Immobilized Metal Ion Affinity Chromatography (IMAC), developed by Porath et al (1), is based on the interaction of certain protein residues (histidines, cysteines, and to some extent tryptophans) with cations of transition metals. The Copper Chelating Resin is specifically designed for the purification of proteins that associate with copper ions (2-3), including 6x histidine tagged proteins.
Immobilized metal affinity chromatography (IMAC) resin utilizing copper (Cu2+) for the purification of 6x histidine tagged proteins.
This resin binds to six histidine residues (6x His), a common tag used in protein purification. The resin consists of iminodiacetate coupled to 6% cross-linked agarose beads. The iminodiacetate binds divalent copper ion with a capacity of 20-40μmoles Cu2+/ml resin. The protein binding capacity is >50mg protein per ml resin. We have demonstrated binding of >100mg of a 50kDa 6XHis tagged proteins to a ml of resin.
Chelating Resins are also available. Cobalt has the highest selectivity followed by Zinc, Nickel then Copper, but has the lowest loading capacity. Copper has the highest loading capacity, followed by Nickel then Zinc.
- For the purification of Copper Binding proteins, including 6x His proteins
- High capacity: >50mg/ml
- Ligand density: 20-40μmoles Cu2+ /ml resin
- Bead Structure: 6% cross-linked agarose
- Affinity purification of copper binding proteins
- Affinity purification of proteins with a 6x His tag.