Description
Cambio Co-NTA MagBeads
The His tag is the most widely used affinity tag due to its small size and versatility under native and denaturing conditions, as well as in presence of detergents and many other additives. Magnetic beads are ideal for protein purification from dilute supernatants and for pull-down experiments. The agarose surface of our MagBeads is identical to that of Cambio Agarose, making them an ideal combination for small-scale screening and scale-up.
In addition to the widely used Ni-NTA MagBeads, Cambio offers high-performance Cambio Co-NTA MagBeads for purification of his-tagged proteins. Specificity of this transition metal for histidine stretches is typically higher than that of nickel (see Fig. 1). Cambio Co-NTA MagBeads are ferrimagnetic agarose beads coupled to an NTA chelating ligand, loaded with cobalt ions. Cambio Co-NTA MagBeads are delivered as a 25% suspension.
Why Cambio Co-NTA MagBeads?
- Optimal balance of yield and purity
- Low non-specific binding
- Superior DTT and EDTA stability
- Ideal for purification from dilute solutions, or pulldown experiments
- Also available as Co-NTA Agarose and prepacked cartridges
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 (Fig.1). Generally, cobalt exhibits the highest 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 chelating ligands (IDA or NTA) and different metal ions.
Figure 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
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