The detection, characterization, and quantification of biomolecules.
The Proteomics Facility provides a variety of proteomics analyses, as well as related protein support services. It is administered by the Center for Biomedical Research Support and the College of Pharmacy with additional support from the Cancer Prevention and Research Institute of Texas. Two state-of-the-art Thermo Orbitrap mass spectrometers (Elite and Fusion) with Dionex UPLC chromatography systems provide qualitative proteomics analyses, with Scaffold software used for data validation and visualization. Quantitative proteomics uses stable isotope labeling such as iTRAQ or TMT reagents, as well as spectral counting and peak area label free methods. Protein post-translational modifications such as phosphorylation, acetylation, methylation, oxidation, and ubiquitination are identified from the high resolution data. Associated proteolytic digest and phosphopeptide enrichment protocols are available as well. Protein molecular weight determination is conducted on the Orbitrap Fusion. Self-service instruments are available for researchers to use for IR based protein quantitation, FPLC separations, and mass spectrometry measurements, with training provided by core staff.
Core Services and Collaborative Projects:
Protein/peptide molecular weight determination by ESI or MALDI.
Protein identification by LC-MS/MS and database search for individual gel bands and complex mixtures
Relative quantitation of peptides/proteins with spectral counting, peak area, or stable isotope labeling by TMT or iTRAQ.
Protein modification analysis for phosphorylation, methylation, acetylation, ubiquitinylation, glycosylation, inhibitor binding, and chemical adduct site determination.
Self-service instrumentation available:
HPLC and FPLC (4°C)
MALDI-TOF MS molecular weight determination