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Updated: Jun 1, 2026

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Expression, Isolation, and Purification of Soluble and Insoluble Biotinylated Proteins for Nerve Tissue Regeneration
Published on: January 22, 2014
Production of a recombinant full-length prion protein in a soluble form without refolding or detergents
Yasuhiro Arii1, Satoshi Oshiro, Keita Wada
1Department of Food Science and Nutrition, Mukogawa Women's University, Nishinomiya, Hyogo, Japan. arii@mukogawa-u.ac.jp
Bioscience, Biotechnology, and Biochemistry
|June 15, 2011
Abstract:
Recombinant prion protein has been produced in insoluble form and refolded following solubilization with denaturants. It is, however, preferable to use a soluble recombinant protein prepared without artificial solubilization. In this study, a soluble recombinant prion protein was produced in Escherichia coli cells by coexpression of neuregulin I-β1 and purified to high purity.

