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. 2017 Aug 31;7:10202. doi: 10.1038/s41598-017-09725-w

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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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In vitro demonstration of LdMAPK1 mediated phosphorylation by western blot analysis. Recombinant HSP70 (A{a}) and HSP90 (B{a}) and HSP90 site directed mutants (C{a}) depicts loading controls. Prior to antibody incubations, Ponceau S staining of membrane for total protein precipitated with TCA after in vitro kinase reaction. A(b), B(b) and C(c) depicts western Blot analysis using anti-phosphoserine(pSer)/phosphothreonine(pThr)/phosphotyrosine(pTyr) monoclonal antibody (lanes 1–3). C(b) Shows western Blot analysis using anti- HSP90 polyclonal antibodies. The molecular masses (kDa) are shown on the left of (a) and (b).