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. 2022 Dec 1;22:376. doi: 10.1186/s12935-022-02799-1

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Pull-down of GST-APC^2539–2772 containing the EB1 domain. GST-APC^2539–2772 was tested against the following MBP-tagged proteins: JUN^100–331 (lane 1), JUN^FL (lane 2), FOSL1^40–282 (lane 3), TCF7^152–359 (lane 4), TCF7^FL (lane 5), and MBP alone (negative control; lane 6). The signal of MBP alone in all the samples (lanes 1–5) represents the binding of cleaved MBP protein to the amylose resin, likely resulting from leaky expression or cleavage during purification. The TCF7^152–359 and TCF7^FL constructs show fragmentation represented by multiple bands below the expected target protein. An arrow indicates the expected molecular weight of the target protein/fragment (green signal GST; red signal MBP)