PEC's Proteomics Platform

COFRADIC

Unlike gel-electrophoresis based proteomic methods, COFRADIC relies on the chromatographic properties of proteome-derived peptide mixtures. These highly complex peptide mixtures are here reduced in complexity, following selected chemical or enzymatic amino-acid alterations, without compromising the representation of the parent proteins.
 
In theory, COFRADIC can be applied to the isolation of any type of peptide, provided that it can be specifically and quantitatively modified. So far, COFRADIC has been used to isolate methionyl, cysteinyl, amino terminal and/or carboxy terminal, N-glycosylated and phosphorylated peptides and peptides structurally involved in ATP/ADP small molecule binding from trypsin proteolytic digests of a proteome.
 
The N-terminal peptides are particularly useful because every protein is represented by only one peptide, thereby reducing a sample's complexity to the highest degree while monitoring in vivo protein processing events on a proteome-wide level (Van Damme et al., Nat Methods, 2005 and Nature Methods, 2010). In theory, all posttranslational modified peptides that can be altered specifically could be analyzed by COFRADIC.
 

Other proteomics services

Besides COFRADIC applications, the PEC receives peptide and protein samples that are analyzed by state-of-the-art mass spectrometers.

Typical services include, but are not limited to:

  • the characterization of isolated protein complexes
  • differential proteome analysis
  • protein quantification using SRM techniques
  • the analysis of protein modifications such as phosphorylation and ubiquitination
  • protein mass determination
  • identification of protein partners binding to drugs or small molecules

Here, gel spots or gel bands are accepted for analysis next to samples in solution. 

Applications

  • Differential proteome analysis of whole cells, tissues and body fluids using metabolic labeling, post-metabolic labeling and label-free analysis
  • Identification of a highly diverse set of in vivo co- and post-translational modifications; e.g., N-acetylation, phosphorylation, oxidation, ubiquitination etc.
  • Characterization of in vivo protein processing and protease targets (protease degradomics)


An overview of proteomics-related papers published by PEC's manager Kris Gevaert is found at http://www.ncbi.nlm.nih.gov/pubmed?term=gevaert%20k  

Contact us:

Francis Impens

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VIB Proteomics Expertise Center, UGent (PEC)
VIB Dept. of Medical Protein Research
Albert Baertsoenkaai 3
9000 GENT
BELGIUM
phone: +32 9 264 92 74

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

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