Protein Interaction Analysis | CovalX

CovalX developed a method for a fast, sensitive and accurate analysis of protein complexes by High-Mass MALDI mass spectrometry. Unfragmented and undigested, the protein complexes are detected intact using specially developed cross-linking reagents and high-mass detection system.

Using cross-linking chemistry and High-Mass MALDI ToF mass spectrometry, it becomes possible to easily analyze non-covalent protein complexes in the 1-1000 kDa range.

The use of High-Mass MALDI allows a much faster, cheaper and more accurate method for studying protein interactions:

  • The stoichiometry of the complex: unique information for understanding the shape of your protein complex.
  • Clear identification of the partners involved in the complex.
  • No need for immobilization, the complex is detected without labeling.
  • Fast: 30 minutes per assay.
  • Specific: only the specific complexes are detected.
  • Sensitive: Only a few hundred femtomoles of the protein sample is a few ul are required to achieve the analysis.

In the spectrum presented, the protein complex AMPk is analyzed by High-Mass MALDI ToF mass spectrometry before cross-linking (black) and after cross-linking (red) with CovalX's K200 MALDI MS Analysis kit. Before cross-linking, the three subunits α, β, and γ of the protein complex are detected with m=30.22 kDa, m=37.38 kDa, and m=64.97 kDa. After cross-linking, the intact protein complex corresponding to the stoichiometry [α·β·γ] is detected with m=129.95 kDa. Riek U et al.; J. Biol. Chem.; 2008.

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