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Despite the fact that more than two-thirds of recombinant biopharmaceutical products are glycoproteins, few advances in glycan analytics have been  developed that have made meaningful improvements to how therapeutic  protein glycosylation is studied. Regulatory agencies worldwide require state-of-the-art glycan analyses and the demands placed on these methods seem to be ever increasing. Ultimately, it is necessary to present robust, reproducible, and information-rich methods for glycan analysis in regulatory filings for  glycoprotein-based biotherapeutics.

In this GEN webinar, Matthew Lauber, Ph.D., Principal Applications Chemist  for Waters, will present on innovative sample preparation and LC-based  separation techniques for the qualitative and quantitative characterization  of protein glycosylation at varying levels of analysis, including intact protein, protein subunits, glycopeptides, and released glycans.

Dr. Lauber will describe a streamlined released N-glycan sample-preparation workflow utilizing the new GlycoWorks™ RapiFluor-MS™ N-Glycan Kit.  Additionally, he will share new developments for hydrophilic interaction  chromatography (HILIC) that make it possible to perform complementary  analyses of glycans while they are still attached to their counterpart protein  residues. Case studies will be shown that use an optimized stationary phase found in ACQUITY UPLC® Glycoprotein BEH Amide columns to resolve the  glycoforms of intact and digested glycoproteins. It is hoped that the presented information will assist investigators in selecting the appropriate techniques to address the analytical challenges posed by biotherapeutic protein glycosylation.

Who Should Attend

  • Biochemists
  • Researchers interested in novel chromatography methods
  • Biopharmaceutical and therapeutic protein developers
  • Scientists developing biopharmaceutical analytical workflows
  • QC/QA scientists manufacturing biotherapeutic proteins
  • Protein analytical scientists interested in glycan analysis

You Will Learn

  • About a new wide-pore (300Å) amide-bonded, organo silica stationary phase found in ACQUITY UPLC® Glycoprotein BEH Amide Columns.
  • How to develop methods to achieve unprecedented separations of intact and digested protein glycoforms.
  • How to take better advantage of HILIC to provide complementary data for a wide variety of techniques.
  • Details of the three streamlined steps in the GlycoWorks™ RapiFluor-MS™ N-Glycan Kit that accelerate released glycan preparations and yield extraordinary sensitivity.

Produced with support from:

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Matthew A. Lauber, Ph.D.
Principal Applications Chemist,
Waters Corporation