|
The Protein Characterization Lab (PCL) uses HPLC, LC-MS, LC-MS/MS, and other tools to analyze samples. Protein Characterization is primarily focused on analysing recombinant proteins for generation of peptide maps and identification of important post-translational modifications. The Protein Characterization lab has extensive experience characterizing vitamin-K dependent proteins (such as Factor IX, prothrombin, Protein C, Factor X, Factor VII) and has also characterized recombinant proteins from E. coli and yeast fermentations. PCL has experience in characterizing the following modifications that are found in proteins:
- N-glycosylation – site occupancy, microheterogeneity, and N-glycan structure by MS and MS/MS, level of sialylation.
- O-glycosylation – site occupancy, microheterogeneity.
- Phosphorylation – LC-MS/MS confirmation of low-level phosphorylation in pure recombinant proteins and from blood plasma.
- Sulfation - LC-MS/MS confirmation of low-level phosphorylation in pure recombinant proteins.
- Gamma-carboxylation – use of CID with varying collision energy levels to determine sites of gamma-carboxylation in peptides with 3 or less Gla residues.
- Disulfide bond mapping.
- Deamidation of Asn or Gln
- Oxidation of Met and Trp
- Amino acid mutation or substitution – quantitative analysis of purified proteins produced in E. coli, where codon usage and mis-incorporation can become an issue.
|
Additionally, PCL has experience analyzing tissue homogenates, cell culture supernatants, blood plasma fractions, and other complex samples (e.g., gel slices) for protein identification applications.
|
|
Research & Development
