Abstract
Tamavidin 2 is a fungal avidin-like protein that binds biotin with high affinity. Unlike avidin or streptavidin, tamavidin 2 in soluble form is produced at high levels in Escherichia coli. In this chapter, we describe a method for immobilization and purification of recombinant proteins with the use of tamavidin 2 as an affinity tag. The protein fused to tamavidin 2 is tightly immobilized and simultaneously purified on biotinylated magnetic microbeads without loss of activity.
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The authors thank Dr. Toshihiko Komari for critical reading of the manuscript.
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Takakura, Y., Oka, N., Tsunashima, M. (2014). Expression, Purification, and Immobilization of Recombinant Tamavidin 2 Fusion Proteins. In: Giannone, R., Dykstra, A. (eds) Protein Affinity Tags. Methods in Molecular Biology, vol 1177. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-1034-2_8
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DOI: https://doi.org/10.1007/978-1-4939-1034-2_8
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