Z-Arg-Arg-7-Amido-4-methylcoumarin hydrochloride is a coumarin-labeled dipeptide substrate suited for monitoring protease activity with high fluorescence sensitivity. The arginine-rich sequence enhances recognition by trypsin-like enzymes. Researchers apply it in kinetic profiling and inhibitor evaluation. The Cbz protection ensures synthetic stability and predictable cleavage behavior.
CAT No: R2283
CAS No:136132-67-7
Synonyms/Alias:136132-67-7;Z-Arg-Arg-7-amido-4-methylcoumarin hydrochloride;Z-Arg-Arg-Amc Hydrochloride salt;Z-Arg-Arg-AMC hydrochloride;Z-Arg-Arg-AMC (hydrochloride);MFCD00133576;N-alpha-cbz-arg-arg7-amido-4-methylcoumarinhydrochloride;benzyl N-[(2S)-5-(diaminomethylideneamino)-1-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]carbamate;hydrochloride;Z-RR-AMC;DA-59250;DA-65922;HY-134434;CS-0142223;G85391;634-364-2;benzyl (S)-5-guanidino-1-((S)-5-guanidino-1-(4-methyl-2-oxo-2H-chromen-7-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate hydrochloride;L-Argininamide,n2-[(phenylmethoxy)carbonyl]-L-arginyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-,monohydrochloride(9ci);
Z-Arg-Arg-7-Amido-4-methylcoumarin hydrochloride is a synthetic peptide substrate widely utilized in biochemical and molecular biology research. Structurally, it comprises a dipeptide sequence (arginine-arginine) conjugated to a 7-amido-4-methylcoumarin fluorophore, and is typically supplied as a hydrochloride salt for enhanced solubility and stability. The substrate is specifically designed for the sensitive detection and quantification of proteolytic enzyme activity, particularly those enzymes with trypsin-like or arginine-specific cleavage preferences. Its unique combination of peptide sequence and fluorogenic tag makes it a valuable reagent for kinetic studies, enzyme characterization, and high-throughput screening in academic, pharmaceutical, and industrial settings.
Enzyme Activity Assays: As a fluorogenic peptide substrate, Z-Arg-Arg-7-Amido-4-methylcoumarin hydrochloride is extensively employed in the measurement of serine protease activity, especially for enzymes such as trypsin, thrombin, and certain kallikreins. Upon enzymatic cleavage at the arginine-arginine bond, the highly fluorescent 7-amido-4-methylcoumarin moiety is released, enabling real-time, quantitative monitoring of protease activity. This property supports detailed kinetic analyses, enzyme profiling, and comparative studies of protease specificity under various experimental conditions.
High-Throughput Screening: The compound's robust fluorescent signal upon enzymatic hydrolysis makes it ideally suited for high-throughput screening (HTS) applications in drug discovery and inhibitor development. Researchers can leverage its rapid and sensitive readout to evaluate large compound libraries for modulators of protease function, facilitating the identification of novel enzyme inhibitors or activators. The substrate's compatibility with microplate-based fluorescence assays enhances assay throughput and reproducibility, which are critical for pharmaceutical lead optimization and biochemical target validation.
Protease Specificity Studies: Z-Arg-Arg-7-Amido-4-methylcoumarin hydrochloride serves as a precise tool for dissecting the substrate specificity of arginine-preferring proteases. By systematically varying assay conditions or comparing different enzyme isoforms, scientists can investigate the molecular determinants of substrate recognition and cleavage efficiency. These studies provide valuable insights into protease function, regulation, and potential physiological roles, contributing to a deeper understanding of proteolytic pathways in biological systems.
Biochemical Pathway Analysis: The substrate is a valuable reagent for elucidating protease-driven pathways in cell and tissue extracts. By monitoring the generation of the fluorescent product in complex biological samples, researchers can assess endogenous protease activities, profile changes in response to stimuli, or evaluate the impact of genetic or pharmacological interventions. This approach supports the mapping of proteolytic cascades and the identification of key regulatory nodes in physiological and pathological contexts.
Analytical Validation and Instrument Calibration: In addition to its use in biological assays, Z-Arg-Arg-7-Amido-4-methylcoumarin hydrochloride is frequently employed for the calibration and validation of fluorescence-based analytical instruments. Its well-characterized fluorescence properties and predictable enzymatic release profile make it a reliable standard for optimizing assay sensitivity, linearity, and dynamic range in spectrofluorometers, microplate readers, and related platforms. Such calibration procedures ensure the accuracy and reproducibility of quantitative measurements in diverse experimental workflows.
4. Myotropic activity of allatostatins in tenebrionid beetles
5. C-Peptide replacement therapy and sensory nerve function in type 1 diabetic neuropathy
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