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Merck

606839

Sigma-Aldrich

ISOGRO®-13C,15N Powder -Growth Medium

98 atom % 15N, 99 atom % 13C

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About This Item

MDL號碼:
分類程式碼代碼:
12352200
NACRES:
NA.12

同位素純度

99 atom % 13C
98 atom % 15N

品質等級

形狀

solid

技術

bio NMR: suitable
protein expression: suitable

儲存溫度

−20°C

包裝

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.

法律資訊

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

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Brendan C Mullaney et al.
Cell metabolism, 12(4), 398-410 (2010-10-05)
Acyl-CoA synthases are important for lipid synthesis and breakdown, generation of signaling molecules, and lipid modification of proteins, highlighting the challenge of understanding metabolic pathways within intact organisms. From a C. elegans mutagenesis screen, we found that loss of ACS-3, a long-chain
Claire Rosnoblet et al.
The Journal of biological chemistry, 287(53), 44249-44260 (2012-11-16)
Nonstructural protein 5B (NS5B) is essential for hepatitis C virus (HCV) replication as it carries the viral RNA-dependent RNA polymerase enzymatic activity. HCV replication occurs in a membrane-associated multiprotein complex in which HCV NS5A and host cyclophilin A (CypA) have
Melanie H Smith et al.
The Journal of biological chemistry, 289(37), 25670-25677 (2014-08-03)
A substantial fraction of nascent proteins delivered into the endoplasmic reticulum (ER) never reach their native conformations. Eukaryotes use a series of complementary pathways to efficiently recognize and dispose of these terminally misfolded proteins. In this process, collectively termed ER-associated
Tobias S Ulmer et al.
The Journal of biological chemistry, 280(10), 9595-9603 (2004-12-24)
Misfolding of the protein alpha-synuclein (aS), which associates with presynaptic vesicles, has been implicated in the molecular chain of events leading to Parkinson's disease. Here, the structure and dynamics of micelle-bound aS are reported. Val3-Val37 and Lys45-Thr92 form curved alpha-helices
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

商品

Utilizing ISOGRO® Supplementation of M9 Minimal Media to Enhance Recombinant Protein Expression.

相关内容

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