Developing a Robust Affinity Tag Platform Using Engineered Streptavidin

The affinity chromatography technique is one of the most specific and therefore most efficient methods of purifying proteins. But protein-based affinity resins are usually more expensive due to more costly development and production. In order to reduce these costs, the resin must be reusable, and its longevity may be increased through efficient cleaning. Harsh clean-in-place (CIP) procedures, however, require that the resin be stable over a wide range of pH and temperature, as well as be compatible with various buffer conditions. These requirements have guided the further development of the Strep-tag technology — a new affinity tag system that takes advantage of the strong interaction between streptavidin and biotin.

During this webinar, attendees will learn how Strep-Tactin®, a modified streptavidin variant, was further developed into Strep-Tactin®XT, a high-affinity variant with extraordinary stability. The biotin binding pocket of the former Streptavidin derivative was modified to enhance durability and even resist extensive and repeated CIP procedures. The high-affinity successor resin has a picomolar binding strength that allows specific protein capture and simple elution. As a result, the enhanced variant is an excellent product for bioprocessing.

Register for this webinar to learn more about a robust affinity tag platform for protein purification and bioprocessing needs.

Speaker

Fabian Mohr, Vice President Research & Development, IBA Lifesciences

Fabian Mohr received his master’s degree in biology from the Technical Univ. of Munich. During his PhD thesis he worked on the isolation of minimally manipulated regulatory T cells for adoptive T-cell therapy. In 2019, Fabian Mohr joined IBA Lifesciences. He currently works as Vice President R&D and is responsible for product & technology innovation.

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