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Addition of imidazole during binding improves purity of histidine-tagged proteins
The purity of histidine-tagged proteins purified by metal chelate affinity chromatography can often be improved by optimizing the imidazole concentration in the sample and binding buffer to achieve a balance between purity and yield of the protein of interest. We determined a concentration range of imidazole that minimized the nonspecific binding of untagged proteins to Ni Sepharose™ High Performance, thereby greatly improving target protein purity. We demonstrate this approach using histidine-tagged protein kinase G ([His]6-PknG) from Mycobacterium bovis.
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