Protein expression in E. coli: Overcoming the solubility hurdle
Expression of recombinant proteins using the bacterium Escherichia coli is still the most widely used method to produce purified proteins for functional studies. Despite its ease of use, expression in E. coli sometimes poses problems, such as toxicity, protein folding and solubility issues. Small protein tags like the LYTAG included in the new DUALXPress kit help to overcome solubility issues: the LYTAG is added to the protein of interest and dramatically enhances the solubility of the fusion protein, which is then easily purified to high purity using the dualTRAP resin. After a single round of purification, the protein can be immediately used for downstream assays.
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