Interaction Analysis Kits and Reagents

The analysis of protein complexes by MALDI mass spectrometry is typically labor intensive because of the tendency of these complexes to dissociate during analysis. CovalX has developed a method for the easy and fast analysis of protein complexes using High-Mass MALDI mass spectrometry. The first step of the analysis is to stabilize the non covalent complexes of interest using dedicated cross-linking reagents and protocols. After stabilization, the sample are ready for direct analysis by High-Mass ToF mass spectrometry.

High-Mass MALDI ToF mass spectra of the protein complex Thymidine Kinase (TK). A. TK (1ul) analyzed without cross-linking. Only the monomer is detected. B. TK analyzed after cross-linking with disuccimidyl suberate (0.1 mg/ml, 30 minutes incubation time). TK dimer is detected with m=87.8 kDa. C. Same analysis with CovalX K100 analysis reagent (0.1 mg/ml, 30 minutes incubation time).

To analyze intact protein complexes by High-Mass MALDI ToF mass spectrometry, it is crucial to stabilize specifically the complexes with highly efficient cross-linking reagents. CovalX has developed dedicated reagent and buffers to prepare non-covalent protein complexes for High-Mass MALDI analysis. To increase cross-linking efficiency, CovalX's reagents contain cocktails of cross-linkers with different spacers lengths able to covalently bind specific protein complexes with the highest efficiency. The specificity of CovalX cross-linking reagents allows to stabilize covalently protein complexes even in contaminated or unpurified samples.

Peer Reviewed Publication:

 Reactivity and Applications of New Amine Reactive Cross-Linker for Mass Spectrometry Detection of Protein Complexes. Bich, C et al. Anal. Chem, 2009, Article ASAP, 8 December 2009. more...

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