608300
ISOGRO®-15N,D Powder -Growth Medium
98 atom % 15N, 97 atom % D
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About This Item
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isotopic purity
98 atom % 15N
97 atom % D
form
solid
technique(s)
bio NMR: suitable
protein expression: suitable
storage temp.
−20°C
Related Categories
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 Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Nicholas C Fitzkee et al.
The Journal of biological chemistry, 285(23), 18072-18084 (2010-04-07)
The human immunodeficiency virus type 1 (HIV-1) integrase (IN) is a critical enzyme involved in infection. It catalyzes two reactions to integrate the viral cDNA into the host genome, 3' processing and strand transfer, but the dynamic behavior of the
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
Christian Koehler et al.
The Journal of biological chemistry, 286(17), 14842-14851 (2011-03-04)
NarE is a 16 kDa protein identified from Neisseria meningitidis, one of the bacterial pathogens responsible for meningitis. NarE belongs to the family of ADP-ribosyltransferases (ADPRT) and catalyzes the transfer of ADP-ribose moieties to arginine residues in target protein acceptors.
Alexandria N Richart et al.
The Journal of biological chemistry, 287(22), 18730-18737 (2012-04-12)
The chromoshadow domain (CSD) of heterochromatin protein 1 (HP1) was recently shown to contribute to chromatin binding and transcriptional regulation through interaction with histone H3. Here, we demonstrate the structural basis of this interaction for the CSD of HP1α. This
Articles
Utilizing ISOGRO® Supplementation of M9 Minimal Media to Enhance Recombinant Protein Expression.
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