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. 2017 Dec 1;7:16696. doi: 10.1038/s41598-017-16959-1

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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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Cortactin repeats and helical domain do not homo-oligomerize. (A) Schematic diagram of the defined domains of cortactin. Abbreviations: NTA, amino-terminal acidic region; H, helical domain; SH3, Src-homology 3. Cortactin repeats 1 through 6 are indicated. The cortactin regions included in constructs cortactinCR and cortactinCRH are indicated. (B) Amino acid sequence of the 6½ cortactin repeats shown. (C) SEC-MALS for cortactinCRH (green) and cortactinCR (blue). Predicted molecular masses for monomeric proteins including N-terminal vector derived residues are 36.5 kDa and 27.4 kDa for cortactinCRH and cortactinCR. SEC-MALS observed experimental molecular masses are 43.9 (±1.2%) kDa and 29.9 (±1.5%) kDa for cortactinCRH and cortactinCR, respectively.