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
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Ara Celi DiCostanzo et al.
The Journal of biological chemistry, 287(33), 27997-28006 (2012-06-29)
Light chain amyloidosis is an incurable protein misfolding disease where monoclonal immunoglobulin light chains misfold and deposit as amyloid fibrils, causing organ failure and death. Previously, we determined that amyloidogenic light chains AL-09 and AL-103 do not form fibrils at
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
Xavier Hanoulle et al.
The Journal of biological chemistry, 284(20), 13589-13601 (2009-03-20)
We report here a biochemical and structural characterization of domain 2 of the nonstructural 5A protein (NS5A) from the JFH1 Hepatitis C virus strain and its interactions with cyclophilins A and B (CypA and CypB). Gel filtration chromatography, circular dichroism
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
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
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