Affinity purification of histidine-tagged proteins

Jacky Schmitt; Heike Hess; Hendrik G. Stunnenberg

doi:10.1007/BF01674434

Affinity purification of histidine-tagged proteins

Jacky Schmitt, Heike Hess, Hendrik G. Stunnenberg

Research output: Contribution to journal › Article › peer-review

201 Citations (Scopus)

Abstract

Expression of recombinant proteins is a standard technique in molecular biology and a wide variety of prokaryotic as well as eukaryotic expression systems are currently in use. A limiting step is often the purification of the expressed recombinant protein, particularly if mammalian expression systems that yield low expression levels are employed. Here, we discuss the advantages and restrictions of tagging recombinant proteins with histidines and purifying them by Ni²⁺-NTA chromatography.

Original language	English
Pages (from-to)	223-230
Number of pages	8
Journal	Molecular Biology Reports
Volume	18
Issue number	3
DOIs	https://doi.org/10.1007/BF01674434
Publication status	Published - Oct 1993
Externally published	Yes

Keywords

affinity purification
histidine
nickel
recombinant protein
tagging

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10.1007/BF01674434

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KW - nickel

KW - recombinant protein

KW - tagging

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Affinity purification of histidine-tagged proteins

Abstract

Keywords

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