Meeting the Challenge of Optimizing His-tag Protein Purification, Upcoming Webinar Hosted by Xtalks

TORONTO, Oct. 15, 2020 /PRNewswire-PRWeb/ -- Expressing proteins modified with a His-tag is a very powerful and common way to efficiently purify your target molecule. The His-tag provides effective capture using Immobilized Metal-ion Affinity Chromatography (IMAC). But, as usual, not much is simple and there are challenges in the form of tagged proteins not binding and eluting as expected.

The binding can be affected by many things, such as:

• The expression system used (inclusion bodies, secretion, PTM, proteolytic cleavage)
• The length of the His-tag
• Differences in affinity for the particular metal ion bound to the chelator on the resin
• The chelator ligand itself
• Reducing agents and chelating components in the feed
• The buffer composition during binding and elution

So, even if the purification technique is simple in itself, it can be very hard to know what is wrong when no (or very little) of your target proteins are collected in your test tube. Where do you start in terms of troubleshooting? What are the signs to look for to understand what may need to be changed? How do you tackle the challenge of optimizing your His-tag protein purification method?

Our featured speaker will go through the most common challenges, give their best hints & tips for what to look out for and what you can do to solve them. She will go through some application examples and discuss methods of screening before a decision is made in regards to which set-up and purification method to move forward with.

Join Anna Heijbel, Sr Global Product Manager, Bio-Works in a live webinar on Wednesday, October 28, 2020 at 10am EDT (2pm GMT/UK).

For more information or to register for this event, visit Meeting the Challenge of Optimizing His-tag Protein Purification.

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SOURCE Xtalks