Broadcast Date: October 2nd, 2014
Time: 11 AM EDT, 8 AM PDT

Omics analyses, including proteomic and lipidomic studies of cell extracts or liquid biopsies, can yield information enabling novel discoveries ranging from biomarker identification and vaccine development to forensics and drug discovery.

However, without careful sample preparation and analysis, omic’s data can be misleading as biological samples can contain confounding components such as abundant proteins, salts, and detergents. This webinar will focus on improved techniques for preparing and analyzing samples for proteomic and lipidomic studies.

Webinar panelists will discuss novel strategies for sample extraction, fractionation, depletion and enrichment, including the use of infrared-based spectrometry to simultaneously monitor total protein and lipid content during sample preparation. Use of a novel instrument, the Direct Detect® spectrometer, to exploit IR-based protein quantitation for complex biological samples will also be presented. The development and use of pressure cycling technology as a novel means of controlling biomolecular interactions during sample preparation will also be discussed as will development of a technology platform for enhancing protein therapeutics through selective modification.

Who Should Attend

  • Proteomics researchers
  • Biochemists analyzing protein structure and function relationships
  • Biomarker assay technicians
  • Biomarker discovery scientists
  • Drug development scientists
  • Lipid biochemists

You Will Learn

  • Improved techniques for tackling the complexity of biological samples to improve reproducibility and signal-to-noise ratios in proteomic analyses.
  • Strategies for sample preparation that are optimized for the chosen downstream analytical method, such as mass spectrometry or immunoassays.
  • How the Direct Detect® Spectrometer uses IR-based quantitation to measure total protein and analyze lipid content using a single measurement, requiring only 2 μL of sample per analysis.
  • That IR-based protein quantitation is compatible with detergents, reducing agents, and other buffer components that interfere with traditional protein quantitation assays.

Produced with support from:

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Panelists

Alexander Lazarev, Ph.D.
Vice President of Research and Development,
Pressure BioSciences

Ivona Strug, Ph.D.,
Senior Biochemical Scientist,
EMD Millipore