A modified metal-ion affinity chromatography procedure for the purification of histidine-tagged recombinant proteins expressed in Drosophila S2 cells.

@article{Lehr2000AMM,
  title={A modified metal-ion affinity chromatography procedure for the purification of histidine-tagged recombinant proteins expressed in Drosophila S2 cells.},
  author={Ruth Lehr and Louis C Elefante and Kristine K Kikly and Stephen P. O'Brien and Robert B. Kirkpatrick},
  journal={Protein expression and purification},
  year={2000},
  volume={19 3},
  pages={362-8}
}
We have developed a modified method of immobilized metal-ion affinity chromatography (IMAC) that can be used for the purification of histidine-tagged proteins from conditioned medium containing free copper ions. Classical methods of IMAC purification, using resins such as Ni-NTA, have proven inefficient for this type of purification and require multiple… CONTINUE READING