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. 2021 Apr 6;12(4):351. doi: 10.1038/s41419-021-03595-x

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© The Author(s) 2021

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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Fig. 4 — A The mRNA and protein levels for SOCS2 after SOCS2-AS1 overexpression or knockdown. B RNA FISH in HEC-1A cells showed that SOCS2-AS1 was principally located in the cytoplasm. C, D Subcellular localization of SOCS2-AS1 was analyzed by qPCR in cellular fractions of HEC-1A and Ishikawa cells. GAPDH was used as a cytosolic marker, and U6 was used as a nuclear marker. E Silver staining of biotinylated SOCS2-AS1-associated proteins. Three SOCS2-AS1-specific bands (red arrows) were excised and analyzed using mass spectrometry. F Top-10 protein hits of bands, resulting from MS are labeled with a red arrow in E. G Western blot of the AURKA proteins from sense and antisense SOCS2-AS1 pull-down assays. H RNA immunoprecipitation experiments were performed using anti-AURKA antibody, and qPCR was used to detect SOCS2-AS1. MEG3 was used as a negative control. I Western blot of AURKA in samples pulled down by full-length (FL) or truncated SOCS2-AS1 (Δ1, 1–235; Δ2, 1–148; Δ3, 149–574).