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Quantitative Protein Expression and Phosphorylation Analysis

presented by

Scott Kuzdzal
PerkinElmer Life and Analytical Sciences

April 12, 2007

BCC1 - W.M. Keck Foundation Amphitheater


Background:

Scott Kuzdzal received his Ph.D. in Analytical Chemistry in 1997 from the University of California at Riverside. He served as a postdoctoral fellow at the Johns Hopkins University School of Medicine, where he co-founded and directed the Johns Hopkins Center for Biomarker Discovery with Dr. Daniel Chan. He has extensive industrial research experience, managing the serum and membrane proteomics groups at Celera and working in a senior scientist role at PerkinElmer. He also has a strong clinical chemistry background and has directed Toxicology and Therapeutic Drug Monitoring Labs at Johns Hopkins Medical Institutions. He currently serves on the editorial review board of Proteomics and hosts the USHUPO website (USHUPO.org). He has published protein and peptide biomarkers for pancreatic cancer (HIPAP1), Alzheimer's disease and ovarian cancer using a wide variety of separation and detection methods. Scott has lectured at continuing medical education courses at Johns Hopkins Hospital, George Mason University/INOVA Fairfax Hospital and the NIH, as well as conferences worldwide. He has co-authored several proteomics book chapters and has multiple patents. Scott currently serves as a Technology Leader of Molecular Medicine for PerkinElmer.

Abstract:


  1. Quantitative protein expression from sera and cell lysates using an isobaric mass tag protein labeling technology


    A novel technology for the multiplexed analysis of proteins by tandem mass spectrometry will be described and demonstrated in several applications.The technology utilizes up to ten reactive isobaric peptides that can be covalently attached to either cysteine or lysine residues at the protein level. Thus, proteins from up to ten samples can be processed at the same time to provide large gains in productivity relative to existing quantitative methods. Furthermore, the ability to process 7 - 10 samples simultaneous enables pharmacological applications such as kinetic and dose response analyses based on protein expression from a single experiment. The quantitative capability of the technology will be demonstrated by several applications including analyzing low abundance proteins in animal sera and elucidating the kinetics of protein expression in HeLa cells following treatment with actinomycin D, an apoptosis-inducing agent.

  2. Enrichment and detection of protein phosphorylation


    Titania-based Thin-film Magnetic Beads for the Enrichment of phosphopeptides


    A titania-based enrichment technology has been developed for the selective enrichment of phosphopeptides prior to mass spectrometric analysis. The technology is suitable for the analysis of phosphorylation sites, phosphopeptide biomarkers and cell signaling events. Sensitivity to the low femtomole level from protein digests will be demonstrated. Also the high selectivity provided by the titania allows enrichment of phosphopeptides
    directly from complex biological matrices, such as cell lysates, blood plasma and sera.


    Dinuclear zinc-based phosphosensor for the detection of protein phosphorylation in gels and blots


    A novel di-nuclear zinc complex has been developed for the selective detection of phosphorylated proteins separated in gels or blots. The binding and spectral properties of the phosphosensor are distinct, allowing for a family of stains with differing spectral properties that are broadly compatible with any gel imager and/or laser scanner. Sensitivity and selectivity will be demonstrated in a number of applications including the identification of phosphoproteins from rat liver cytosol and the selective binding to an array of over 6000 phosphotyrosine peptides derived from the human proteome.

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