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.
Pharmaceutical, biotech and medical device industries apply restrictive quality systems in their bio-production processes. Among the numerous parameters controlled daily by scientists, I have selected a particular one for this post, i.e endotoxin detection.
Isolation of highly purified untagged proteins is crucial in today’s R&D programs. Up to now, recombinant protein production approaches were often based on the use of “tags” to make protein purification (and solubility) more convenient. Unfortunately, these tags can be real experimental hurdles in downstream applications. Protein experts are now considering “tag-free” alternatives (including outsourcing) for producing untagged proteins more rapidly, more efficiently, and without jeopardizing the rest of the research project. Let’s see how this is possible.
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