Protein modifications that result in mass increases or losses to proteins are readily detectable by mass spectrometry. The facility has extensive experience with characterizing acetylation, methylation, and phosphorylation modifications. Since there are over 300 known protein modifications, the Proteomics Facility should be consulted during the design-phase of experiments in order to develop the appropriate strategy for mass spectrometric analysis of the modification. PTM analysis often requires purified protein in the amount of approximately 500 nanograms to 1 microgram.
Sample preparation involves SDS-PAGE gel electrophoresis, digestion, and desalting of gel slices. Investigators can take their samples through the complete preparation, or the proteomics staff can assist with some steps. If you choose to prepare your own gel samples, see our Tips for SDS-PAGE Gel Handling
If you are using a FHCRC project id for billing, please fill out the Internal Submission Form and submit with your sample.
If billing is to be submitted to the University of Washington or other external institution, fill out the External Submission Form and submit with your sample.
Data generated within the resource are transferred through automated pipelines to systems supported by the Hutchinson Center's Research Computing Support shared resource. Data is transferred to the user's 'fred' account, in the researcher's proteomics folder.
