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Ni-induced selective precipitation of His-tagged recombinant proteins shortens purification time while maintaining high yield.

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Department of Biotechnology and Life Science, Faculty of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Nakamachi, Koganei-shi, Tokyo 184-8588, Japan; Institute of Global Innovation Research, Tokyo University of Agriculture and Technology, 3-8-1 Harumi-cho, Fuchu-shi, Tokyo 183-8538, Japan. Electronic address:

Nickel-NTA affinity chromatography is the current standard method for purifying Histagged recombinant proteins. However, this process involves repetitive tasks, can be time-consuming, and reduces protein yield. Here, we present a simple, fast, and handy method for purifying His-tagged proteins using free Ni²⁺.

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