SEE ALSO...
Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
---|---|---|---|---|---|---|
L-Arginine 7-amido-4- methylcoumarin dihydrochloride | 113712-08-6 | sc-281539 sc-281539A | 100 mg 250 mg | $136.00 $238.00 | ||
L-Arginine 7-amido-4-methylcoumarin dihydrochloride serves as a substrate for trypsin, showcasing unique fluorescence properties upon enzymatic cleavage. Its structure allows for specific interactions with the active site of trypsin, leading to efficient hydrolysis. The compound exhibits distinct reaction kinetics, with a measurable increase in fluorescence intensity correlating with substrate conversion. This behavior highlights its potential for real-time monitoring of proteolytic activity in biochemical assays. | ||||||
Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride | 21653-40-7 | sc-253173 sc-253173A | 25 mg 100 mg | $82.00 $230.00 | ||
Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride acts as a selective substrate for trypsin, characterized by its unique chromogenic properties. Upon cleavage by trypsin, it releases a nitroaniline moiety, resulting in a colorimetric change that can be quantitatively analyzed. The compound's structural features facilitate strong binding to the enzyme's active site, enhancing reaction rates. Its distinct kinetic profile allows for precise measurement of trypsin activity in various experimental conditions. | ||||||
Nα-Benzoyl-DL-arginine β-naphthylamide hydrochloride | 913-04-2 | sc-250547 sc-250547A | 500 mg 1 g | $68.00 $98.00 | ||
Nα-Benzoyl-DL-arginine β-naphthylamide hydrochloride serves as a specific substrate for trypsin, exhibiting unique fluorescence properties upon enzymatic cleavage. The β-naphthylamide group enhances the compound's affinity for the enzyme, promoting efficient substrate-enzyme interactions. This compound's reaction kinetics reveal a rapid turnover rate, making it suitable for dynamic studies of proteolytic activity. Its structural design allows for selective recognition by trypsin, facilitating detailed enzymatic analysis. | ||||||
N-4-Tosyl-L-arginine methyl ester hydrochloride | 1784-03-8 | sc-207949 sc-207949A | 5 g 25 g | $40.00 $118.00 | 1 | |
N-4-Tosyl-L-arginine methyl ester hydrochloride acts as a potent trypsin substrate, characterized by its sulfonamide moiety that enhances binding affinity through specific electrostatic interactions. The compound's unique structure promotes a favorable transition state during hydrolysis, resulting in distinct reaction kinetics. Its hydrophobic characteristics contribute to solubility in various environments, allowing for versatile experimental applications in protease activity assessments. | ||||||
N-α-Benzoyl-L-arginine ethyl ester hydrochloride | 2645-08-1 | sc-269942 | 1 g | $36.00 | ||
N-α-Benzoyl-L-arginine ethyl ester hydrochloride serves as a selective substrate for trypsin, distinguished by its aromatic benzoyl group that facilitates strong π-π stacking interactions with the enzyme's active site. This compound exhibits unique reaction kinetics, characterized by a rapid cleavage rate due to its optimal steric configuration. Additionally, its ethyl ester functionality enhances lipophilicity, promoting effective substrate-enzyme interactions in diverse biochemical assays. | ||||||
Nα-Benzoyl-L-arginine-7-amido-4-methylcoumarin hydrochloride | 83701-04-6 | sc-301455 sc-301455A | 50 mg 250 mg | $130.00 $531.00 | 2 | |
Nα-Benzoyl-L-arginine-7-amido-4-methylcoumarin hydrochloride acts as a specific substrate for trypsin, featuring a coumarin moiety that fluoresces upon cleavage, allowing for real-time monitoring of enzymatic activity. The compound's unique amide bond enhances its stability while facilitating precise interactions with the enzyme's active site. Its distinct structural design promotes efficient hydrolysis, making it a valuable tool for studying proteolytic pathways and enzyme kinetics. | ||||||
N-α-Benzoyl-DL-arginine 4-nitroanilide monohydrochloride | 911-77-3 | sc-207952 sc-207952A sc-207952B | 100 mg 500 mg 5 g | $67.00 $79.00 $292.00 | ||
N-α-Benzoyl-DL-arginine 4-nitroanilide monohydrochloride serves as a selective substrate for trypsin, characterized by its nitroanilide group that undergoes significant colorimetric changes upon enzymatic cleavage. This transformation allows for quantitative analysis of trypsin activity. The compound's unique structural features, including the aromatic benzoyl group, enhance its binding affinity to the enzyme, promoting rapid reaction kinetics and facilitating detailed studies of proteolytic mechanisms. | ||||||
Nα-Benzoyl-L-arginine 4-methoxy-β-naphthylamide hydrochloride | 100900-33-2 | sc-215529 sc-215529A sc-215529B | 25 mg 50 mg 250 mg | $214.00 $306.00 $510.00 | 1 | |
Nα-Benzoyl-L-arginine 4-methoxy-β-naphthylamide hydrochloride acts as a specific substrate for trypsin, distinguished by its methoxy-β-naphthylamide moiety, which exhibits notable fluorescence changes upon enzymatic hydrolysis. This property enables sensitive detection of trypsin activity. The compound's unique interactions with the enzyme's active site, driven by its aromatic and polar characteristics, enhance substrate specificity and influence reaction rates, providing insights into proteolytic pathways. |