Recombinant protein expression and purification for therapeutic development or for in vitro studies can sometimes be a real challenge. It requires huge investments in both time and cost in order to obtain high yields of pure and active recombinant proteins. My aim in writing this post, is to give you a simple guide to easily establish optimal conditions for recombinant protein expression and production in E. Coli, of problematic unstable proteins of interest.
Decidedly, producing and purifying a protein is a form of art.
Indeed, each recombinant protein (rec. protein) to be produced in vitro has specific characteristics and singularities that make its production and purification most definitely challenging. In this post, I’d like to share and review a few tips and basics for optimal design of experiment when producing functional recombinant proteins and working on protein purification.
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