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906433

Sigma-Aldrich

TLAM-Iδ1LVproR-U-13C Methyl Labeling Kit

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.12

technique(s)

bio NMR: suitable

Quality Level

200

shipped in

dry ice

storage temp.

−70°C

General description

TLAM-Iδ1LVproR-U-[13C] kit has 13C isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.

Application

For protein methyl group assignment by 13C isotope labeling of amino acid methyl groups separately or simultaneously.
TLAM-Iδ1LVproR-U-[13C] kit is used to label isoleucine, leucine and valine residues with 13C isotopomer. This kit has been tested with protein isotopic labeling in E. coli. It can be used to increase the sensitivity, interaction correlation and resolution of larger proteins in NMR spectroscopy (typically above 50 KDa).

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.

Pictograms

Corrosion
GHS05

Signal Word

Danger

Hazard Statements

H314

Hazard Classifications

Skin Corr. 1B

Storage Class Code

8A - Combustible corrosive hazardous materials

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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
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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