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Welcome To The Blair Lab

We are one out of 40 member labs within the Center for Cancer Pharmacology, a Type I center, within the Department of Pharmacology.

Dr. Blair's laboratory consists of 2,000 nsf of new laboratory space on the eighth floor of the Biomedical Research Building II/III on Curie Boulevard on the University of Pennsylvania campus. The lab is equipped with four Waters 2690 Alliance HPLC and five Hitachi gradient HPLC systems (four 6200, one 7100) each fitted with Hitachi (L-4200, L-2400) UV detectors and Hitachi (D-2500) printing integrators and Autosampler 2200/EZ. Two of the Waters systems are attached to triple quadrupole mass spectrometers. There are five tandem mass spectrometers (two Thermo Finnigan TSQ Quantum Ultra, one Applied Biosystems API4000) and five LC/ion trap mass spectrometers (Thermo Finnigan LCQ classic three dimensional ion trap and LTQ linear ion trap) and one Thermo Finnigan LTQ-FT Fourier transform ion cyclotron resonance instrument. The availability of this instrumentation allows both quantitative and structural determinations to be performed in our many projects as well as offer support to other Center Investigators.

Access to additional instrumentation is available through the adjacent Proteomics Core Facility for which Dr. Blair acts as the Scientific Director. The Facility is located in 2,000 nsf also on the eighth floor of the Biomedical Research Building II/II. It is equipped with an Thermo Scientific LTQ Orbitrap-XL equipped with Waters nanoAcquity LC system; Thermo Scientific LTQ-XL equipped with Eksigent nano LC-2D; Thermo Scientific LTQ equipped with Eksigent nano LC-2D; Thermo Scientific TSQ Quantum triple quadrupole mass spectrometer equipped with Waters 2690 Series LC system.

Research in our laboratory is heavily involved in the use of mass spectrometry for proteomics, lipidomics, and DNA analysis. We are particularly interested in determining the factors that control lipid hydroperoxide-mediated damage to DNA, RNA, and proteins. Methodology is being developed to characterize covalent modifications to these macromolecules using novel mass spectrometry techniques, determining how these can be evaluated as potential “biomarkers” of various physiological processes and disease states, and assessing how such processes can be prevented using novel pharmacological agents.

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