The his-tag is a series of six to nine histidine residues generally fused to either the carboxy or amino terminus of a recombinant protein. The small size of the his-tag, compared with other common epitope tags, makes it less likely to obstruct the target protein’s structure or function and more suitable to use under denaturing conditions. The string of histidine residues binds to several types of immobilized metal ions, including nickel, cobalt and copper. The binding to metal ions under specific buffer conditions, allows for the simple purification and detection of his-tagged proteins.
His-Tag antibodies provide another dependable method for the detection and purification of tagged target proteins without a protein-specific antibody or probe. Invitrogen his-tag antibodies reliably detect recombinant his-tagged proteins. Each antibody is validated for use in applications such as ELISA, western blot, flow cytometry, immunofluorescence, immunohistochemistry, immunocytochemistry, and immunoprecipitation. Invitrogen his-tag antibodies also come with the option of being HRP, biotin or fluorophore conjugated to meet all your research needs.