Metal Affinity Chromatography Resins

Metal affinity chromatography is a variant of affinity chromatography designed to separate proteins or peptides according to their affinity to metal ions immobilized on a resin. The resins, which make up a column's stationary phase, contain metals such as Zn2+, Cu2+, Cd2+, Hg2+, Co2+, Ni2+, and Fe2+. This technique is commonly used to purify recombinant proteins with metal-chelating residues, such as histidine, tryptophan, and cysteine. Bound proteins can be subsequently eluted by altering the pH or ionic strength of the mobile phase. Browse for various metal affinity resins below and visit the supplier page for more information.