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Merck

616729

ISOGRO®-D Powder -Growth Medium

97-99 atom % D

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.12
MDL number:
Isotopic purity:
97-99 atom % D
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isotopic purity

97-99 atom % D

technique(s)

bio NMR: suitable

storage temp.

−20°C

Quality Level

Packaging

This product may be available from bulk stock and can be packaged on demand. For information on pricing, availability and packaging, please contact Stable Isotopes Customer Service.

Legal Information

ISOGRO is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

13 - Non Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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J L Urbauer et al.
The Journal of biological chemistry, 276(44), 41128-41132 (2001-08-24)
The association of the bacteriophage T4-encoded AsiA protein with the final sigma(70) subunit of the Escherichia coli RNA polymerase is one of the principal events governing transcription of the T4 genome. Analytical ultracentrifugation and NMR studies indicate that free AsiA
Antonina A Berkut et al.
The Journal of biological chemistry, 289(20), 14331-14340 (2014-03-29)
In this study, we present the spatial structure of the wheat antimicrobial peptide (AMP) Tk-AMP-X2 studied using NMR spectroscopy. This peptide was found to adopt a disulfide-stabilized α-helical hairpin fold and therefore belongs to the α-hairpinin family of plant defense
Dries Verdegem et al.
The Journal of biological chemistry, 286(23), 20441-20454 (2011-04-15)
Nonstructural protein 5A (NS5A) is essential for hepatitis C virus (HCV) replication and constitutes an attractive target for antiviral drug development. Although structural data for its in-plane membrane anchor and domain D1 are available, the structure of domains 2 (D2)
Xavier Hanoulle et al.
The Journal of biological chemistry, 282(47), 34148-34158 (2007-09-15)
The chemotaxis and integrin-mediated adhesion of T lymphocytes triggered by secreted cyclophilin B (CypB) depend on interactions with both cell surface heparan sulfate proteoglycans (HSPG) and the extracellular domain of the CD147 membrane receptor. Here, we use NMR spectroscopy to
Emma A Morrison et al.
The Journal of biological chemistry, 289(10), 6825-6836 (2014-01-23)
EmrE, a small multidrug resistance transporter, serves as an ideal model to study coupling between multidrug recognition and protein function. EmrE has a single small binding pocket that must accommodate the full range of diverse substrates recognized by this transporter.

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