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. 2019 Sep 10;9:12941. doi: 10.1038/s41598-019-49418-0

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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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(a) Representative western blots against IQGAP1 and IRS-1 in whole cell lysates, HSP90 used as loading control. Quantifications shown in graphs to the right, n = 4 independent experiments. (b) Isolated adipocytes obtained after chow or HFD-feeding of C57BL6/J mice, were pre-incubated with or without insulin (10 nM, 20 min) prior homogenization. Lysates were subjected to immunoprecipitation with anti-IQGAP1 antibody, followed by western blot analysis against IQGAP1 and IRS-1 in the immunoprecipitates. IgG used as a negative control. Quantification of total amount of IQGAP1 immunoprecipitated, and IRS-1 detected in immunoprecipitates are shown in graph to the right. n = 4 independent experiments. (c) Representative western blots against IQGAP1, p85, total and phosphorylated levels of Akt p(S473), caveolin-1 and actin in different fractions; the whole cell lysate (Lys), supernatant from the immunoprecipitation (Sup) and immunoprecipitates (IP). Quantification of IQGAP1 and p85 shown in graph to the right. Data presented as mean ± SD, *p ≤ 0.05.