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. 2014 Dec 30;13:179. doi: 10.1186/s12934-014-0179-z

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© Fleetwood et al.; licensee BioMed Central. 2014

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Evaluation of OmpT-mediated release and small-scale purification of displayed Affibody molecule. A. Flow-cytometric analysis for comparison of surface expression of recombinant proteins between pAraBAD-Z_IgG-EC in OmpT-negative E. coli BL21 and pAraBAD-Z_IgG-EC in OmpT-positive E. coli DH5α. B. SDS-PAGE showing IMAC-purified supernatants from pAraBAD-Z_IgG-EC in OmpT-negative E. coli BL21 and pAraBAD-Z_IgG-EC in OmpT-positive E. coli DH5α. Supernatants from non-induced samples, indicated with (−), were included as controls. C. Mass spectrum from ESI-MS analysis of IMAC-purified supernatants from pAraBAD-Z_IgG-EC in OmpT-positive E. coli DH5α. Theoretical molecular weight of the OmpT-cleaved Z_IgG-His₆ is 9712 Da. D. SPR-based biosensor analysis on the IMAC-purified Z_IgG-His₆. Response units (RU) on the y-axis and time on the x-axis. Representative sensorgrams from injection of Z_IgG-His₆ at three different concentrations over human IgG immobilized on the chip surface. Injections were performed in duplicates.