Where You Are:


Main Phone: 813-745-1192

Scientific Director:
John Koomen, PhD

Staff Scientists:
Robert Sprung, PhD - Identification & Quantification

Bin Fang, PhD - Post-Translational Modification


The Proteomics Core Facility helps to design experiments, performs the necessary analyses, and provides interpreted results and publication-quality figures for users.

The Core provides all research needs for targeted protein identification and functional investigations, including separations and mass spectrometry.

For post-translational modification analysis, the goal is to target specific sites in each protein and to obtain information about the presence or absence of the modification in all submitted samples.

For clinical and translational research, the goal is to direct the research to meaningful segments of the proteome, such as phosphoproteins or ubiquitinated proteins, and to conduct research based on protein identification for finding novel candidate biomarkers.

The majority of work performed within the Core involves:

Protein Separations

  • Protein: SDS-PAGE, HPLC, isoelectric focusing, immunodepletion, size exclusion, ultrafiltration
  • Peptide: HPLC separation (reverse-phase, strong cation exchange), isoelectric focusing, titanium dioxide/IMAC, antibody capture for phosphotyrosine profiling

 Mass Spectrometry

  • MALDI MS & MS/MS for mass analysis, protein identification, LC-MALDI
  • LC-MS/MS for protein ID, PTM analysis, and quantification
  • LC-MRM for targeted peptide detection as well as quantification of expression and modification

Peptide Synthesis
Peptide synthesis is performed at the 20 micromole scale to support quantitative mass spectrometry and for other needs of Moffitt investigators. In addition to standard peptides, the Core synthesizes stable isotope-labeled peptides and post-translationally modified peptides according to the needs of the project.

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