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Sigma-Aldrich

DLAM-LVproR-13C4 Methyl Labeling Kit

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About This Item

Código UNSPSC:
12352200
NACRES:
NA.12

técnica(s)

bio NMR: suitable

Nível de qualidade

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Categorias relacionadas

Descrição geral

DLAM-LVproR-13C4 , Kit has 13C4 isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.

Aplicação

DLAM-LVproR-13C4 methyl labeling kit is used for stereospecific labeling of leucine and valine. This kit has been tested with protein isotopic labeling in E. coli. It is used to produce methyl-labeled proteins and acquire precise dynamic information with high resolution in solid-state NMR spectroscopy.
For protein methyl group assignment by 13C isotope labeling of amino acid methyl groups separately or simultaneously.

Embalagem

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.

Pictogramas

Corrosion

Palavra indicadora

Danger

Frases de perigo

Classificações de perigo

Skin Corr. 1B

Código de classe de armazenamento

8A - Combustible corrosive hazardous materials


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Dae-Won Sim et al.
Molecules (Basel, Switzerland), 22(8) (2017-08-16)
A large portion of proteins in living organisms are membrane proteins which play critical roles in the biology of the cell, from maintenance of the biological membrane integrity to communication of cells with their surroundings. To understand their mechanism of
Rime Kerfah et al.
Journal of biomolecular NMR, 63(4), 389-402 (2015-11-15)
A new strategy for the NMR assignment of aliphatic side-chains in large perdeuterated proteins is proposed. It involves an alternative isotopic labeling protocol, the use of an out-and-back (13)C-(13)C TOCSY experiment ((H)C-TOCSY-C-TOCSY-(C)H) and an optimized non-uniform sampling protocol. It has
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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