In addition to mass analysis of intact proteins, the Core also performs proteolytic digestions of proteins, the products of which can be further analyzed by tandem mass spectrometry (MS/MS) for peptide sequencing and interrogation of protein modifications. The Proetomics Core of the University of Kentucky has the expertise and equipment to perform sophisticated proteomic and mass spectral analysis. Please contact us to discuss your project and to determine how we can help you reach your research goal.
- Identification of unknown proteins from gel pieces or solutions
- Characterization of protein post-translational modifications and identification of the modification sites. Commonly identified modifications include phosphorylation, acetylation, methylation, and ubiquitination.
- Sample preparation including digestion of proteins in gel or solution
- Data analysis, including database searching for protein identification and protein modifications
- Analysis of intact proteins
- de novo sequence analysis of peptides using special ETD fragmentation
- Quantitative analysis using isotope-labeling and/or label-free methods
- 2D gel electrophoresis and staining (outsourced to Kendrick labs)
- 2D DIGE (outsourced to Applied Biomics)
- Gel imaging
- Gel spot cutting
Acknowledging the Core in Publications
Proteomic Core users are expected to acknowledge work done for them by the Core in any publications in which data generated in the Core is used. Please include in your publications the following statement, or a similar one:
“Mass spectrometric analysis was performed at the Proteomics Core Facility of the University of Kentucky. This core facility is supported in part by funds from the Office of the Vice President for Research.”
Also, please send us information about your publication. This information is used to ensure continued support of the Proteomics Core Facility.