The PCL specializes in the identification and characterization of individual proteins, global proteomics analysis from variety of different starting materials, targeted and global analysis of macromolecular post-translational modifications, characterization of entire protein complexes and other macromolecular interactions, protein cross linking mapping and intact protein mass analysis.
- Protein identification and characterization from different sample types using variety of proteases, separation, and mass spectrometry methods.
- Characterization of complex proteomes (e.g., serum, tissue, cell lysates).
- Global comparative proteomic quantitation using TMT, SILAC, dimethyl labeling and/or LFQ.
- Global comparative Posttranslational Modification (PTM) quantitation using TMT, SILAC, dimethyl labeling, LFQ and affinity enrichment for modifications such as phosphorylation, ubiquitination, and acetylation.
- MHC I and II peptide identification and global immunopeptidome analysis.
- Protein complex isolation and characterization.
- Identification of DNA and RNA interacting proteins by affinity purifications of nucleic acids probes followed by mass spectrometry-based identification of bound proteins.
- Protein contact mapping using mass spectrometry cleavable cross linkers.
- Intact protein analysis, protein-drug conjugate analysis.
- Analytical protein and peptide fractionation using different methods such as size exclusion chromatography (SEC), reverse phase (RP) and ion exchange (SCX).