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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:
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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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