Cobalt agarose beads have a binding capacity of 6-12 mg/ml with approximately 30 kDa protein. Cobalt binds fewer host protein contaminants, resulting in lower background than nickel resins and no metal contamination in eluted histidine-tagged protein sample. In addition, it allows for purification of proteins under native or denaturing conditions. Cobalt Agarose works very well with Ni/Cu/Co Resin Wash Buffer and 6x Histidine Protein Elution Buffer.
IDA cross-linked Agarose resin consists of iminodiacetic acid groups ligated by stable ether linkages via a spacer arm. IDA is a tridentate chelating agent, covalently coupled to cross-linked agarose beads. This resin is loaded with Co2+. The resulting, ready to use resin is ideal for rapid purifications of His-tagged proteins.
Affinity Chromatography is based on the interaction between certain superficial protein residues (histidines, cysteines and to a lesser extent tryptophans), with transition metal cations, forming chelates.
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