Co-NTA Agarose 100
PureCube 100 Co-NTA Agarose
The His tag is the most widely used affinity tag due to its small size, low immunogenicity, and versatility under native or denaturing conditions, as well as in presence of detergents and many other additives. Cube Biotech introduces the novel PureCube 100 Co-NTA Agarose, based on high quality crosslinked agarose with 100 µm mean diameter, providing high flow rates in batch and FPLC applications. Due to the excellent flow properties of PureCube 100 Agarose, combined with the high capacity NTA ligand, high dynamic yield and protein purity can be achieved. Compared to Ni-NTA, Co-NTA shows higher specificity towards polyhistidines; however the affinity is lower (Fig.1). Typically, lower yields of His-tagged proteins with higher purity are obtained when Co-NTA is used. PureCube 100 Co-NTA Agarose is provided as a 50% suspension. To detect His-tagged proteins in Western Blot experiments, Cube Biotech offers the highly specific PentaHis antibody.
For purification of his-tagged proteins from cell culture supernatants or for pull-down experiments, we recommend PureCube Co-NTA MagBeads.
Why PureCube 100 Co-NTA Agarose?
- 100 µm agarose beads for high flow rates in batch and FPLC
- High purity of His-tagged protein
- Excellent recovery even with low concentrated samples
- Stable in 10 mM DTT and 1 mM EDTA. Need to use higher concentrations?
Different metal ions confer different binding affinity and specificity
Loading different metal ions to a resin results in differing affinity and specificity for a his-tagged protein. Generally, cobalt exhibits the higest binding specificity of commonly used IMAC metal ions, leading to relatively low yields but high purity. Copper, at the other end of the spectrum, has a high affinity leading to high yields but unspecific binding. In searching for the optimal resin to purify a protein, it is recommended to explore different metal ions.
Fig. 1: Affinity and specificity of metal ions commonly used for IMAC. Loading an IMAC resin with different metal ions can adjust the affinity and specificity to optimize the purity and yield of a purified protein.