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Copper Chelating Resin, High Capacity >50mg/ml, 10ml Resin, 786-285, G-BIOSCIENCES (CAT#: STEM-C-3166-LGZ)

Highlights

For the purification of Copper Binding proteins, including 6x His proteins
High capacity: >50mg/ml
Ligand density: 20-40μmoles Cu2+ /ml resin

Cat Number: STEM-C-3166-LGZ

Application: Affinity purification of copper binding proteins.<br />Affinity purification of proteins with a 6x His tag.

Model: 786-285

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Description

Immobilized metal ion affinity chromatography (IMAC) was developed by Porath et al. (1) and is based on the association of certain protein residues (histidine, cysteine and to some extent tryptophan) with the transition Interactions of metal cations. Copper chelating resins are specifically designed for the purification of proteins associated with copper ions (2-3), including 6-fold histidine-tagged proteins.

Immobilized metal affinity chromatography (IMAC) resin utilizes copper (Cu2+) to purify 6-fold histidine-tagged proteins.

This resin binds six histidine residues (6x His), a common tag used for protein purification. The resin consists of iminodiacetate coupled to 6% cross-linked agarose beads. The binding capacity of iminodiacetate to divalent copper ions is 20~40μmol Cu2+/ml resin. The protein binding capacity is 50 mg protein per ml resin. We have demonstrated the binding of 100mg of 50kDa 6XHis-tagged protein to one milliliter of resin.

Immobilized nickel, cobalt and zinc chelating resins are also available. Cobalt has the highest selectivity, followed by zinc, nickel, and copper, but has the lowest loading capacity. Copper has the highest loading capacity, followed by nickel and then zinc.

Specific binding/wash and elution buffers are available.

Specification

Size: 10ml Resin

Features

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

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