Epitope tagging is the procedure of inserting a short amino acid sequence into a protein within an expression vector via genetic engineering and it is a widely used technique in proteomics and various other biological sciences. The sequence of the tag is engineered using recombinant DNA technology, and grafted into the protein of interest by placing the encoded sequence of the epitope into a matching open reading frame. The antibody generated against this engineered epitope can recognize it, thereby enabling the tagged protein to be isolated, purified and visualized/analyzed by immunodetection methods. In other words, epitope tags represents an artificial epitope that is recognized by a common antibody and the antibodies recognizing a tag are useful for detecting proteins with low immunogenicity. 6-Histidine or H-H-H-H-H-H motif is used as a tag on many recombinant proteins to facilitate their purification and detection. Our 6-Histidine Epitope Tag antibody recognizes the His-tag fused to the amino- or carboxy- termini of targeted proteins in transfected or transformed cells, and is useful for Western blot, IHC- paraffin embedded on frozen sections, ELISA, FLOW Cytometry and Immunoprecipitation applications.