Pyr-Arg-Thr-Lys-Arg-AMC TFA combines a pyroglutamate cap, basic residues, and a fluorogenic AMC group for sensitive cleavage detection. Charged side chains assist solubility and enzyme recognition. Researchers analyze its kinetics to characterize protease activity. Use spans fluorescence-based assays, substrate evaluation, and mechanistic profiling.
CAT No: R2436
CAS No:1255501-99-5
Synonyms/Alias:1255501-99-5;Pyr-Arg-Thr-Lys-Arg-AMC TFA;Pyr-Arg-Thr-Lys-Arg-AMC (TFA);Pyr-Arg-Thr-Lys-Arg-AMC trifluoroacetate;(2S)-N-[(2S)-1-[[(2S,3R)-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]-3-hydroxy-1-oxobutan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]-5-oxopyrrolidine-2-carboxamide;2,2,2-trifluoroacetic acid;HY-P4349A;MFCD17215945;L-Pyroglutamyl-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin trifluoroacetate salt;Pyr-Arg-Thr-Lys-Arg-AMCtrifluoroacetate;DA-57259;CS-0693663;pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin trifluoroacetate salt, >=96% (HPLC);
Pyr-Arg-Thr-Lys-Arg-AMC TFA, also known as a fluorogenic peptide substrate, is a synthetic compound designed for sensitive detection of protease activity in biochemical and molecular biology research. Featuring a unique sequence capped with the 7-amino-4-methylcoumarin (AMC) fluorophore, this substrate enables real-time monitoring of enzymatic cleavage events through robust fluorescence signals. The trifluoroacetic acid (TFA) salt form ensures enhanced solubility and stability, making it particularly suitable for in vitro assays and high-throughput screening applications. Its tailored peptide sequence enables specificity for certain proteases, facilitating detailed studies of enzyme kinetics, substrate specificity, and inhibitor screening in a variety of research settings.
Protease Activity Assays: Pyr-Arg-Thr-Lys-Arg-AMC TFA is widely employed in the quantitative analysis of protease activity, particularly for enzymes that recognize and cleave after basic amino acid residues. By incorporating the AMC fluorophore at the C-terminus, the substrate releases a fluorescent signal upon enzymatic cleavage, allowing researchers to monitor proteolytic reactions in real time. This sensitive detection method is instrumental in characterizing enzyme kinetics, comparing protease activity across different samples, and optimizing assay conditions for both academic and industrial research environments.
Enzyme Inhibitor Screening: The fluorogenic nature of this peptide substrate makes it an ideal tool for high-throughput screening of protease inhibitors. By measuring changes in fluorescence intensity, scientists can rapidly evaluate the efficacy of potential inhibitory compounds in blocking protease-mediated substrate cleavage. This approach accelerates the identification and optimization of lead compounds in drug discovery pipelines, providing a robust and reproducible platform for assessing inhibitor potency and selectivity under various experimental conditions.
Biochemical Pathway Elucidation: Pyr-Arg-Thr-Lys-Arg-AMC TFA serves as a valuable probe for dissecting complex proteolytic pathways within biological samples. Its selective recognition by specific proteases enables researchers to map enzyme-substrate interactions and unravel regulatory mechanisms governing protease-mediated processes. By integrating this substrate into cell lysate or tissue extract assays, it becomes possible to investigate the roles of individual enzymes in physiological or pathological contexts, paving the way for deeper insights into cellular signaling and homeostasis.
Enzyme Engineering and Specificity Studies: The defined sequence and fluorogenic properties of this peptide substrate support detailed studies of protease substrate specificity and the engineering of novel enzyme variants. Researchers can utilize it to assess the impact of amino acid substitutions within the substrate or enzyme, enabling rational design of proteases with altered selectivity or enhanced catalytic efficiency. These investigations contribute to the development of tailored enzymes for biotechnological, diagnostic, or therapeutic applications, expanding the utility of protease-based technologies.
Quality Control in Bioprocessing: In the context of biomanufacturing and protein production, Pyr-Arg-Thr-Lys-Arg-AMC TFA is employed to monitor unwanted protease activity that may compromise product integrity. By incorporating the substrate into quality control workflows, manufacturers can detect and quantify residual protease contaminants, ensuring the consistency and stability of recombinant protein products. This proactive approach aids in troubleshooting process deviations, optimizing purification protocols, and maintaining the high standards required for advanced biotechnological applications.
Fluorogenic peptide substrates such as Pyr-Arg-Thr-Lys-Arg-AMC TFA continue to play a pivotal role in advancing enzymology, molecular biology, and bioprocessing research. Their ability to provide rapid, sensitive, and quantitative readouts of protease activity underpins a wide array of scientific investigations, from fundamental studies of enzyme mechanisms to applied research in drug discovery and biotechnology. As research demands evolve, the versatility and reliability of this substrate support ongoing innovation in protease-related fields, reinforcing its value as an indispensable tool for academic and industrial laboratories alike.
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