3150-25-2

Basic information

• Product Name: 3-NITROPHENYL-BETA-D-GALACTOPYRANOSIDE
• Synonyms: NITROPHENYL-B-D-GALACTOPYRANOSIDE, 3-;3-NITROPHENYL-BETA-D-GALACTOPYRANOSIDE;3-NITROPHENYL-B-D-GALACTOSIDE;m-nitrophenyl beta-D-galactopyranoside;P-Nitrophenyl-Beta-D-GalactopyranosideA.R.;3-Nitrophenylb-D-galactopyranoside;3-Nitrophenyl β-D-galacto-hexopyranoside;3-nitrophenyl α-D-galactopyranoside(m-
• CAS NO: 3150-25-2
• Molecular Formula: C₁₂H₁₅NO₈
• Molecular Weight: 301.25
• EINECS: 221-585-0
• Product Categories: Substrates;Dextrins、Sugar & Carbohydrates
• Mol File: 3150-25-2.mol
• Article Data: 4

Chemical Properties

• Melting Point: 178-179°C
• Boiling Point: 573.5 °C at 760 mmHg
• Flash Point: 300.6 °C
• Appearance: /
• Density: 1.599 g/cm³
• Storage Temp.: 2-8°C
• CAS DataBase Reference: 3-NITROPHENYL-BETA-D-GALACTOPYRANOSIDE(CAS DataBase Reference)
• NIST Chemistry Reference: 3-NITROPHENYL-BETA-D-GALACTOPYRANOSIDE(3150-25-2)
• EPA Substance Registry System: 3-NITROPHENYL-BETA-D-GALACTOPYRANOSIDE(3150-25-2)

Safety Data

• Hazardous Substances Data: 3150-25-2(Hazardous Substances Data)

Usage

General Description

3-Nitrophenyl-beta-D-galactopyranoside is a chemical compound used in biochemical research as a chromogenic substrate for the detection of enzyme activity. It is a colorless to pale yellow crystalline powder with a molecular formula of C12H15NO8. 3-NITROPHENYL-BETA-D-GALACTOPYRANOSIDE is often used to detect the activity of beta-galactosidase, an enzyme that catalyzes the hydrolysis of beta-galactosides into monosaccharides. Upon hydrolysis by beta-galactosidase, 3-nitrophenyl-beta-D-galactopyranoside produces a yellow-colored product, making it a useful tool for measuring enzyme activity in biological samples.

Upstream product

• 52571-64-9 Tetra-O-acetyl-m-nitrophenyl-α-D-galactopyranosid 
• 74808-10-9 2,3,4,6-tetra-O-acetyl-D-galactopyranosyl trichloroacetimidate 
• 25878-60-8 D-galactose pentaacetate 
• 554-84-7 meta-nitrophenol 
• 4163-60-4 β-D-galactose peracetate 
• 2872-67-5 (2R,3S,4S,5R,6S)-2-(acetoxymethyl)-6-(3-nitrophenoxy)tetrahydro-2H-pyran-3,4,5-triyl triacetate 
• 3068-32-4 1-bromo-1-deoxy-2,3,4,6-tetra-O-acetyl-a-D-galactopyranoside 

Downstream Products

• 2872-67-5 (2R,3S,4S,5R,6S)-2-(acetoxymethyl)-6-(3-nitrophenoxy)tetrahydro-2H-pyran-3,4,5-triyl triacetate 
• 1824-94-8 methyl beta-D-galactopyranoside 

Relevant articles and documents

Strong Inhibition of Cholera Toxin B Subunit by Affordable, Polymer-Based Multivalent Inhibitors

Cholera is a potentially fatal bacterial infection that affects a large number of people in developing countries. It is caused by the cholera toxin (CT), an AB5 toxin secreted by Vibrio cholera. The toxin comprises a toxic A-subunit and a pentameric B-subunit that bind to the intestinal cell surface. Several monovalent and multivalent inhibitors of the toxin have been synthesized but are too complicated and expensive for practical use in developing countries. Meta-nitrophenyl α-galactoside (MNPG) is a known promising ligand for CT, and here mono- and multivalent compounds based on MNPG were synthesized. We present the synthesis of MNPG in greatly improved yields and its use while linked to a multivalent scaffold. We used economical polymers as multivalent scaffolds, namely, polyacrylamide, dextran, and hyperbranched polyglycerols (hPGs). Copper-catalyzed alkyne azide cycloaddition reaction (CuAAC) produced the inhibitors that were tested in an ELISA-type assay and an intestinal organoid swelling inhibition assay. The inhibitory properties varied widely depending on the type of polymer, and the most potent conjugates showed IC50 values in the nanomolar range.

Evaluating N-benzylgalactonoamidines as putative transition state analogs for β-galactoside hydrolysis

Experimental evidence is provided for p-methylbenzyl-d-galactonoamidine to function as a true transition state analog for the enzymatic hydrolysis of aryl-β-d-galactopyranosides by β-galactosidase (A. oryzae). The compound exhibits inhibition constants in the low nanomolar concentration range (12-56 nM) for a selection of substrates. Along these lines, a streamlined synthetic method based on phase-transfer catalysis was optimized to afford the required variety of new aryl-β-d-galactopyranosides. Last, the stability of the galactonoamidines under the assay conditions was confirmed. This journal is the Partner Organisations 2014.