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Merck
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Key Documents

906646

Sigma-Aldrich

TLAM-Iδ1MεTγ-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

General description

TLAM- Iδ1MεTγ-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
TLAM- Iδ1MεTγ-13CH3 kit is optimized with regio-specific labeling of isoleucine, methionine and threonine residues with 13CH3 isotopomer. This kit has been tested with protein isotopic labeling in E. coli. It is used in filtering inter-molecular NOEs in supramolecular assemblies and more precise structural information of homo-oligomeric protein structure.

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

signalword

Danger

hcodes

H314

Hazard Classifications

Skin Corr. 1B

Storage Class

8A - Combustible corrosive hazardous materials

Certificados de análisis (COA)

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Jose Luis Ortega-Roldan et al.
Methods in molecular biology (Clifton, N.J.), 1764, 73-85 (2018-04-02)
In this chapter, we describe how NMR chemical shift titrations can be used to study the interaction between two proteins with emphasis on mapping the interface of the complex and determining the binding affinity from a quantitative analysis of the
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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