The proteomics core facility at Sunnybrook Research Institute (SRI) provides kinetics analysis by surface plasmon resonance, peptide/protein fractionation and purification, and mass spectrometry-based protein identification and characterization.
We provide services and methods development for these research projects:
- Label-free differential proteomics: Proteins are fractionated (reversed phase chromatography , 2D gel, 1D gel (GeLC) or IEF), digested and identified by LC-MS/MS. Quantitative information is provided through Agilent Spectrum Mill software. View the reference.
- Differential proteomics with stable isotope labeling: Typically, two protein populations are labeled (for example, by iTraq, ICPL, SILAC) and mixed. The mixed proteins are fractionated, digested and identified by LC-MS/MS.
- Protein identification and characterization: Protein identification/characterization from silver or coomassie stain gel or from solution.
- Phospho-peptide enrichment and analysis by electron transfer dissociation MS (ETD-MS).
- Measurement of interaction kinetics by Biacore 3000.
- Sample fractionation by HPLC such as:
- size exclusion (gel filtration);
- reversed phase; and
- strong cation exchange chromatography.
- Experiment design, data interpretation and technical support in sample preparation are available.
Please contact us to discuss your projects and get pricing information.
Our services are available to internal and external users.