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R4883

Sigma-Aldrich

Resorufin β-D-galactopyranoside

~95%, powder

Synonym(s):

3-Phenoxazone 7-(β-D-galactopyranoside)

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About This Item

Empirical Formula (Hill Notation):
C18H17NO8
CAS Number:
95079-19-9
Molecular Weight:
375.33
Beilstein/REAXYS Number:
4335306
MDL number:
MFCD00064055
UNSPSC Code:
12352204
PubChem Substance ID:
24899376
NACRES:
NA.32

product name

Resorufin β-D-galactopyranoside, ~95%

assay

~95%

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

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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.

Storage Class

11 - Combustible Solids

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’.

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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
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
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
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