beta-Synuclein Protein from Xenopus laevis: Overexpression in Escherichia coli of the GST-Tagged Protein and Production of Polyclonal Antibodies

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Zhu Yuan^1,2, Xinyu Zhao¹, Fei Yan¹, Jian Zhao¹, Huanyi Liu¹, Shaoquan Xiong¹, Jiong Li¹, Lijuan Chen^1*, and Yuquan Wei¹

¹State Key Laboratory of Biotherapy, West China Hospital, West China Medical School and College of Life Science, Sichuan University, Chengdu, Sichuan 610041, China; fax: (86) 28-8516-4060; E-mail: lijuan17@hotmail.com

²Department of Immunology, Chengdu Medical College, Chengdu, Sichuan 610083, China

^* To whom correspondence should be addressed.

Received March 12, 2007; Revision received June 8, 2007

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This report presents a procedure to obtain and purify recombinant beta-synuclein from Xenopus laevis expressed in Escherichia coli as a glutathione-S-transferase fusion protein. After identification by mass spectrometry, the protein was then used to raise anti-X. laevis beta-synuclein polyclonal antibodies, which were suitable to detect the presence of beta-synuclein in X. laevis brain by Western blot. This is the first report of a positive identification of beta-synuclein in an amphibian at the protein level.

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KEY WORDS: Xenopus laevis, beta-synuclein, Escherichia coli, beta-synuclein expression, antibody production

DOI: 10.1134/S0006297907110144

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