The Proteomics Core Facility provides a wide range of protein analyses for different applications in biomedical sciences. We offer protein identification and quantification analyses to profile changes in the abundance of proteins and their modifications (e.g. phosphorylation, acetylation, glycosylation, ubiquitylation, SUMOylation) from cell extracts and immunopurified protein complexes.

Our facility also offers immunopeptidome analyses to identify peptides and neoantigens associated to major histocompatibility complexes from cell cultures and biological specimens.

The facility is equipped with high performance LC-MS/MS instruments enabling the identification of trace levels peptides in complex samples and can combine different on-line or off-line fractionation methods to expand the comprehensiveness of proteomic analyses.

For more information, visit the CAPCA

Services offered:

• Affinity methods for the enrichment of different protein modifications (e.g phosphorylation, acetylation, glycosylation, ubiquitylation, SUMOylation)
• Separation of protein extracts by gel electrophoresis
• Band excision and proteolytic digestion
• In solution digestion with different enzymes (e.g. trypsin, chymotrypsin, Glu-C, Asp-N)
• Off-line fractionation (e.g. cation exchange, basic reverse phase chromatography)
• Protein analysis using nano-scale liquid chromatography/tandem mass spectrometry (nanoLC-MS/MS)
• Quantitative proteomic analyses using label-free, metabolic labeling (e.g. Stable Isotope Labeling by/with Amino acids in Cell culture, SILAC) and isobaring labeling (e.g. Tandem mass tag, TMT)
• Protein identification using LC-MS/MS and bioinformatics analysis using different search engines (e.g. PEAKS, Mascot, MaxQuant)
• Convenient and flexible data reporting
• Identification of post-translational modifications
• Sample analysis training using nanoLC-MS/MS for IRIC’s students and postdoctoral fellows