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4-Nitrophenyl 2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside is a versatile chromogenic substrate designed for the detection and quantification of various glycosidase enzymes. This substrate is widely used in enzyme assays, producing a yellow color upon cleavage by target enzymes. The 4-Nitrophenol released in this reaction can be easily monitored spectrophotometrically, allowing for rapid and accurate enzyme analysis. This high-quality substrate provides a convenient and reliable tool for researchers in biochemistry, enzymology, and related fields.

Aldol® 467 N-acetyl-beta-D-glucosaminide is a chromogenic and fluorogenic enzyme substrate used for detection of beta-N-acetyl-glucosaminidase activity. The colorless enzyme substrate is cleaved in the presence of beta-N-acetyl-glucosaminidase yielding development of a yellow product. In addition, green fluorescence is generated when a suitable matrix or Aldol® 355 fluorescence enhancer is present. Aldol® 467 N-acetyl-beta-D-glucosaminide amide can be used in enzymatic assays or in live bacterial cultures. Aldol® 467 N-acetyl-beta-D-glucosaminide is suitable for use in liquid and solid media, under aerobic as well as anaerobic conditions.

4-Chloro-3-indoxyl-1,3-diacetate is a chromogenic substrate used in the identification of bile acids. It reacts with 4-chlorophenol to form a red dye. This compound is also used as a ligand for metal ions.

4-Nitrophenyl 2-acetamido-3-O-(2,3,4,6-tetra-O-acetyl-b-D-galactopyranosyl)-2-deoxy-a-D-galactopyranoside is a chromogenic substrate designed for the detection and quantification of enzyme activity. This tetra-acetylated compound is specifically designed to be cleaved by enzymes, releasing a yellow 4-nitrophenol product that can be easily measured spectrophotometrically, allowing for accurate and sensitive analysis of enzyme kinetics and inhibition studies.

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 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

Modified naphtol AS substrate used in histochemical and cytochemical staining

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-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.