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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recording and the presentation.