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. 2021 Oct 25;40:337. doi: 10.1186/s13046-021-02129-9

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© The Author(s) 2021

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. 7 — The interaction of TMEM44-AS1 and SerpinB3 activates Myc. (A) TMEM44-AS1 pulldown assay was performed and the associated proteins were separated with SDS-PAGE and silver staining. (B) SerpinB3 in TMEM44-AS1 RNA pulldown were analyzed by western blot. (C) Co-localization of TMEM44-AS1 and SerpinB3 in glioma cells. TMEM44-AS1 probes (red) and SerpinB3 antibody (green) were used for staining. Scale bars, 20 μm. (D-E) RNA immunoprecipitation (RIP) using the SerpinB3 antibody followed by RT-qPCR for TMEM44-AS1. (F-H) Expression of Myc and EGR1 in LN-18 and U251 cells co-transfected with TMEM44-AS1 plasmid and si-SerpinB3. **p < 0.01 vs. vector; **P < 0.01 vs. TMEM44-AS1