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Webinars » A general capture and purification platform for tagless proteins based on a self-cleaving split-intein tag

A general capture and purification platform for tagless proteins based on a self-cleaving split-intein tag

In this webinar, we will present a novel capture resin that can be used to capture and purify target proteins via fusion to a 35 amino acid tag. The captured protein can be washed at pH 8.5 or higher, where the cleavage reaction is suppressed, and then rapid cleaving can be induced by a pH shift to less than 6.5. Key to the development of this technology is the introduction of pH sensitivity into the split intein and a new understanding of how the initial amino acid sequence of the target protein can be used to predict cleaving rates.

What you will learn:

  • The overall system and its application
  • Case studies, including biosimilar proteins expressed in E. coli and mammalian cells
  • Basic information on predicting cleavage efficiency based on target protein amino acid sequence


  • Speaker: David Wood, Ph.D. Associate Professor of Chemical
    and Biomolecular Engineering Ohio State University
  • Date: Weds, Dec 2nd, 2020
  • Time: 2 pm EST
  • Time:
  • Register Now

Speaker Bio

Dr. David Wood is an Associate Professor of Chemical and Biomolecular Engineering at The Ohio State University. He has worked in GMP manufacturing of Neupogen® at Amgen and downstream biologics process development at Bristol Myers Squibb. He holds two patents on intein-based technologies, one of which forms the core of his current work on disruptive innovations in downstream bioprocessing. Overall, he is considered an expert in protein purification using self-cleaving tag methods, and he is currently working to commercialize the intein technology for applications in research and ultimately commercial manufacturing.