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. 2013 Jul 1;14:15. doi: 10.1186/1471-2091-14-15

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Copyright © 2013 Bozzi et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Purification of the recombinant α-DG mucin-like domain, α-DG(316–484). α-DG-DG(316–484) purification steps were analysed by 12% SDS-PAGE stained with Coomassie Brilliant Blue R-250 dye. Lane 1, overall cell lysate from E. coli expressing the chimaeric protein Trx-α-DG(316–484); lane 2, purified Trx-α-DG(316–484); lane 3, Trx-α-DG(316–484) upon thrombin cleavage: two upper bands referring to α-DG peptides plus a lower band of Trx are observable; lane 4, purified and concentrated α-DG(316–484). The lower band refers to a processed α-DG(316–461) product that has been characterized by mass spectrometry.