Others

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.

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.

2-Nitrophenyl laurate is a fatty acid that is not able to be degraded and has a high affinity for magnetic particles. It can be used in the immobilization of bacteria, such as Stenotrophomonas maltophilia, which are resistant to many antibiotics. 2-Nitrophenyl laurate also inhibits the enzyme lipolytic enzymes, which are responsible for the degradation of phospholipids in the cell membrane. This inhibition may lead to an increase in bacterial susceptibility to antibiotics. 2-Nitrophenyl laurate is a synthetic substrate that can be used to study the regulation of lipolytic enzymes by regulatory proteins.

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 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

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-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.