Posts Tagged ‘chromatography’
Want to learn how to purify and refold biologically active proteins in under 90 minutes? If so, read on…
The expression and purification of recombinant proteins using e. coli as a bacterial host is quite common. One of the challenges facing recombinant protein scientists is the formation of insoluble protein aggregates known as inclusion bodies. While it is often undesirable to have insoluble protein aggregates in your lysate, inclusion bodies can offer the advantage of increased recombinant protein expression levels, easy isolation, low degradation of the expressed protein and high homogeneity of the protein of interest. Nonetheless, recovering the desired proteins from inclusion bodies can often be time consuming and difficult.
In this Bio-Rad tech note you will learn how to purify and refold bioactive proteins expressed in inclusion bodies in a single automated step.