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4-nitrophenyl 6-O-DMT-a-D-mannopyranoside is a fluorescent substrate for the enzyme beta-glucosidase. It reacts with an acyl group at the C2 position of the glycoside moiety, producing an aldehyde group at the C1 position and a hydroxymethylene group at the C4 position. This reaction is catalyzed by beta-glucosidase, which cleaves the glycosidic linkage in sucrose and other disaccharides. The product can be detected using luminescence methods, such as chemiluminescence or bioluminescence.
4-nitrophenyl 6-O-DMT-a-D-mannopyranoside is used to detect β glucosidase activity in bacteria. This substrate has been shown to be sensitive and specific for β glucosidase activity when combined with fluorescence detection technology

Modified naphtol AS substrate used in histochemical and cytochemical staining

1-Naphthyl-alpha-D-mannopyranoside is a chromogenic substrate. It is used in diagnostics and as a reagent for enzymatic analysis of alpha-mannosidase activity in culture media, food testing, and environmental testing.

4-Nitrophenyl beta-galactoside (pNP-Gal) is a chromogenic substrate commonly used in enzymatic assays to detect and quantify the presence of beta-galactosidase. It is hydrolyzed by the enzyme to release 4-nitrophenol, which produces a yellow color that can be measured spectrophotometrically. Similarly, 4-Nitrophenyl beta-glucoside (pNP-Glc) can be used to assay beta-glucosidase activity. 4-Nitrophenyl beta-globotrioside (pNP-Glo) is a similar compound that has been designed as a substrate for glycosidases that cleave terminal beta-galactosyl-(1->3)-N-acetylgalactosamine residues. In these assays, the release of 4-nitrophenol can be measured to determine the activity of the enzyme under study. The use of chromogenic substrates like pNP-Glo allows for the rapid and reliable detection of glycosidase activity in a variety of biological samples.

4-Nitrophenyl alpha-D-maltotetraoside is a chromogenic substrate used for the detection of alpha-glucosidase and alpha-amylase activity. The four glucose units in the molecule are hydrolyzed by the enzyme, releasing 4-nitrophenol and allowing for easy colorimetric measurement of enzymatic activity

4-Nitrophenyl-myo-inositol-1-yl phosphate is a highly specific chromogenic substrate used for the detection, quantification, and characterization of phosphoinositide phosphatases. When cleaved by the target enzyme, it generates a highly absorbing 4-nitrophenyl moiety, producing a yellow color that can be measured spectrophotometrically. This versatile substrate is valuable in examining phosphoinositide phosphatase activity, enzyme kinetics, substrate specificity, and inhibition studies in various cellular processes, including signal transduction, lipid metabolism, and membrane trafficking.