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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.

2-Nitrophenyl 2-acetamido-2-deoxy-b-D-galactopyranoside is a carboxymethyl derivative of the natural substrate of β-galactosidase, which is used as a substrate for the production of recombinant proteins in the corynebacterium glutamicum. The enzyme β-galactosidase hydrolyzes this substrate to produce an acid molecule and a sugar molecule. This product can be used in biotechnological processes for the production of recombinant proteins or other bioactive molecules. It can also be used in the isolation of nucleic acid from bacteria or fungi, or to study bacterial membrane transport systems. 2NPGAG can be expressed as a recombinant protein with expression vectors such as pET21a and pET24a. It has been shown that this product inhibits transport through membranes by binding to cellulose, which may be useful for studies on cellulose biosynthesis

2-Nitrophenyl 2,3-di-O-acetyl-4-O-triethylsilyl-b-D-xylopyranoside is a chromogenic substrate for enzmatic assays to measure xylosidase activity. It is a derivative of xylose that can be hydrolyzed by xylosidase to release the yellow-colored 2-nitrophenyl group, which can be detected spectrophotometrically. By modifying the xylose molecule with acetyl and triethylsilyl groups, the enzyme substrate becomes more stable and resistant to degradation. This substrate is commonly used in the study of plant biomass degradation and in the detection of xylosidase activity in microorganisms.

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.

Aldol® 455 is a substrate for the enzyme beta-galactosidase. It is used in food testing, staining, and environmental testing. Aldol® 455 has been shown to be a good substrate for fluorogenic and chromogenic substrates. It can be conjugated with an antibody or other ligand for use in immunoassays. Aldol® 455 is of high purity and high quality, making it suitable for use in diagnostics and as an enzyme substrate. This product can also be used as a culture media additive.

4-Nitrophenyl 4,6-O-benzylidene-3-O-(2,3,4,6-tetra-O-acetyl-b-D-glucopyranosyl)-b-D-glucopyranoside is a high purity fluorescent reagent that can be used as a substrate for many enzymes. It is also used in environmental testing and to detect the presence of nitrophenols in food. This product has CAS number 545414.

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.

4-Nitrophenyl b-D-thiomannopyranoside acts as a substrate for β-mannosidase and thioglycoligase. Upon enzymatic cleavage, these substrates release 4-nitrophenol, a yellow chromophore that can be detected spectrophotometrically at 405 nm, facilitating quantitative measurements of enzymatic activity. Consequently, these substrates are widely used in biochemical research, clinical diagnostics, and drug discovery for evaluating the function of specific enzymes in various biological processes.

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.

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-Nitrophenyl lacto-N-tetraoside is a chromogenic substrate for enzymes that cleave lactose-specific linkages, such as beta-galactosidases. Upon enzyme cleavage, the pNP group is released, resulting in a yellow-colored solution that can be spectrophotometrically quantified at 405 nm. This substrate is commonly used in detecting lactose hydrolysis activity, such as in dairy industry for production optimization studies, or in microbiology for bacterial lactose fermentation assays. Its tetrasaccharide structure resembles that of lactose and makes it a specific substrate for lactose-utilizing enzymes. The properties of 4-nitrophenyl lacto-N-tetraoside make it a useful tool in enzyme kinetics studies and screening of new lactose-utilizing microorganisms.

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.

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.