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. 2016 Sep 9;6:33149. doi: 10.1038/srep33149

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Copyright © 2016, The Author(s)

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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The culture media from tcHGF-PA (tc), scHGF(Xa)-PA (sc), or mock (m)-transfected HEK293T cells were immunoprecipitated with either t8E4, t1E4, or NZ-1, followed by the SDS-PAGE and Coomassie staining. The wild-type HGF protein was fully converted into two-chain species because of the cleavage by serum-derived protease during the expression, while the engineered “Xa” version remained as single chain species under the same condition. Because of the non-reducing condition employed here, however, both proteins migrated as an ~75-kDa band (arrowhead).