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M1678

Millipore

MUG EC broth

NutriSelect® Plus, suitable for microbiology

Synonym(s):

4-Methylumbelliferyl β-D-Glucuronide Escherichia coli Broth

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About This Item

UNSPSC Code:
41171606
NACRES:
NA.85

sterility

non-sterile

Quality Level

form

powder

shelf life

limited shelf life, expiry date on the label

manufacturer/tradename

NutriSelect® Plus

technique(s)

microbiological culture: suitable

final pH

6.9±0.2 (25 °C)

application(s)

agriculture
environmental
food and beverages
veterinary
water monitoring

microbiology

suitability

selective and differential for Escherichia coli
selective and differential for coliforms

Application

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

Components

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

Preparation Note

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.

Footnote

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.

Legal Information

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(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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