Nickel and copper chelate–coated plates are ideal for analyzing polyhistidine-tagged fusion proteins by ELISA-based methods. Proteins that contain a succession of several histidine residues at the amino or carboxyl terminus have a strong binding affinity for metal. Copper is less discriminating in its binding specificity than nickel, but has a higher binding capacity.
The figure above depicts coupling of a 6x histidine-tagged protein/peptide to the nickel-chelate plate. His = histidine; NiC = nickel chelate
Overview of His-tagged protein expression and purification: The DNA sequence specifying a string of six to nine histidine residues is frequently used in vectors for production of recombinant proteins. The result is expression of a recombinant protein with a 6xHis or poly-His-tag fused to its N- or C-terminus.
For Research Use Only. Not for use in diagnostic procedures.