MilliporeSigma™ anti-Histidine-Tagged Protein Clone: 13/45/31/2,

Description

• Specifically detects Histidine-Tagged Protein Clone: 13/45/31/2 in All, Tag samples, and it is validated for ELISA, Immunofluorescence, Immunoprecipitation, Immuno Blotting Identification of proteins for which there does not exist antibodies has traditionally been overcome by the use of epitope tagging systems in which expression vectors containing an open reading frame encoding a small fragment of a specific protein (for which an antibody exists) together with multiple cloning sites are used to express foreign genes
• Several different epitope tagging systems of this type currently in use include maltose-binding-protein (MBP), glutathione S-transferase (GST), TrpE, and myc
• Tags are generally placed at either the N-or C-terminus of the protein as epitope tags placed within a coding sequence of a target protein increases the possibility of interference with the function of the protein and also decreases ability of tag-specific antibody to detect epitope tagged sequence buried by native folding of the target protein
• A second type of epitope tagging involves the addition of multiple histidine residues, usually six residues, at either the N- or C-terminus of the target protein
• Expressed proteins with such a tag may then be purified by binding to divalent metal ion columns, most commonly to chelated-Ni 2+ columns using a technique known as IMAC or immobilized metal ion chromatography
• This type of epitope tagging is particularly suited for the purification of recombinant proteins from E
• coli expression systems
• Analysis of histidine-tagged proteins by immunoblotting or immunofluorescence may also be done using an antibody to the histidine tag itself, thereby eliminating the need for an antibody specific for the protein in question.