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. 2016 Sep 9;8(8):1598–1605. doi: 10.1080/19420862.2016.1226716

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© 2016 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 1. — The epitope of MEDI3622 is located in TACE M-domain. (A) Schematic representations of the full-length TACE/ADAM10 chimeric variants. P, M, D, C, TM, and CT stand for prodomain (which is cleaved in mature proteins), metalloproteinase domain, disintegrin-like domain, Cys-rich domain, transmembrane domain, and cytoplasmic domain, respectively. The prodomain and metalloproteinase domain of TACE were replaced with the ADAM10 counterparts to construct the variant LoF_M, and vice versa for the variant GoF_M. (B) Characterization of MEDI3622s binding to full-length TACE chimeric variants by FACS. Protein expression was monitored using anti-TACE polyclonal antibody or anti-ADAM10 monoclonal antibody. The y axis represents side scatter characteristics, and the x axis represents the mean fluorescence intensity. Mock control staining was used to set gates; numbers in gates reflect the percentage of positive cells. MEDI3622 did not bind to the variant LoF_M that encodes the ADAM10 M-domain, but recognized the variant GoF_M when grafting the TACE M-domain into ADAM10.