概述

Immobilized Metal Ion Affinity Chromatography (IMAC), developed by Porath (1975), is based on the interaction of certain protein residues (histidines, cysteines, and to some extent tryptophans) with cations of transition metals. The Cobalt Chelating Resin is specifically designed for the purification of recombinant proteins fused to the 6 x histidine (6XHis) tag. The Cobalt Chelating Resin is specifically designed for the purification of recombinant proteins fused to the 6 x histidine (6XHis) tag expressed in bacteria, insects, and mammalian cells. The resin is high affinity and selectivity for recombinant fusion proteins that are tagged with six tandem histidine residues. Although 6 X His tagged proteins bind with a slightly lower efficiency compared to Nickel Chelating Resin there is a significant reduction in non-specific binding. The Cobalt Chelating Resin can be used to purify 6X His tagged proteins under native and denaturing conditions. Proteins bound to the resin can be eluted with low pH buffer or competition with imidazole or histidine. The Cobalt Chelating Resin uses IDA (iminodiacetic acid) as its functional ligand. The tertiary amine and carboxylic acid side chains of IDA serve as the chelating ligands for dior trivalent metal ions. The structure offers selective binding of recombinant His-tagged proteins when this resin is charged with transition metals. As a result, the desired proteins can often be purified close to homogeneity in a single step.

组分

10 ml

属性

Ligand Density:	20~40μmoles Co2+/ ml resin
Binding Capacity:	>50mg/ml resin. We have demonstrated binding of >100mg of a 50kDa 6X His tagged proteins to a ml of resin
Bead Structure:	6% cross‐linked agarose