Outros

S-(4-Nitrophenyl)mercapturic acid (S-NPMA) is the major metabolite of 4-nitrophenol, which is a precursor to dyes and pharmaceuticals. S-NPMA has been detected in urine samples from humans, rats, and mice. The main metabolic pathway for S-NPMA is an oxidative conversion by cytochrome P450 enzymes. S-NPMA has been found to be a useful biomarker for the presence of polycyclic aromatic hydrocarbons in wastewater and human urine. The levels of this compound have also been shown to increase with age in humans.

4-Nitrophenyl trimethylacetate is a cytosolic proteinase inhibitor. It binds to the active site of trypsin and other enzymes that hydrolyze peptide bonds, thereby inhibiting the activity of these enzymes. 4-Nitrophenyl trimethylacetate has been shown to inhibit soybean trypsin, which has led to its use as a model system for studying enzyme inhibition. The binding site on 4-Nitrophenyl trimethylacetate is competitive with respect to substrate binding but not with respect to the enzyme's catalytic triad. This inhibitor also has a high buffer capacity and can be used in low pH systems.

Jalapeno green-Gal (Jalapeno green-beta-D-galactopyranoside) is a chromogenic indicator for beta-galactosidase activity. The colorless product is cleaved by lactose-utilizing bacteria in liquid media or on agar plates and yields a Jalapeno green colored precipitate. Jalapeno green-Gal can also be used as detecting agent for beta-galactosidase activity in reporter gene assays or for identification of positive transformants on agar plates when using the α-complementation approach.

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

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.

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.