906433
TLAM-Iδ1LVproR-U-13C Methyl Labeling Kit
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About This Item
Codice UNSPSC:
12352200
NACRES:
NA.12
Prodotti consigliati
tecniche
bio NMR: suitable
Livello qualitativo
Condizioni di spedizione
dry ice
Temperatura di conservazione
−70°C
Descrizione generale
TLAM-Iδ1LVproR-U-[13C] kit has 13C isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.
Applicazioni
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).
Confezionamento
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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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
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
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
Articoli
Methyl Isotope-Labeling of Proteins from NMR-Bio
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