Beta-synuclein protein from Xenopus laevis: overexpression in Escherichia coli of the GST-tagged protein and production of polyclonal antibodies

Abstract

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.