Immobilized Metal Ion Affinity Chromatography (IMAC), developed by Porath (1), is based on the interaction of certain protein residues (histidines, cysteines, and to some extent tryptophans) with cations of transition metals. The Zinc Chelating Resin is specifically designed for the purification of proteins that associate with Zinc ions (2-3), including 6x histidine tagged proteins.
Immobilized metal affinity chromatography (IMAC) resin utilizing zinc (Zn2+) 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 zinc ion with a capacity of 20-40μmoles Zn2+/ml resin. The protein binding capacity is >20mg protein per ml resin. We have demonstrated binding of >40mg 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 Zinc Binding proteins, including 6x His proteins
- High capacity: >20mg/ml
- Ligand density: 20-40μmoles Zn2+ /ml resin
- Bead Structure: 6% cross-linked agarose
- Affinity purification of zinc binding proteins
- Affinity purification of proteins with a 6x His tag.