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
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.