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 is a synthetic peptide substrate featuring a 7-amino-4-methylcoumarin (AMC) fluorogenic label and a trifluoroacetic acid (TFA) salt form. This pentapeptide sequence is engineered for high specificity in protease activity assays, particularly for enzymes that recognize basic amino acid residues such as arginine and lysine. The presence of the AMC group allows for sensitive detection of enzymatic cleavage events via fluorescence, making the compound a valuable tool in biochemical research focused on protease characterization, inhibitor screening, and enzymatic pathway elucidation. Its defined sequence and robust labeling make it a preferred choice for laboratories seeking reliable and reproducible results in peptide-based assay systems.
Protease activity assays: Pyr-Arg-Thr-Lys-Arg-AMC TFA is widely employed as a fluorogenic substrate in the quantitative analysis of serine and cysteine proteases, especially those with trypsin-like specificity. Upon enzymatic cleavage at the C-terminal arginine, the AMC moiety is released, resulting in a measurable fluorescence signal. This property enables researchers to monitor protease kinetics in real time, assess substrate specificity, and determine catalytic parameters such as Km and Vmax under various experimental conditions. The substrate's design ensures minimal background fluorescence, facilitating precise detection even in complex biological samples.
Enzyme inhibitor screening: The peptide's sensitivity to proteolytic cleavage makes it an ideal substrate for high-throughput screening of protease inhibitors. By incorporating Pyr-Arg-Thr-Lys-Arg-AMC TFA into microplate assays, researchers can rapidly evaluate the potency and selectivity of novel inhibitor compounds based on their ability to reduce AMC fluorescence release. This approach is crucial for drug discovery programs aimed at targeting dysregulated protease activity in diverse biological processes, as well as for validating the specificity of candidate molecules prior to more advanced studies.
Substrate specificity profiling: The defined sequence of this fluorogenic peptide allows for detailed mapping of protease substrate preferences. By comparing cleavage efficiency across different enzyme isoforms or mutant variants, scientists can elucidate the structural determinants governing substrate recognition and catalysis. Such studies are fundamental to understanding protease function in physiological and pathological contexts, and they inform the rational design of custom substrates or selective inhibitors for specialized research applications.
Cell-free biochemical pathway analysis: In vitro systems utilizing Pyr-Arg-Thr-Lys-Arg-AMC TFA enable the dissection of proteolytic pathways outside of cellular environments. The substrate's amenability to real-time fluorescence detection supports the reconstruction of enzymatic cascades, evaluation of cofactor dependencies, and investigation of post-translational modifications that influence protease activity. This facilitates mechanistic studies that would be challenging to perform in vivo, providing valuable insights into the regulation of proteolysis at the molecular level.
Analytical method development: The robust fluorescent response of the AMC label upon peptide cleavage is leveraged in the optimization and validation of analytical protocols for protease quantification. Laboratories can use the substrate to calibrate fluorometric instruments, standardize assay conditions, and establish quality control benchmarks for routine protease monitoring. The reproducibility and sensitivity of the substrate's response make it a reliable reference material for developing new analytical techniques or adapting existing workflows to novel research questions.
1. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
4. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
5. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More