Protein Analysis and Identification by Mass Spectrometry
The W.M. Keck Biomedical Mass Spectrometry Laboratory within the Biomolecular Research Facility identifies and analyzes proteins and other molecules of biological interest from gels and solution using current mass spectrometry techniques. The laboratory also performs some quantitative analyses
To discuss projects, contact Dr. Nicholas Sherman 434.924.0070.
- Protein identification and sequencing from gel or solution by either peptide mass fingerprinting or ESI-LC/MS/MS at the low femtomole level (Simple mixture MS/MS service).
- Analysis of such as tissue and media (Complex mixture MS/MS service)
- protein analysis of samples prepared by Laser Capture Microdissection (GTRF)
- Proteomics, comparison of proteins in tissue samples using chemical/isotopic labels or label free analysis
- Absolute quantitation of proteins using labeled peptides and selective reaction monitoring (MRM service)
- Identification of phosphorylation sites using titanium dioxide enrichment
- Identification of post-translational modifications (e.g. ubiquitination) (de novo sequencing service/PTM service)
- De Novo (manual) sequence analysis of novel proteins to obtain sufficient sequence data for cloning
- High resolution, high mass accuracy measurements of peptides and small proteins by ESI
- Mass determination by MALDI mass measurements for confirming identity of peptides and proteins, either by staff or open access self service
- Identification of interaction partners
- Quantitative analysis of metabolites, peptides, biomarkers, small molecules by SRM
Good sample preparation is vital in getting good data. When starting a new project, read our guidelines and discuss the project with Dr. Sherman. Enter sample information into LabLink, which is where your data will be posted