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 immobilised metal affinity chromatography (IMAC). Here, we describe efficient procedures for the isolation of highly purified His-tagged target proteins from an Escherichia coli host using IMAC.
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Loughran, S.T., Walls, D. (2011). Purification of Poly-Histidine-Tagged Proteins. In: Walls, D., Loughran, S. (eds) Protein Chromatography. Methods in Molecular Biology, vol 681. Humana Press. https://doi.org/10.1007/978-1-60761-913-0_17
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DOI: https://doi.org/10.1007/978-1-60761-913-0_17
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