| Literature DB >> 27730558 |
Sinéad T Loughran1, Ronan T Bree2, Dermot Walls3,4.
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.Entities:
Keywords: 6×Histidine; Affinity chromatography; IMAC; Ni-NTA; Polyhistidine; Protein purification
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Year: 2017 PMID： 27730558 DOI： 10.1007/978-1-4939-6412-3_14
Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745