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HisTrap products for purification of histidine-tagged recombinant proteins by affinity chromatography are based on Ni Sepharose media, exploiting the chelating affinity of poly-histidine for divalent metal ions. The products are available in formats ranging from bulk chromatography media and prepacked columns to magnetic beads and 96-well filter plates. Binding, washing, and elution of histidine-tagged proteins is conveniently supported by the His Buffer Kit that contains carefully prepared buffer concentrates as well as protocols for the purification of histidine-tagged proteins.

Histidine tags are widely used because they are small and rarely interfere with the function, activity, or structure of target proteins. Immobilized metal ion affinity chromatography (IMAC) is the most common method for purifying histidine-tagged proteins. IMAC media charged with divalent metal ions, such as nickel, selectively retain histidine-tagged proteins and allow for the purification of insoluble histidine-tagged proteins from inclusion bodies when denaturing conditions are used. Successful IMAC purification gives a high yield of pure and active target protein. The key to successful IMAC purification is finding the right balance of conditions for binding and elution, and to maximize yields of histidine-tagged proteins with minimum contamination from other components.