OCT 30, 2018 10:00 AM PDT
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Post-translational Modifications and Data-Independent Acquisitions - Challenges and Opportunities

SPONSORED BY: Cell Signaling Technology
C.E. CREDITS: P.A.C.E. CE | Florida CE
Speakers
  • Assistant Professor, Buck Institute for Research on Aging, Director of the Mass Spectrometry Core, Buck Institute; Adjunct Professor, USC.
    Biography
      I am a Research Associate Professor with an independent laboratory and the Director of the Mass Spectrometry Core at the Buck Institute for Research on Aging. I am especially interested in protein chemistry and modern mass spectrometric technologies to advance the field of Proteomics mainly in the context of Aging Research. I am directly involved in a large variety of research projects (spanning neurodegenerative diseases, cancer, diabetes, mitochondrial damage, molecular mechanisms of aging, protein posttranslational modifications, bacterial pathogenesis etc.), and in mass spectrometric method development that will benefit biological projects. To date this work has resulted in 99 peer-reviewed publications. Several research projects include investigation of protein phosphorylation, glycosylation, acetylation, succinylation and other posttranslational modifications, as well as differential expression of proteins during disease and aging processes. I have collaborated on several projects specifically investigating mitochondrial acetylation and succinylation - and I have been working on different phosphorylation projects using various affinity enrichment strategies.

    Abstract:
    DATE: October 30, 2018
    TIME: 10:00am PT, 1:00pm ET
     
    Identification and quantification of post-translational modifications (PTM) presents a unique challenge to proteomic studies. Often PTMs feature low abundances and many possible functionally-distinct locations may exist within each protein. Although label-free data independent acquisitions (DIA or SWATH®Acquisition) have been extensively used for global proteomics workflows and quantification of proteins, so far there are only few studies applying DIA to study post-translational modifications. Here, we present several DIA-PTM studies, specifically of phosphorylated as well as acylated proteins using different affinity enrichment approaches. We are specifically using Cell Signaling Technology affinity enrichment kits for our work (PTMScan® affinity enrichment kits for acetylation/succinylation and PTMScan® Direct Tyrosine and Serine/Threonine Kinases Reagents).
     
    In this webinar you will learn:
    • Use of simultaneous affinity enrichment workflows by combining different PTM antibodies for ‘one-pot enrichment’ approaches
    • Relevance of assessing protein PTM isoforms based on PTM site localization
    • Applications involving stable isotope labeled PTM-peptides

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