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The focus of biological research is now moving toward a systematic characterization of genes and their encoded proteins from the perspective of their expression and function in cells (proteomics). Proteomics encompasses a wide variety of experiments to determine the function and interactions of a protein of interest. Many of these experiments require large quantities of pure protein.

Recombinant protein expression in E. coli can be a powerful method for producing large quantities of protein quickly, but it also can be an exercise in frustration. Eukaryotic proteins often show low solubility, low yield, or incorrect folding in E.coli. Choice of an appropriate affinity tag, E.coli strain and growth conditions have profound implications for the success of your protein expression experiment.

This webinar will provide an introduction to E.coli protein expression, examine affinity tags and E.coli strains, and give some direction in criteria for choosing the best system for an experiment. We will review various applications for which affinity tags are often used and the associated protein purification methods. Optimization of culture growth and protein purification will be covered in detail.

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