Scil Proteins Services has an outstanding expertise of in vitro protein refolding and of developing industrial and laboratory processes for both protein folding and purification.
In vitro protein folding. Figure taken from Dietrich et al. 2003 (PDF, 1,14 MB)
The basic principle of reactivating proteins from inclusion bodies appears conceptually simple: preparation of inclusion bodies, solubilization and subsequent folding (renaturation) of the protein. However, finding optimal conditions for refolding is a challenging task. The first matrix experiments are designed taking into account the physicochemical properties and possible disulfide bonds of the protein. Protein folding is a first-order reaction. Therefore, unspecific side reactions of higher order, i.e. aggregations, are kinetically preferred at high protein concentrations. Consequently a second and contingently a third screening round have to be performed to determine optimal protein concentrations and/or the best reduction agents such as DTT, GSH or cystein.
(PDF, 1,14 MB)
The basic principle of reactivating proteins from inclusion bodies appears conceptually simple: preparation of inclusion bodies, solubilization and subsequent folding (renaturation) of the protein. However, finding optimal conditions for refolding is a challenging task. The first matrix experiments are designed taking into account the physicochemical properties and possible disulfide bonds of the protein. Protein folding is a first-order reaction. Therefore, unspecific side reactions of higher order, i.e. aggregations, are kinetically preferred at high protein concentrations. Consequently a second and contingently a third screening round have to be performed to determine optimal protein concentrations and/or the best reduction agents such as DTT, GSH or cystein.
