906514
SLAM-Aβ-13CH3 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
SLAM-Aβ-13CH3 Kit has 13CH3 isotopomer precursor and contains protocol instructions for creation of isotopically-labeled proteins.
Applicazioni
For detection of long-range nOes or for the NMR study of large proteins
The methyl group in alanine is labeled by 13CH3 isotopomer using SLAM-Aβ-13CH3 Kit. The labeled methyl probes are well separated in Methyl-TROSY spectra. This kit has been tested with protein isotopic labeling in E. coli. It is used to increase high level of 13CH3 isotopomer in methyl groups of Alanine. They are also used to study structural dynamics, interactions of proteins and reduce the spectral overlap using combination of SLAM kits
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.
Codice della classe di stoccaggio
11 - Combustible Solids
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Zachary K Boswell et al.
Biochemistry, 58(3), 144-155 (2018-10-20)
NMR spectroscopy is particularly adept at site-specifically monitoring dynamic processes in proteins, such as protein folding, domain movements, ligand binding, and side-chain rotations. By coupling the favorable spectroscopic properties of highly dynamic side-chain methyl groups with transverse-relaxation-optimized spectroscopy (TROSY), it
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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