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Protein identification

Identification and determination of sequence coverage of a highly purified protein, immunoprecipitation experiment (see separate info) or identification of proteins in a complex mixture is performed after proteolytic cleavage.

Samples are accepted either in-solution, protein pellet or protein bands from a gel separation. Gel cuts are submitted in a tube and covered by 3% acetic acid in ultra pure water. Avoid the use of detergents as NP40, Triton X100 and Tween since their presence significantly interferes with the downstream MS analysis. The proteins are typically cleaved by trypsin into peptides in-gel, in-solution or filter-aided sample preparation (FASP) and analyzed by nanoLC- MS/MS. The detected peptide mass and the fragment ions are matched against protein sequences supplied by the user or against a publicly available protein database such as SwissProt using e.g.Mascot or Proteome Discoverer.

This service can be combined with offline fractionation such as high-pH reversed-phase LC or SCX to further maximize the number of protein identifications by reducing sample complexity. For plasma projects, we offer affinity depletion of high abundant proteins from human, rat and mouse.

 

Page Manager: Jörgen Bergström|Last update: 3/29/2016
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