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Merck

M1678

Millipore

MUG EC broth

NutriSelect® Plus, suitable for microbiology

Sinónimos:

4-Methylumbelliferyl β-D-Glucuronide Escherichia coli Broth

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About This Item

Código UNSPSC:
41171606
NACRES:
NA.85

esterilidad

non-sterile

Nivel de calidad

formulario

powder

caducidad

limited shelf life, expiry date on the label

fabricante / nombre comercial

NutriSelect® Plus

técnicas

microbiological culture: suitable

pH final

6.9±0.2 (25 °C)

aplicaciones

agriculture
environmental
food and beverages
veterinary
water monitoring

microbiology

idoneidad

selective and differential for Escherichia coli
selective and differential for coliforms

Aplicación

Used for the detection of E. coli by a fluorogenic procedure.

Componentes

Ingredients (g/L)
Casein enzymatic hydrolysate, 20.00
Lactose, 5.00
Bile salts mixture, 1.50
Dipotassium phosphate, 4.00
Monopotassium phosphate, 1.50
Sodium chloride, 5.00
4-Methylumbeliferyl β-D-glucuronide (MUG), 0.05

Nota de preparación

Suspend 37 g of MUG EC Broth in 1000 ml of distilled water. Dispense in tubes containing inverted Durham′s tubes. Sterilize by autoclaving at 15 lbs. pressure (121°C) for 12-15 minutes.

Nota al pie de página

We offer two media types: the superior granulated GranuCult® and the cost-efficient powdered NutriSelect® culture media, depending on your needs.
The designations basic, plus, or prime are added to indicate the quality control level, from basic quality control to standard QC plus to prime for full regulatory compliance.

Información legal

GRANUCULT is a registered trademark of Merck KGaA, Darmstadt, Germany
NutriSelect is a registered trademark of Merck KGaA, Darmstadt, Germany

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Feng, P.C.S.
Applied and Environmental Microbiology, 43, 132-132 (1982)
Jun Zhao et al.
Cell metabolism, 31(5), 937-955 (2020-04-24)
Cell proliferation and inflammation are two metabolically demanding biological processes. How these competing processes are selectively executed in the same cell remains unknown. Here, we report that the enzyme carbamoyl-phosphate synthetase, aspartyl transcarbamoylase, and dihydroorotase (CAD) deamidates the RelA subunit

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