iFOLD Protein Refolding Systems

Protein functional and structural studies often require a large amount of pure, correctly folded protein, which is commonly produced in Escherichia coli (E. coli) expression systems. However, production of foreign proteins in E. coli can result in the formation of inclusion bodies (IB) — dense, insoluble, aggregates of misfolded protein. IB also have useful attributes — they are easily purified, resistant to proteolysis, and can be solubilized with chaotropic agents. Defining conditions that promote refolding of a chemically denatured protein into its native conformation is empirical and often time consuming. Simultaneous and systematic evaluation of a large number of refolding conditions increases chances of identifying an optimal refolding condition for a given protein.

We have taken the tedium and guesswork out of finding the optimal refolding condition for your target protein! Our iFOLD™ Protein Refolding Systems provide comprehensive refolding screens in a 96-well plate format and are based on an extensive literature review of successful refolding experiments and information contained in theREFOLDdatabase(http://refold.med.monash.edu.au). The systems differ in the chemistry used to denature the inclusion bodies and in the refolding additives included in the 96-well plate. In addition to a 96-well plate containing 92 (System 1) or 94 (System 2) unique refolding additive combinations, the systems include the reagents needed to purify inclusion bodies and solubilize the component proteins.