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Aldol® 515 N-glutaryl-L-phenylalanine amide is a chromogenic and fluorogenic enzyme substrate used for detection of L-glutamate-phenylalanine (GluPhe)-specific peptidase activity. The colorless enzyme substrate is cleaved the GluPhe-specific peptidase, yielding development of orange-red coloration. In addition, red fluorescence is generated when Aldol® 355 fluorescence enhancer or a suitable matrix is present. Aldol® 515 N-glutaryl-L-phenylalanine amide can be used in enzyme assays and live bacterial cultures. Aldol® 515 N-glutaryl-L-phenylalanine amide is suitable for use in liquid and solid media, under aerobic as well as anaerobic conditions.

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.

4-Nitrophenyl b-D-cellohexaoside is a substrate for many enzymes and can be used to detect the presence of these enzymes in biological samples. It can also be used to detect the presence of bacteria, fungi, parasites, and viruses. 4-Nitrophenyl b-D-cellohexaoside is an excellent substrate for enzyme reactions that produce a chromogenic or fluorogenic product. This product is often conjugated with other compounds such as antibodies or antigens to form an immunoassay. 4-Nitrophenyl b-D-cellohexaoside is made from a high purity chemical by a process called nitration with sodium nitrate and sulfuric acid.

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.

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-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.