Mass Spectrometry and Proteomics Shared Facility
Co-Directors: Stephen Barnes, PhD and Helen Kim, PhD
Department/Center Association: Department of Pharmacology and Toxicology, Comprehensive Cancer Center (CCC), Center for Nutrient -Gene Interaction (CNGI), Purdue-UAB Botanicals Center (PUBC), and Skin Disease Research Center (SDRC)
Established: 1993

Mission
The goal of this facility is to provide state of the art technology and education in mass spectrometry and proteomics to the UAB research community, to support ongoing research efforts, and to enhance capabilities for obtaining future extramural funds.

Facility Description
The Mass Spectrometry and Proteomics Shared Facility is located on the 4th floor in the McCallum Building, 1918 University Boulevard. Funds for the operation of the Mass Spectrometry Shared Facility come in part from the UAB CCC P30 Grant, the U54 CNGI, the P50 PUBC for Age-related Disease, and the P30 SDRC.

The MASS SPECTROMETRY component has instrumentation that enables the following types of analysis:

• Tentative identification of a parent polypeptide (in a gel band or spot, for example) from internet database searching using the tryptic peptide fingerprint generated by matrix-assisted laser desorption ionization mass spectrometry (MALDI-TOF-MS);
  
• Tentative identification of a protein modification such as phosphorylation or sulfation;
  
• Conclusive identification of a polypeptide, peptide, or peptide modification by sequence analysis via quadrupole time of flight mass spectrometry (QTOF MS);
  
• HPLC analysis of mixtures of small compounds such as pharmaceuticals, specific dietary supplements, or extracts of plants (LC-MS); and
  
• Nano-liquid chromatography mass spectrometry to study protein composition in very dilute or precious samples (nano-LC-MS).
  
  

The PROTEOMICS component offers the following types of services:

• Biological sample workup for 1- or 2-dimensional gel electrophoresis;
  
• One and two-dimensional gel electrophoresis, typically isoelectric focusing in the first dimension, followed by the standard SDS-polyacrylamide gel electrophoresis in the second dimension;
  
• 2D gel staining with Coomassie Brilliant blue, silver staining, or fluorescent Sypro Ruby;
  
• Software-assisted 2D gel image analysis for quantitative analysis of protein differential expression, and/or alterations in protein modifications; and
  
• Robotic gel spot excision and ingel digestion to generate samples for mass spectrometry analysis.
  

The above proteomics analysis is offered on mini gels, microtiter plate-size gels, or maxi gels (23x20 cm). Any size gel generated by an individual lab can be processed, however.

Additional Information
Mass spectrometers and robotic and automated instrumentation for proteomics have been awarded to Drs. Kim and Barnes. The proteomics instrumentation was added to the Shared Facility in Spring, 2003. Installation and operation of the fourier transform-ion cyclotron resonance mass spectrometer (FT-ICR-MS) is expected by Spring, 2005. This instrument will be available to current NIH investigators.

Services and Fees
The CCC, CNGI, PUBC and SDRC NIH grants provide partial support for personnel in the facility. The remaining salary support, as well as the running costs of supplies and equipment maintenance, comes from charges made for the various services. These are detailed on the facility website: http://www.uab.edu/proteomics. CCC, CNGI, PUBC and SDRC members have priority for the services over other members of the UAB community, although there is no difference in the charges. There are proportionately higher charges for services for non-UAB academic institutions and for industry customers. These are also on the website. All charges are subject to revision, as the facility undergoes modification of personnel or services.

Contact Information
Co-Directors: Stephen Barnes, PhD and Helen Kim, PhD
Emails: sbarnes@uab.edu, helenkim@uab.edu
Phones: 205-934-7117, 205-934-3880

Website: http://www.uab.edu/proteomics

Click here to return to the SOM Research Web Site's home page.