6xHis has little to no effect on the structure and properties of the protein, so there is generally no need to remove the tag after purification.
Hexa-His is a peptide consisting of 6 His residues, used as a metal binding site for the recombinant protein.
Hexa His is an amino acid sequence composed of 6 histidine residues linked sequentially, also known as hexa histidine-tag, 6×His-tag or His-tag. Hexa His is responsible for the degradation of GM2 gangliosides and various terminals containing N-acetylhexosamine in the brain and other tissues. The B form is active against some oligosaccharides, while the S form has no measurable activity. Hexa His as a metal-binding site for recombinant proteins. His-Tag sequences can be added to the N-terminus or C-terminus of the target protein by using vectors provided by molecular biology companies. This tag is followed by an enzyme cleavage site that is usually a specific protease, such as the Leu-Val-Arg-Gly-Ser peptide sequence, which is recognized and cleaved by thrombin.