Pefachrome® FXa* integrates a chromogenic element with a tailored peptide sequence that enables precise monitoring of enzyme activity. Its cleavage-responsive design assists kinetic and mechanistic investigations. The compound's structural features support controlled solubility and assay performance. Applications include protease research, substrate profiling, and biochemical method development.
CAT No: R2620
CAS No:80895-10-9
Synonyms/Alias:PEFACHROME(R) FXA*;80895-10-9;acetic acid;methyl N-[(2R)-3-cyclohexyl-1-[[2-[[(2S)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-1-oxopropan-2-yl]carbamate;CH3OCO-D-CHA-Gly-Arg-pNA (acetate);Pefachrome(R)fxa*;DTXSID30584964;CH3OCO-D-CHA-Gly-Arg-pNA acetate;DA-66544;Pefachrome(R) Fxa, >=95.0% (HPLC);HY-153829;CS-0865277;Acetic acid--3-cyclohexyl-N-(methoxycarbonyl)-D-alanylglycyl-N~5~-(diaminomethylidene)-N-(4-nitrophenyl)-L-ornithinamide (1/1);
Pefachrome(R) fxa* is a synthetic chromogenic substrate specifically engineered for the detection and quantification of activated factor X (FXa) activity in biochemical assays. As a small-molecule substrate, it features a peptide sequence mimicking the natural cleavage site recognized by FXa, conjugated to a chromogenic reporter group. Upon enzymatic hydrolysis by FXa, the substrate releases a colored product, enabling sensitive spectrophotometric measurement. This substrate is widely utilized in coagulation research, enzymology, and drug discovery due to its high specificity and reliable performance in in vitro assay systems.
Enzyme activity assays: Pefachrome(R) fxa* is routinely employed in the quantitative measurement of FXa activity in purified systems, plasma, or other biological samples. Its design allows for the direct and continuous monitoring of FXa-mediated substrate cleavage, facilitating kinetic studies and the determination of enzymatic parameters such as Km and Vmax. Researchers rely on this substrate to assess FXa function under varying experimental conditions, providing critical data for understanding the biochemistry of the coagulation cascade.
Anticoagulant screening: The substrate serves as a valuable tool in the screening and characterization of direct and indirect FXa inhibitors, which are of significant interest in anticoagulant drug development. By enabling real-time monitoring of FXa inhibition, it supports high-throughput screening workflows and detailed mechanistic studies. The chromogenic readout allows for precise quantification of inhibitor potency, selectivity, and mode of action, aiding in the optimization of lead compounds for preclinical research.
Quality control and standardization: In industrial and clinical laboratory settings, Pefachrome(R) fxa* is utilized for the calibration and quality assurance of FXa-based diagnostic assays and reagents. Its consistent performance and well-characterized cleavage kinetics make it an ideal standard for validating assay sensitivity, linearity, and reproducibility. Laboratories depend on this substrate to maintain rigorous assay standards and to troubleshoot performance issues in coagulation testing platforms.
Biochemical pathway analysis: The substrate is instrumental in dissecting the molecular mechanisms underlying blood coagulation and related proteolytic pathways. By providing a quantifiable and specific readout of FXa activity, it enables researchers to investigate the regulation of prothrombinase complex formation, feedback mechanisms, and the impact of cofactors or modulators. These insights contribute to a deeper understanding of hemostasis and thrombosis at the molecular level.
Protein engineering and mutagenesis studies: Pefachrome(R) fxa* is also applied in the functional characterization of recombinant FXa variants or engineered proteases. By comparing substrate cleavage rates and patterns, scientists can assess the impact of specific amino acid substitutions on enzyme activity, substrate recognition, and inhibitor sensitivity. This application supports the rational design of novel proteases with tailored properties for research or biotechnological applications, expanding the utility of chromogenic substrates in protein science.
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