Affinity purification of histidine-tagged proteins |
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| Authors: | Jacky Schmitt Heike Hess Hendrik G. Stunnenberg |
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| Affiliation: | (1) Gene Expression Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany |
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| 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.Abbreviations GST glutathione S-transferase - NTA nitrilotriacetic acid - His histidine - PAGE polyacrylamide gel electrophoresis |
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| Keywords: | tagging histidine affinity purification recombinant protein nickel |
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