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 Aminopeptidase B, characterized by its unique coumarin moiety that enhances fluorescence upon enzymatic cleavage. This property allows for sensitive detection of enzymatic activity. The compound's structural features facilitate specific interactions with the enzyme, promoting efficient substrate binding and hydrolysis. Its kinetic profile reveals a distinct turnover rate, influenced by the enzyme's catalytic efficiency and substrate concentration. | ||||||
L-Lysine 7-amido-4-methylcoumarin, acetate salt | 201853-23-8 | sc-300887B sc-300887 sc-300887A | 100 mg 250 mg 1 g | $185.00 $330.00 $1085.00 | 1 | |
L-Lysine 7-amido-4-methylcoumarin, acetate salt, acts as a substrate for Aminopeptidase B, distinguished by its unique amido and coumarin components that contribute to its reactivity. The compound exhibits selective binding to the enzyme's active site, leading to a notable increase in fluorescence upon cleavage. Its structural conformation allows for optimal alignment during the catalytic process, resulting in a specific reaction pathway that enhances the enzyme's hydrolytic activity. | ||||||
L-Arginine β-naphthylamide hydrochloride | 18905-73-2 | sc-207793 sc-207793A | 1 g 5 g | $219.00 $663.00 | ||
L-Arginine β-naphthylamide hydrochloride serves as a substrate for Aminopeptidase B, characterized by its β-naphthylamide moiety that enhances enzyme affinity. This compound undergoes hydrolysis, producing a distinct chromogenic product that facilitates real-time monitoring of enzymatic activity. The presence of the arginine side chain promotes specific interactions with the enzyme's active site, influencing reaction kinetics and enabling precise substrate turnover rates. Its unique structural features contribute to a tailored enzymatic response. |