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. 2017 Nov 23;7:16163. doi: 10.1038/s41598-017-16342-0

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Endogenous TG2 is robustly S-nitrosylated in Mouse Tissues. SNO-TG2 isolated from three separate mouse kidneys (designated as 1, 2 and 3). 10 μg samples were loaded on to each lane for immunoblot analysis. (A) 0.5% of total input (B). Proteins eluted from ascorbate treated samples (+ascorbate) = SNO-proteins. (C). Proteins eluted from untreated samples (−ascorbate) = controls. SNO-modified TG2 was eluted from thiopropyl-Sepharose beads and analyzed by immunoblots using mouse monoclonal antibody against TG2 (cub7402, ThermoFisher Scientific) as described under Materials and Methods. GAPDH, a prototypic SNO-modified protein (detected using rabbit monoclonal antibody Abcam, Ab181602) is included as a control.