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906581

Sigma-Aldrich

DLAM-AβVproS-13CH3 Methyl Labeling Kit

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.12

technique(s)

bio NMR: suitable

Quality Level

shipped in

dry ice

storage temp.

−70°C

Categorías relacionadas

General description

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

Application

DLAM-AβVproS-13CH3 is an optimized kit to produce proteins with 13CH3 isotopomer on β-methyl alanine and valine residues. This kit has been tested with protein isotopic labeling in E. coli. It is used in 1H-13C methyl TROSY approach to study the interactions and dynamics in very large protein complexes. For protein-protein complexes spectral complexity is reduced using differentially labeled samples.
For detection of long-range nOes or for the NMR study of large proteins

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.

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues.
Rivka L Isaacson et al.
Journal of the American Chemical Society, 129(50), 15428-15429 (2007-11-29)
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
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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