Affinity purification of histidine-tagged proteins

Mol Biol Rep. 1993 Oct;18(3):223-30. doi: 10.1007/BF01674434.


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 Ni(2+)-NTA chromatography.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Chromatography, Affinity / methods
  • Evaluation Studies as Topic
  • HeLa Cells
  • Histidine / chemistry
  • Humans
  • Nickel
  • Nitrilotriacetic Acid
  • Protein Denaturation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification*


  • Recombinant Proteins
  • Histidine
  • Nickel
  • Nitrilotriacetic Acid