Expression of recombinant proteins is a standard technique in molecula
r biology and a wide variety of prokaryotic as well as eukaryotic expr
ession systems are currently in use. A limiting step is often the puri
fication of the expressed recombinant protein, particularly if mammali
an expression systems that yield low expression levels are employed. H
ere, we discuss the advantages and restrictions of tagging recombinant
proteins with histidines and purifying them by Ni2+-NTA chromatograph
y.