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HLAM-AβIδ1MεLVproSTγ-13CH3 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

Related Categories

General description

HLAM-AβIδ1MεLVproSTγ-13CH3 kit has 13CH3 isotopomer precursors and contains protocol instructions for creation of isotopically-labeled proteins.

Application

For detection of long-range nOes or for the NMR study of large proteins
HLAM-AβIδ1MεLVproSTγ-13CH3 is an optimized kit used to produce proteins with 13CH3 isotopomer on methyl groups of alanine, isoleucine, methionine, leucine and threonine residues. This kit has been tested with protein isotopic labeling in E. coli. It can be used to study large molecular system and complex protein structure in NMR spectroscopy along with other spectroscopic approaches. The sensitivity of the isotopomer can be enhanced by three-fold multiplicity. This kit can also be used to simplify crowded spectra to provide specific probes of dynamic and structural studies in solid state NMR spectroscopy.

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. jj

Pictograms

Corrosion
GHS05

Signal Word

Danger

Hazard Statements

H314

Hazard Classifications

Skin Corr. 1B

Storage Class Code

8A - Combustible corrosive hazardous materials

Certificates of Analysis (COA)

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César Fernández et al.
Current opinion in structural biology, 13(5), 570-580 (2003-10-22)
Transverse relaxation-optimized spectroscopy (TROSY), in combination with various isotope-labeling techniques, has opened avenues to study biomolecules with molecular masses of up to 1000000Da by solution NMR. Important recent applications of TROSY include the structure determination of membrane proteins in detergent
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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