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.
Small GTP-binding proteins such as Rho and Ras GTPase family members are involved in regulating cell signalling pathways and impact a wide range of cellular processes, functions, and morphology. In this post, you’ll discover two types of Small G-protein Activation Assays to easily measure the GTP-bound form of your protein of interest, as well as some tips for choosing between both solutions and finding the assays that fit best with your cell signalling experiments.
Protein biochemistry brings together a vast and varied world of methods of protein production, purification and characterization. Once you have successfully achieved the production of your protein in a selected system, you need to think about the following steps. Indeed, the quest does not stop there! The next step is purification, during which you will try to isolate your protein of interest from the surrounding contaminants while keeping it soluble and active. Your ultimate aim is to keep your protein “happy” by choosing the perfect buffer. You will be faced with a bewildering array of choices leading you to ask yourself “where do I start…?”.
Keep calm – it’s easy…
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