Non-exhaustive list of services offered by the Bordeaux Proteome Platform. 
For other types of applications, please contact the platform manager, Caroline Tokarski.

Sample preparation for Mass Spectrometry analysis

• Electrophoretic or chromatographic separation of proteins/peptides (SDS-PAGE, 2D-PAGE, OffGel, GelFree, C18, C4, SEC, IEX, monolithic…).
• Enrichment/depletion of proteins/peptides (sera analysis, plasmas, etc.).
• Enrichment of peptide subspecies (phosphoproteomics, glycosylation…).
• Proteolysis adapted to the sample and the analysis (in gel, en solution, stratégie multi-enzymatique, échantillons à l’état de traces …).

Analysis of proteins/peptides by High Resolution Mass Spectrometry

• Identification of proteins in complex mixtures.
• Characterization of proteins: measurement of molecular mass, identification and localization of co/post-translational modifications (phosphorylation, glycosylation, ubiquitination, etc.).
• de novo sequencing (no database comparsion) de novo de protéines.
• Protein de novo sequencing
• Differential expression proteomics with labeling (SILAC, TMT) or without labeling (Label-free).

Bio-informatics data processing

• Reprocessing of mass spectrometry data for the identification, characterization and quantification of proteins using dedicated software.
• Partnership with the Bordeaux Bioinformatics Center for the analysis and integration of omics data: statistical validation, enrichment in GO terms, tools for visualization and interpretation of results, functional annotation of proteomes.

R&D expertises

• Structural analysis of proteins by isotopic exchange or cross-linking: conformational study, protein-protein interactions, epitope mapping, etc.
• Imaging by MALDI-Orbitrap mass spectrometry: identification and localization of lipids, metabolites, peptides/proteins (in situ digestion)…
• Structural analysis of proteins by isotopic exchange or cross-linking: conformational study, protein-protein interactions, epitope mapping, etc.
• Top-down proteomic analysis: identification of intact proteins and their post-translational or chemical modifications, identification of protein variants, identification of cleaved protein forms in situ.
• Analysis of glycoproteins/glycopeptides: identification and localization of N- and O-glycosylations
• Trace and ultra-trace analysis in the field of cultural heritage: identification of proteins, lipids and sugars, chemical/post-translational modifications, original biological species from different types of ancient materials.