North Dakota INBRE

Proteomics is a cutting-edge technology that examines the entire protein complement (proteome) or sub-proteome of a species related to its healthy and abnormal states. Since its introduction in the early 1990s, proteomics has become a core technology in life science, assisting researchers in understanding signal transduction, discovering biomarkers and identifying targets for new drugs.

The INBRE Proteomics Core Facility was opened in the spring of 2003. It's current suite of instruments enables high-throughput protein identification and quantitation for discovery applications.

This facility provides investigators both inside and outside INBRE with instrumentation, expertise and training. It functions as a technical platform that helps develop a highly interactive and collaborative biomedical research group, and increases the competitiveness of the investigators through the services and the research resources of the core facility.

The facility also provides undergraduate students, graduate students and post-doctoral fellows in the state with the opportunity to learn advanced proteomics technology.

Personnel

Core Director
John B. Shabb, Ph.D.
Associate Professor
Department of Biochemistry and Molecular Biology
University of North Dakota School of Medicine & Sciences
501 Columbia Road North
Grand Forks, ND 58203
Office phone: (701) 777-4946
Departmental FAX: (701) 777-2385
jshabb@medicine.nodak.edu

Research Specialist
Wallace W. Muhonen, M.S.
Department of Biochemistry and Molecular Biology
Room 3568
Office phone: (701) 777-0674
muhonen@medicine.nodak.edu

Instrumentation

• Applied Biosystems/MD SCIEX 4800 MALDI TOF/TOF
  This instrument is designed for high throughput protein/peptide identification and quantitation.
• Applied Biosystems LC TEMPO MALDI
  An integrated nanoflow HPLC/automated spotter designed to complement the ABI 4800 for separation and analysis of complex peptide mixtures.
• Agilent 1100 nanoflow HPLC
  In combination with the LC TEMPO MALDI provides capabilities for multi-dimensional LC/MS/MS
• Shimadzu preparative HPLC
  Useful for large-scale fractionation of complex protein mixtures
• Useful for large-scale fractionation of complex protein mixtures
  Protein database search software for peptide and protein identification

Here are examples of sample types that have been analyzed to date:

• Accurate mass determination of synthetic peptides.
• Identification of interacting proteins isolated by affinity chromatography and separated by SDS polyacrylamide gel electrophoresis
• Identification of sites of post-translational modifications in recombinant proteins, including acetylation and phosphorylation.

Projects under development:

• Characterization of post-translational modifications in native integral membrane proteins
• Profiling of defined biomarkers in biological fluids

The Proteomics Core is equipped with reagents and small equipment for 2D-electrophoresis. This resource is available to individual users with approval from the Core Director. The facility also is equipped for in-gel and in-solution sample preparation.

Costs & Acknowledgements

Costs:
The Proteomics Core does not currently charge fees for service. This will likely change as the Proteomics Core seeks to establish sustainable practices through establishment of a cost center. In the meantime, projects that receive the highest priority are those that will generate critical preliminary data for extramural grant applications.

Other projects:
Investigators who wish to include mass spectrometry in future research plans must consult with the Core Director so that costs associated with proteomics aims are adequately incorporated into future budgets.

Co-authorship and acknowledgement of support:
Co-authorship of research articles involving Core-generated data will be determined between individual investigators and the Core Director. All research papers that include the use of data generated by the Proteomics Core will include the following acknowledgement: The University of North Dakota Proteomics Core (JBS, WWM) is supported by NIH grant number P20 RR016741 from the INBRE program of the National Center for Research Resources.