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. 2019 Nov 5;11(11):1729. doi: 10.3390/cancers11111729

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Validation of HMGB1-interactions: (a) Cytokeratin-7 co-immunoprecipitation with HMGB1. PC-3 lysates were immunoprecipitated with anti-HMGB1 antibody or normal mouse IgG and immunoblotted with antibodies to Cytokeratin-7 and HMGB1; complete membranes provided as Supplementary Materials Imagen S1. Protein G horseradish peroxidase (HRP)-labelled was used as a secondary antibody to minimize the signal given by the light and heavy chains of the immunoprecipitation antibody. (b) Immunofluorescent localization of HMGB1 in PC-3 cells and comparison to Hoechst-stained nuclei. (c) Immunofluorescent co-localization of HMGB1 and Cytokeratin-7 by confocal microscopy in PC-3 cells. HMGB1 is shown in green, and Cytokeratin-7 is in red. Co-localization is seen in yellow by merging. (d) Validation of interactions with HNRNPU, SRSF3, and UBC after HMGB1 immunoprecipitation and MS peptide identification.