Abstract
His-tagging is the most widespread and versatile strategy used to purify recombinant proteins for biochemical and structural studies. Recombinant DNA methods are first used to engineer the addition of a short tract of poly-histidine tag (His-tag) to the N-terminus or C-terminus of a target protein. The His-tag is then exploited to enable purification of the “tagged” protein by Immobilized Metal Affinity Chromatography (IMAC). Here, we describe efficient procedures for the isolation of highly purified His-tagged target proteins from an E. coli host using IMAC.
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Loughran, S.T., Bree, R.T., Walls, D. (2017). Purification of Polyhistidine-Tagged Proteins. In: Walls, D., Loughran, S. (eds) Protein Chromatography. Methods in Molecular Biology, vol 1485. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6412-3_14
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DOI: https://doi.org/10.1007/978-1-4939-6412-3_14
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