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. 2021 Mar 12;10(3):26. doi: 10.1038/s41389-021-00313-2

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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. 2 — A Schematic illustration of ELF3 and EHF gene products is shown. The long form variant of EHF includes 22 amino acid residues from exon 1 (EHF-LF), whereas the short form variant of EHF excludes exon 1 (EHF-SF). The pointed and ETS domains are shown as grey and hatched areas, respectively. The primers used to amplify EHF-LF, EHF-SF, and total EHF are shown in blue, red, and black arrows, respectively. B mRNA levels of two EHF transcript variants were analyzed by conventional RT-PCR. C and D IB with the indicated antibodies were performed in COS7 transfected with control vector (cont.) or the indicated plasmids (C), and in HNSCC cells (D). E ETS1 (D), EHF-SF (D), and ELF3 (S2B) protein levels were densitometrically quantified and compared with those of α-tubulin. The ratio of protein expression of ETS1/α-tubulin to that of EHF-SF/α-tubulin + ELF3/α-tubulin in SAS cells was indicated as “1”. α-tubulin was used as a loading control (D). EHF-LF(M23V), a mutant in which Met 23 in EHF-LF was substituted with Val (C).