ArticleMethods in molecular biology (Clifton, N.J.)2023
Poly-Histidine-Tagged Protein Purification Using Immobilized Metal Affinity Chromatography (IMAC).
Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- Preparation and Properties ofInternational journal of food science · 2026Article
- From Genetic Engineering to Preclinical Safety: A Study on Recombinant Human Interferons.International journal of molecular sciences · 2025Article
- Affinity-Based Copolymer Coating for Oriented Protein Immobilization in Biosensor Development.Biosensors · 2025Article
- Purification of SlREC2 from wild-type tomato leaflets using immunoaffinity chromatography and immunoprecipitation.Frontiers in plant science · 2025Article
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3 authors at 2 institutions in 1 country.
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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). In this chapter, we describe efficient procedures for the isolation of highly purified His-tagged target proteins from an Escherichia coli host using IMAC in a bind-wash-elute strategy that can be performed under both native and denaturing conditions.
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