Does increasing the number of histidine residues beyond the usual six affect the ability of a protein to bind to TALON resin?

Based on Takara Bio's research with TALON resin, increasing the number of histidine residues beyond the usual six does not increase the extent of binding or yield of the tagged protein. We have also found that the use of multiple types of tags does not improve purification results.Protein purification [...]

How do the purification conditions used with TALON resin maximize biological activity more effectively than nickel-based resins?

Since his-tagged proteins bind more specifically to TALON resin than to nickel-based resins, one can use less stringent conditions for washing and elution, obtaining highly pure, natively folded protein with elution conditions that are closer to physiological. Also, since the metal chelator is tetradentate, there is very little leaching of the metal into the eluate.Protein purification [...]

How does TALON provide better purity than Ni-NTA resins?

Each TALON reactive core is complexed with a cobalt ion that has a much higher selectivity for histidine tags than nickel ions. Only proteins containing adjacent histidines or specially positioned histidines are able to bind to TALON. In contrast, the spatial requirement for nickel-based resins is less strict, so using Ni-NTA resins often results in copurification of contaminants.Protein [...]

What types of his-tagged proteins does TALON resin bind to?

TALON resin binds specifically to 6xhis-, 6xHN-, and histidine affinity tag (HAT)-tagged fusion proteins. The tag can be fused to the protein at the N- or C-terminal end of the protein. Wild-type proteins (such as histidine-rich proteins) can also be purified using TALON.Protein purification [...]

What is TALON resin?

TALON resin is an immobilized metal affinity chromatography (IMAC) resin charged with cobalt, which binds to his-tagged proteins with higher specificity than nickel-charged resins, providing exceptional purity.Protein purification [...]