Proteomics/Mass Spectrometry
The Mass Spectrometry Core Facility uses state-of the-art chromatography systems, mass spectrometers and workflows for the in-depth analysis of biomolecules. Our services include:
- Identification of proteins (in-gel or in-solution)
- In-depth proteome analysis (with and without fractionation)
- Interaction proteomics by Affinity Purification Mass Spectrometry (AP-MS)
- Relative quantification of peptides and proteins (label-free quantification, SILAC, dimethyl or TMT labelling)
- Post-translational modification identification (e.g. phosphorylation, ubiquitination, acetylation or glycosylation). Low stoichiometry modifications can be brought into view by enrichment (e.g. Fe-IMAC for phosphorylation)
- Crosslinking-MS (XL-MS) to extract protein structure distance information
- Hydrogen-deuterium exchange (HDX-MS) to uncover interaction interfaces
- Intact mass of proteins and other biomolecules (Topdown-MS)
