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Merck

M1508

Sigma-Aldrich

4-Methylumbelliferone sodium salt

fluorogenic, ≥98% (HPLC), crystalline

Synonym(e):

β-Methylumbelliferone, 7-Hydroxy-4-methylcoumarin

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About This Item

Lineare Formel:
C10H7O3Na
CAS-Nummer:
Molekulargewicht:
198.15
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
PubChem Substanz-ID:
NACRES:
NA.32

product name

4-Methylumbelliferone sodium salt, ≥98% (HPLC), crystalline

Qualitätsniveau

Assay

≥98% (HPLC)

Form

crystalline

Farbe

yellow

Löslichkeit

water: 50 mg/mL

SMILES String

[Na+].CC1=CC(=O)Oc2cc([O-])ccc12

InChI

1S/C10H8O3.Na/c1-6-4-10(12)13-9-5-7(11)2-3-8(6)9;/h2-5,11H,1H3;/q;+1/p-1

InChIKey

JGMQHDNPUCPRQE-UHFFFAOYSA-M

Allgemeine Beschreibung

4-methylumbelliferone (4-MU) is a coumarin derivative.

Anwendung

4-Methylumbelliferone sodium salt has been used:
  • as a substrate to analyze the enzyme kinetics of its glucuronidation in the human liver
  • as a standard to quantify the free 4-methylumbelliferone released as a result of enzyme-substrate action
  • in cell survival assay to inhibit hyaluronan (HA) production and to study its effect on chemoresistance in ovarian cancer

Biochem./physiol. Wirkung

4-methylumbelliferone (4-MU) serves as a hyaluronan (HA) synthesis blocker. It exhibits anti-inflammatory, anti-fibrogenic, and antitumor properties. 4-MU is used to treat biliary spasms and might also be beneficial in nonalcoholic steatohepatitis (NASH), inflammation, hepatocyte injury, and fibrotic response. 4-MU is known to be glucuronidated by most of the uridine 5ฺ-diphospho-glucuronosyltransferase (UGT) isoforms of the human liver. This makes it a potent probe substrate to examine the overall hepatic UGTs activity.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Rebecca M DuBois et al.
PLoS pathogens, 7(12), e1002398-e1002398 (2011-12-07)
Highly pathogenic avian influenza viruses of the H5N1 subtype continue to threaten agriculture and human health. Here, we use biochemistry and x-ray crystallography to reveal how amino-acid variations in the hemagglutinin (HA) protein contribute to the pathogenicity of H5N1 influenza
Ai-Sheng Xiong et al.
PloS one, 6(11), e26773-e26773 (2011-11-19)
A β-glucuronidase variant, GUS-TR3337, that was obtained by directed evolution exhibited higher thermostability than the wild-type enzyme, GUS-WT. In this study, the utility of GUS-TR337 as an improved reporter was evaluated. The corresponding gus-tr3337 and gus-wt genes were independently cloned
Gale E Smith et al.
Virology, 509, 90-97 (2017-06-19)
Avian influenza A (H5N1) viruses represent a growing threat for an influenza pandemic. The presence of widespread avian influenza virus infections further emphasizes the need for vaccine strategies for control of pre-pandemic H5N1 and other avian influenza subtypes. Influenza neuraminidase

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