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 highly specialized synthetic peptide substrate widely utilized in biochemical and hematological research. Designed to facilitate the quantification of proteolytic enzyme activity, S 2238 features a chromogenic group that releases a measurable color change upon enzymatic cleavage. Its unique structure allows for specific and sensitive detection of serine proteases, making it an indispensable tool in laboratories focused on coagulation studies, enzymology, and pharmaceutical development. The substrate's versatility and reliability have established it as a gold standard in assays requiring precise monitoring of enzyme kinetics and inhibitor screening.
Coagulation Research: In studies focused on the blood coagulation cascade, S 2238 serves as a critical reagent for quantifying the activity of serine proteases such as thrombin and Factor Xa. By incorporating S 2238 into chromogenic assays, researchers can monitor the generation or inhibition of these enzymes in real time, enabling detailed analysis of coagulation pathways and the effects of various agents on clot formation and dissolution. This application is fundamental in advancing our understanding of hemostatic mechanisms and developing novel anticoagulant therapies.
Enzyme Kinetics: The chromogenic properties of S 2238 make it ideal for kinetic studies of proteolytic enzymes. Scientists utilize this substrate to measure initial reaction rates, determine Michaelis-Menten constants, and evaluate the specificity of enzyme-substrate interactions. The ability to continuously monitor absorbance changes ensures that kinetic parameters are accurately captured, supporting the rational design of both enzyme inhibitors and activators. This approach is particularly valuable in elucidating the dynamic behavior of serine proteases under various experimental conditions.
Pharmaceutical Development: In the pharmaceutical industry, S 2238 is routinely employed in high-throughput screening platforms to identify and characterize potential inhibitors or modulators of serine proteases. Its robust and reproducible colorimetric response allows for the rapid assessment of compound libraries, expediting the drug discovery process. Researchers rely on S 2238-based assays to evaluate the efficacy and selectivity of candidate molecules, thus streamlining the development of new therapeutic agents targeting coagulation disorders or related pathologies.
Quality Control of Biological Products: S 2238 plays a pivotal role in the quality control and batch release testing of plasma-derived products and recombinant proteins. By incorporating this substrate into standardized assays, manufacturers can verify the functional activity of coagulation factors, ensuring product consistency and performance. The substrate's sensitivity and specificity contribute to the detection of subtle variations in enzyme activity, which is essential for maintaining the integrity of biopharmaceutical products.
Biochemical Pathway Elucidation: Researchers investigating complex biochemical pathways leverage S 2238 to dissect the roles of individual proteases within larger signaling networks. The ability to selectively monitor enzyme activity in vitro enables the mapping of proteolytic cascades and the identification of regulatory checkpoints. This application is instrumental in expanding our knowledge of cellular processes such as inflammation, apoptosis, and tissue remodeling, where serine proteases exert critical control.
In summary, S 2238 stands as a cornerstone substrate in modern enzymology and coagulation research, offering unmatched sensitivity, specificity, and versatility across a diverse array of scientific applications. From fundamental studies of blood coagulation and enzyme kinetics to the fast-paced environment of pharmaceutical development, S 2238 provides researchers with a reliable platform for quantifying protease activity and unraveling complex biological mechanisms. Its integral role in quality control and pathway elucidation further underscores its value as an essential reagent in both academic and industrial laboratories worldwide.
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