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. 2018 Mar 16;8:4664. doi: 10.1038/s41598-018-22959-6

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© The Author(s) 2018

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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FL hCFTR^TS purification and activity. (A) Representative chromatograms for dephosphorylated (red) and PKA phosphorylated (blue) hCFTR^TS run over a Superose 6 10/300 SEC column as a final purification step. (B) hCFTR^TS after purification (no phosphatase or kinase treatment in lane (1), post λPP treatment in lane (2), and post PKA treatment in lane (3) was run on stain-free Bio-rad SDS-PAGE and imaged (left image). The same gel was then stained using Pro-Q Diamond Phosphoprotein Stain to confirm phosphorylation state after λPP and PKA treatment. The full-length gel images are shown in Figure S1B and C. (C) ATPase activity of purified dephosphorylated (red) and phosphorylated (blue) hCFTR^TS at 0.5 µM in the presence of 5 mM ATP was measured using the PK/LDH coupled enzyme assay.