Skip to Content
MilliporeSigma
All Photos(1)

Documents

R4883

Sigma-Aldrich

Resorufin β-D-galactopyranoside

~95%

Sign Into View Organizational & Contract Pricing

Synonym(s):
3-Phenoxazone 7-(β-D-galactopyranoside)
Empirical Formula (Hill Notation):
C18H17NO8
CAS Number:
Molecular Weight:
375.33
Beilstein/REAXYS Number:
4335306
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

assay

~95%

Quality Level

form

powder

solubility

DMSO: 20 mg/mL, clear, orange to red

storage temp.

−20°C

SMILES string

OC[C@H]1O[C@@H](Oc2ccc3N=C4C=CC(=O)C=C4Oc3c2)[C@H](O)[C@@H](O)[C@H]1O

InChI

1S/C18H17NO8/c20-7-14-15(22)16(23)17(24)18(27-14)25-9-2-4-11-13(6-9)26-12-5-8(21)1-3-10(12)19-11/h1-6,14-18,20,22-24H,7H2/t14-,15+,16+,17-,18-/m1/s1

InChI key

QULZFZMEBOATFS-DISONHOPSA-N

Looking for similar products? Visit Product Comparison Guide

General description

Resorufin β-D-galactopyranoside is a non-fluorescent compound and is orange-yellow in color. It is hydrolyzed by the enzyme β-galactosidase (β-Gal) to yield fluorescent resorufin.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Immobilized enzyme kinetics analyzed by flow-through microfluorimetry: resorufin-beta-D-galactopyranoside as a new fluorogenic substrate for beta-galactosidase
Hofmann J and Sernetz M
Analytica Chimica Acta, 163, 67-72 (1984)
Microchip device for performing enzyme assays
Hadd AG, et al.
Analytical Chemistry, 69(17), 3407-3412 (1997)
Brian P English et al.
Nature chemical biology, 2(2), 87-94 (2006-01-18)
Enzymes are biological catalysts vital to life processes and have attracted century-long investigation. The classic Michaelis-Menten mechanism provides a highly satisfactory description of catalytic activities for large ensembles of enzyme molecules. Here we tested the Michaelis-Menten equation at the single-molecule
Yuliang Xie et al.
Analytical chemistry, 84(17), 7495-7501 (2012-08-14)
In this work we present an acoustofluidic approach for rapid, single-shot characterization of enzymatic reaction constants K(m) and k(cat). The acoustofluidic design involves a bubble anchored in a horseshoe structure which can be stimulated by a piezoelectric transducer to generate
Seung-Yong Jung et al.
Langmuir : the ACS journal of surfaces and colloids, 24(9), 4439-4442 (2008-03-26)
A device with femtoliter-scale chambers and controlled reaction initiation was developed for single-molecule enzymology. Initially separated substrate and enzyme streams were rapidly mixed in a microfluidic device and encapsulated in an array of individual microreactors, allowing for enzyme kinetics to

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service