S 2238 is a chromogenic peptide substrate incorporating a para-nitroaniline reporter group for enzymatic cleavage studies. The sequence allows sensitive monitoring of protease activity and turnover kinetics. Researchers employ it to map cleavage-site specificity and catalytic profiling. Its well-defined structure ensures reproducible analytical performance.
CAT No: R2219
CAS No:64815-81-2
Synonyms/Alias:H-D-Phe-pip-arg-pna;64815-81-2;S-2238;Chromogenic substrate S-2238;H-Phe-pip-arg-pna;H-Phe-pip-arg-p-nitroanilide;S 2238;D-Phenylalanyl-L-2-piperidinecarbonyl-N-(4-nitro phenyl)-L-argininamide;H-D-Phenylalanyl-pip-arg-p-nitroanilide;(2S)-1-[(2R)-2-amino-3-phenylpropanoyl]-N-[(2S)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]piperidine-2-carboxamide;H-D-Phenylalanyl-L-pipecolyl-arginine-nitroanilide;D-Phe-Pip-Arg-PNA;D-Phenylalanyl-(2S)-2-piperidinecarbonyl-N-(4-nitrophenyl)-L-argininamide Dihydrochloride;BDBM12678;DTXSID50983410;YDMBNDUHUNWWRP-VJBWXMMDSA-N;BDBM233013;GLXC-01860;GLXC-01861;(S)-1-(D-Phenylalanyl)-N-((S)-5-guanidino-1-((4-nitrophenyl)amino)-1-oxopentan-2-yl)piperidine-2-carboxamide;AKOS040753879;DA-64082;HY-123275;CS-0082307;H-D-phenylalanyl-L-pipecolyl-L-arginine-p-nitroaniline dihydrochloride;N-(4-nitrophenyl)-N2-{[(2S)-1-D-phenylalanylpiperidin-2-yl]carbonyl}-L-argininamide;(1S)-1-[2-[4-[4-(Aminocarbonyl)phenyl]-1-piperazinyl]ethyl]-3,4-dihydro-N-methyl-1H-2-benzopyran- 6-carboxamide;(2S)-2-{[(2S)-1-[(2R)-2-amino-3-phenylpropanoyl]piperidin-2-yl]formamido}-5-carbamimidamido-N-(4-nitrophenyl)pentanamide;N-[5-Carbamimidamido-1-(4-nitroanilino)-1-oxopentan-2-yl]-1-phenylalanylpiperidine-2-carboximidic acid;
S 2238, also known as Chromogenic Substrate for Factor Xa, is a synthetic peptide-based compound widely utilized in hemostasis research and coagulation studies. Structurally designed to mimic the natural substrates of coagulation factor Xa, it incorporates a chromogenic moiety that enables sensitive spectrophotometric detection of enzymatic activity. The substrate's unique ability to release a measurable chromophore upon cleavage by factor Xa has made it a cornerstone reagent in the quantitative analysis of blood coagulation pathways, anticoagulant efficacy testing, and enzymology research. Its reliable performance and specificity have established S 2238 as an essential tool in both academic and industrial laboratories investigating the molecular mechanisms of thrombosis and hemostatic regulation.
Enzyme Activity Assays: S 2238 is predominantly applied in chromogenic assays for the quantitative determination of factor Xa activity. By serving as a selective substrate, it enables researchers to monitor the rate of substrate hydrolysis through the release of a colored product, which can be precisely measured spectrophotometrically. This application is crucial for kinetic studies of factor Xa, providing insights into enzyme function, catalytic efficiency, and the effects of various modulators or inhibitors on proteolytic activity.
Anticoagulant Screening: The compound plays a vital role in the evaluation of anticoagulant compounds targeting factor Xa. In pharmaceutical development and quality control settings, S 2238-based assays are employed to assess the potency and specificity of direct and indirect factor Xa inhibitors. By quantifying residual enzymatic activity in the presence of candidate molecules, these assays facilitate the screening and optimization of new anticoagulant agents, supporting the advancement of safer and more effective therapeutic options.
Coagulation Pathway Research: S 2238 enables detailed investigation of the intrinsic and extrinsic pathways of blood coagulation by offering a reliable method for tracking factor Xa generation and activity. Researchers utilize the substrate to dissect the complex regulatory networks governing hemostasis, identify key modulators of coagulation cascades, and elucidate the molecular basis of bleeding and thrombotic disorders. The ability to perform real-time, quantitative measurements enhances the mechanistic understanding of coagulation processes at both cellular and molecular levels.
Diagnostic Reagent Development: In the development of diagnostic assays for coagulation disorders, S 2238 is frequently incorporated as a core reagent for the detection and quantification of factor Xa activity in plasma samples. Its high sensitivity and specificity make it suitable for laboratory protocols aimed at identifying abnormalities in the coagulation cascade, such as deficiencies or dysfunctions of clotting factors. By enabling reproducible and accurate measurements, the substrate supports the creation of robust diagnostic platforms for research-use applications.
Enzyme Kinetics and Inhibitor Profiling: The chromogenic peptide substrate provides a robust system for characterizing the kinetic parameters of factor Xa and profiling the inhibitory effects of various compounds. Researchers can determine Michaelis-Menten constants, inhibition modes, and structure-activity relationships by analyzing the interaction of enzyme, substrate, and inhibitors. Such studies are pivotal in the rational design of new anticoagulant molecules and in advancing the fundamental understanding of serine protease biochemistry within the context of blood coagulation.
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