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. 2019 Apr 15;3:11. doi: 10.1038/s41698-019-0083-4

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© The Author(s) 2019

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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Fig. 4 — Recognition by anti-PTEN mAb and functional properties of disease-associated PTEN C-terminal tail variants. a Reactivity of anti-PTEN mAb with amino acid substitutions at PTEN C-terminus found in tumors or in patients. Quantification of the reactivity is shown (mean ± s.d. from two independent experiments), as in Fig. 3c. b Summary of the reactivity of the different anti-PTEN mAb with amino acid substitutions found in tumors or in patients mutations. +, binding; +/− diminished binding; -, no binding. c Functional activity of the disease-associated PTEN variants. Data are shown as the ratio pSer473-AKT/AKT (mean ± s.d. from two independent experiments), quantified by immunoblot with anti-pSer473-AKT and anti-AKT antibodies, from lysates from COS-7 cells co-transfected with PTEN and AKT1. d Subcellular localization of disease-associated PTEN variants. Data are shown as the percentage of cells displaying cytoplasmic (C), nuclear/cytoplasmic (N/C), or nuclear (N) localization (mean ± s.d. from two independent experiments)