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