His Tag-Binding Plates

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

His tag binding plate types

Nickel coated

  • Pierce Nickel Coated Plates—These Ni(2+) 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. Bacterial lysates containing polyhistidine-tagged fusion proteins can be added directly to the plates without the need for blocking.

Copper coated

  • Pierce Copper Coated High Capacity Plates—These copper-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 metals such as copper.

    Thermo Scientific Pierce Copper Coated Plates have high binding capacity because they are coated using an exclusive process that increases the amount of histidine-tagged protein that will bind to the plate surface. Although copper is less discriminating in its binding specificity than nickel, the higher binding capacity of these plates is ideal for high-throughput screening applications that need improved sensitivity and greater dynamic range.

    Our copper-coated plates are available as clear, white, or black plates that can be used with colorimetric, chemiluminescent, or fluorescent detection methods, respectively. Copper coated plates are for use with purified His-tagged proteins. Typical cell lysates contain non–his-tagged proteins that may bind to copper, which can reduce binding capacity and signal-to-noise ratios. For cell lysates, use Pierce Nickel Coated Plates.

Related categories

His-tagged Proteins – Production and Purification

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.