Dear Folks,

Greetings!

I would like to know:

What are the optimal expression conditions and purification strategies to obtain soluble and functionally active recombinant toxins from E. coli, and how can inclusion body formation be minimized during the process?"

This question covers:

• Expression optimization (like temperature, host strain, induction)
• Purification techniques (affinity tags, for example; 6x His tag)
• Inclusion body challenges, which are common with bacterial toxin expression.
• Kindly share your valuable inputs regarding the toxin expression in BL21 strain followed by Ni-NTA affinity chromatography column based elution.

Thanks and Regards,

ARW