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Cobalt Chelating Resin, 0.2ml Spin Column, High Capacity >50mg/ml, 25 Columns, 786-454, G-BIOSCIENCES (CAT#: STEM-C-3162-LGZ)

Highlights

For the purification of Cobalt Binding proteins, including 6x His proteins
High capacity: >50mg/ml
Ligand density: 20-40μmoles Co2+ /ml resin

Cat Number: STEM-C-3162-LGZ

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

Model: 786-454

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Description

Immobilized metal ion affinity chromatography (IMAC) was developed by Porath (1) and is based on the association of certain protein residues (histidine, cysteine and to some extent tryptophan) with transition metals cation interactions.

Cobalt chelating resins are specifically designed for the purification of proteins associated with cobalt ions, including 6-fold histidine-tagged proteins. Although the binding efficiency of 6 X His-tagged proteins is slightly lower than that of nickel chelating resins, non-specific binding is significantly reduced. Cobalt resins have high selectivity for poly-His sequences, but low loading capacity, so cobalt chelating resins are used for valuable recombinant proteins, and the quantity is limited.

Immobilized metal affinity chromatography (IMAC) resin utilizes cobalt (Co2+) 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 iminodiacetic acid and divalent cobalt ions is 20~40μmol Co2+/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.

The resin bed volumes of the spin columns were 0.2, 1 and 3 ml, respectively, and the total column volumes were 1, 8 and 22 ml, respectively. The column is available as a spin format for gravity flow columns.

Immobilized nickel, copper 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.

Our new HOOK™ 6X His Protein Purification Kit is now available and includes everything needed to purify 6X His-tagged proteins from yeast or bacteria, including lysis buffer, lysing enzyme, resin, column and binding, wash and elution buffers . Each kit is available with nickel or cobalt chelate resins. Available kits are:

HOOK™ 6X His Protein Purification (Bacteria): Isolated from bacteria; optimized to produce up to 10mg/250ml of soluble 6X His-tagged protein.
HOOK™ 6X His Protein Spin Purification (Bacteria): Isolation from bacteria; optimized to produce ~1mg/50ml of soluble 6X His-tagged protein culture
HOOK™ 6X His Protein Purification (Yeast): Isolated from yeast; optimized to yield up to 10 mg of soluble 6X His-tagged protein.
HOOK™ 6X His Protein Spin Purification (Yeast): Isolated from yeast; optimized to yield up to 1 mg of soluble 6X His-tagged protein.

Specification

Size: 25 columns

Features

For the purification of Cobalt Binding proteins, including 6x His proteins
High capacity: >50mg/ml
Ligand density: 20-40μmoles Co2+ /ml resin
Bead Structure: 6% cross-linked agarose

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