Proteomics

Proteomics

Proteomic analyses tend to be complex. Prior to sample submission, we recommend contacting us to discuss details on experimental design and sample preparation as well as data analysis strategies.

The Proteomics Core Unit provides consulting and state-of-the-art technologies for peptide and protein

  • identification
  • characterization
  • quantification

Analysis methods include

  • Peptide and recombinant protein molecular weight determination
  • Protein identification
  • Mapping of post-translational protein modifications
  • Multidimensional protein and peptide separation
  • Relative protein quantification

We are using the following methods and equipment

  • Nano LC-MS/MS (LTQ-Orbitrap)
  • Q-Tof Impact HD II
  • Micro/Capillary-High Performance Liquid Chromatography (HPLC)
  • Isoelectric Focusing (IEF)
  • One dimensional SDS-Polyacrylamide Gel Electrophoresis (1D SDS-PAGE)
  • Two-dimensional Polyacrylamide Gel Electrophoresis (2D-PAGE)

Samples are processed from a variety of species and include

  • Cellular extracts
  • Tissue extracts
  • Plasma
  • Immunoprecipitates

Sample preparation for mass spectrometry-based proteomic analysis

original
  • Protein fractionation by 1D SDS-PAGE or 2D-PAGE followed by Coomassie staining and in-gel digestion
  • Peptide fractionation by IEF
  • Protein and peptide fractionation by micro- and capillary-liquid chromatography

Mass spectrometry analysis

original
  • Molecular weight determination of synthetic peptides and recombinant proteins
  • Protein/peptide identification from in-gel digests
  • Multidimensional protein and peptide separations (2D-PAGE, IEF/LC, LC/LC)
  • Characterization and mapping of post-translational protein modifications (e.g., phosphorylation, ubiquitination, acetylation)
  • Relative protein quantification (label free, gel-based, chemical labeling, metabolic labeling)
  • Targeted protein/peptide quantification
Go to Editor View