RE: Removal of bacterial chaperone Hsp70 contaminant from recombinant protein preparation
Dear all, I have a protein expressed at 37C for 3 hours in BL21 DE3 and purified with sub-stoichiometric amount of apparent Hsp70 contaminant even after exhaustive affinity (GST-fusion or His-tagged), ion-exchange and sizing column steps. I would like to know if you have a well-established protocol for getting rid of such a contaminant. I asked around and was told to try adding ATP at certain(?) stage of the purification. I would much appreciate your input. Many thanks! –yong @ the Wistar Institute
