Z-Arg-Arg-βNA acetate features a protected di-arginine motif linked to a β-naphthylamide reporter for chromogenic protease assays. The cationic pair enhances recognition by trypsin-like enzymes. Researchers quantify β-naphthylamine release to assess catalytic rates. Applications include enzyme profiling, substrate optimization, and mechanistic analysis.
CAT No: R2595
CAS No:2237216-27-0
Synonyms/Alias:Z-Arg-Arg-|ANA (acetate);Z-Arg-Arg-betaNA;Z-Arg-Arg-|ANA acetate salt;EX-A9235;HY-158307;CS-1051742;2237216-27-0;
Z-Arg-Arg-βNA acetate is a synthetic peptide substrate widely utilized in biochemical and enzymological research. Structurally, it consists of a benzyloxycarbonyl (Z) protected dipeptide, arginyl-arginine, conjugated to β-naphthylamide (βNA), with the acetate counterion facilitating solubility and handling. This compound is specifically engineered for the study of protease activity, particularly those enzymes that exhibit specificity for arginine-containing sequences. Its chromogenic β-naphthylamide moiety allows for sensitive detection and quantification of enzymatic cleavage events, making it a valuable tool for kinetic analyses and substrate profiling in a range of experimental settings.
Enzyme substrate assays: Z-Arg-Arg-βNA acetate serves as a highly effective chromogenic substrate for the quantitative assessment of serine and cysteine proteases, including trypsin-like and cathepsin B-like enzymes. Upon enzymatic cleavage at the arginine-arginine bond, the release of β-naphthylamine generates a measurable colorimetric or fluorometric signal. This property enables precise monitoring of protease kinetics, substrate specificity, and inhibitor potency in both purified enzyme systems and complex biological samples.
Protease inhibitor screening: The substrate is routinely employed in high-throughput screening protocols aimed at identifying and characterizing novel protease inhibitors. Its well-defined cleavage pattern and robust signal generation facilitate the rapid evaluation of candidate compounds that modulate protease activity. By providing a reproducible and sensitive readout, Z-Arg-Arg-βNA acetate supports the development of selective inhibitors for research into protease regulation and function.
Enzyme characterization: Researchers leverage this dipeptidyl β-naphthylamide derivative to elucidate the substrate preferences and catalytic mechanisms of proteolytic enzymes. Detailed kinetic studies using this substrate allow for the determination of parameters such as Km and Vmax, contributing to a deeper understanding of enzyme-substrate interactions. The information gained from such investigations aids in distinguishing between closely related protease isoforms and in mapping active site architecture.
Biochemical pathway analysis: The compound is instrumental in dissecting proteolytic pathways within cellular lysates or tissue extracts. By serving as a reporter substrate, it enables the identification and quantification of specific protease activities under physiological or experimental conditions. This application provides valuable insights into protease-mediated regulatory processes, including protein turnover, signal transduction, and cellular remodeling.
Quality control in enzyme production: Z-Arg-Arg-βNA acetate is also utilized in the quality assurance of recombinant or purified protease preparations. Its defined substrate properties allow for the standardized assessment of enzyme activity and batch-to-batch consistency during production and purification workflows. By enabling reliable measurement of functional enzyme content, it supports the maintenance of high standards in biomanufacturing and research reagent supply.
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