Related Experiment Videos
Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain
M W Van Dyke1, M Sirito, M Sawadogo
1Department of Tumor Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030.
Gene
|February 1, 1992
Abstract:
Plasmid expression vectors have been constructed that direct the synthesis in Escherichia coli of fusion proteins containing a stretch of six histidine residues at either the N or C terminus. This oligo-histidine domain allows the single-step purification of the fusion proteins, under nondenaturing conditions, by immobilized metal affinity chromatography on Ni2+ bound to iminodiacetic acid-agarose. Several eukaryotic transcription factors (e.g., the upstream stimulatory factor for the adenovirus major late promoter) have been successfully purified, in an active state, by this method.