The most economical way to produce the mg quantities of purified protein required by many studies still requires expression in E. coli. Unfortunately, between 50% and 70% the time, a given protein will not express properly in bacteria. Of those that are correctly folded, a percentage of them will either lose activity during purification or cold storage once purified. To overcome these obstacles we have begun using high hydrostatic pressure refolding (Barofold) which allows us to refold protein at high concentration (1 mg/ml or higher) without adding and removing chaotropic agents.
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