handling. Researchers monitor fluorescence release to characterize catalytic efficiency, specificity, and inhibitor potency.
CAT No: R2605
CAS No:109358-47-6
Synonyms/Alias:109358-47-6;Boc-Leu-Lys-Arg-AMC;BOC-LEU-LYS-ARG-AMC HYDROCHLORIDE SALT;Boc-Leu-Lys-Arg-Mca;tert-butyl N-[(2S)-1-[[(2S)-6-amino-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]carbamate;CHEMBL3142582;DTXSID401111490;HY-P4312;DA-51302;FB110554;CS-0653485;N-[(1,1-Dimethylethoxy)carbonyl]-L-leucyl-L-lysyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-argininamide;tert-butyl ((S)-1-(((S)-6-amino-1-(((S)-5-guanidino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxopentan-2-yl)amino)-1-oxohexan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)carbamate;tert-butyl (S)-1-((S)-6-amino-1-((S)-5-guanidino-1-(4-methyl-2-oxo-2H-chromen-7-ylamino)-1-oxopentan-2-ylamino)-1-oxohexan-2-ylamino)-4-methyl-1-oxopentan-2-ylcarbamate;TERT-BUTYL N-[(1S)-1-{[(1S)-5-AMINO-1-{[(1S)-4-CARBAMIMIDAMIDO-1-[(4-METHYL-2-OXOCHROMEN-7-YL)CARBAMOYL]BUTYL]CARBAMOYL}PENTYL]CARBAMOYL}-3-METHYLBUTYL]CARBAMATE;
Boc-leu-lys-arg-amc hydrochloride salt is a synthetic peptide substrate widely utilized in biochemical and molecular biology research. As a fluorogenic tripeptide conjugated to 7-amino-4-methylcoumarin (AMC), this compound is engineered for high sensitivity in enzymatic assays, particularly those involving protease activity. The presence of the N-terminal tert-butyloxycarbonyl (Boc) group and the C-terminal AMC moiety enables selective detection and quantification of proteolytic cleavage events. Its unique structure makes it a valuable tool for researchers investigating the specificity and kinetics of proteases, as well as for applications requiring robust fluorescence-based readouts.
Enzyme substrate assays: Boc-leu-lys-arg-amc hydrochloride salt serves as a reliable fluorogenic substrate for serine protease activity studies, including those targeting trypsin-like and related enzymes. Upon enzymatic cleavage at the appropriate peptide bond, the AMC group is released, producing a measurable fluorescent signal. This property allows for precise monitoring of protease kinetics, substrate specificity, and inhibitor screening in a variety of in vitro settings. The compound's design ensures minimal background fluorescence and high sensitivity, facilitating quantitative analysis in both endpoint and continuous assays.
High-throughput screening: The fluorogenic nature of this peptide substrate makes it exceptionally well-suited for high-throughput screening (HTS) platforms. Researchers and pharmaceutical scientists utilize it to rapidly evaluate large compound libraries for potential protease inhibitors or modulators. The robust fluorescence response generated upon enzymatic cleavage enables automated detection and data acquisition, supporting efficient lead identification in drug discovery workflows. Its compatibility with microplate readers and automation systems further enhances throughput and reproducibility.
Enzyme kinetics characterization: Detailed kinetic studies of proteases often require substrates that provide real-time, quantifiable outputs. The AMC-conjugated tripeptide structure of this compound allows for continuous monitoring of reaction rates, enabling researchers to calculate key parameters such as Km and Vmax with high accuracy. Such kinetic profiling is essential for elucidating enzyme mechanisms, comparing isoenzyme activity, and optimizing assay conditions in both academic and industrial laboratories.
Protease specificity profiling: Understanding the substrate preferences of proteases is crucial for both basic and applied research. By employing this fluorogenic peptide substrate in specificity assays, scientists can systematically evaluate the cleavage efficiency of various proteases, including engineered or mutant forms. The tripeptide sequence provides a defined recognition motif, allowing for comparative studies that inform substrate design, inhibitor development, and functional annotation of protease families.
Biochemical method development: The versatility of Boc-leu-lys-arg-amc hydrochloride salt extends to the development and optimization of novel biochemical assays. Its well-characterized cleavage mechanism and predictable fluorescence output make it a preferred choice for validating new assay formats, calibrating detection systems, and benchmarking assay performance. Method developers in academic, biotechnology, and pharmaceutical settings leverage its reliability to establish robust protocols for protease detection and quantification, ensuring reproducible results across diverse experimental platforms.
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