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Merck
CN

906573

DLAM-Iδ1VproS-13CH3 Methyl Labeling Kit

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NACRES:
NA.12
UNSPSC Code:
12352200
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technique(s)

bio NMR: suitable

shipped in

dry ice

storage temp.

−70°C

Quality Level

相关类别

General description

DLAM-Iδ1VproS-13CH3 kit has 13CH3 isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.

Application

DLAM-Iδ1VproS-13CH3 is an optimized kit to produce proteins with 13CH3 isotopomer on the methyl groups of isoleucine and valine. This kit has been tested with protein isotopic labeling in E. coli. It is used in NMR investigations of the structure, dynamics and function of challenging biological systems at atomic resolution. Introduction of 13C -labeled methyl group in highly deuterated background enhances the resolution of methyl-TROSY spectra.
For detection of long-range nOes or for the NMR study of large proteins

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.

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Danger

hcodes

Hazard Classifications

Skin Corr. 1B

存储类别

8A - Combustible corrosive hazardous materials

法规信息

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Heyi Zhang et al.
Current opinion in structural biology, 38, 75-82 (2016-06-14)
Proteins come together in macromolecular assemblies, recognizing and binding to each other through their structures, and operating on their substrates through their motions. Detailed characterization of these processes is particularly suited to NMR, a high-resolution technique sensitive to structure, dynamics
Rime Kerfah et al.
Current opinion in structural biology, 32, 113-122 (2015-04-17)
Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the development of new isotopic labeling strategies has opened the possibility of exploiting
Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins.
Pierre Gans et al.
Angewandte Chemie (International ed. in English), 49(11), 1958-1962 (2010-02-17)
Silke Wiesner et al.
Current opinion in structural biology, 35, 60-67 (2015-09-26)
Intermolecular interactions are indispensible for biological function. Here we discuss how novel NMR techniques can provide unique insights into the assembly, dynamics and regulation of biomolecular complexes. We focus on applications that exploit the methyl TROSY effect and show that

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