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. 2018 Aug 8;46(17):8966–8977. doi: 10.1093/nar/gky705

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 2. — hTERP is expressed in telomerase-positive cells. (A–C) Immunolocalization of hTERP in HEK293T (A), Jurkat (B) and HT1080 (C) cells; blue, DAPI-stained nuclei; red, hTERP; scale bars, 5 μm. (D) Western blot analysis of HEK293T, Jurkat and HT1080 cells for the presence of hTERP. GAPDH staining was used as a loading control. (E) Levels of hTERC in HEK293T shLuc (expressed shRNA targeted luciferase mRNA (negative control)), HEK293T shTERC1 and HEK293T shTERC2 (expressed shRNAs targeted hTERC) normalized to the hTERC level in HEK293T cells. Mean ± SD was calculated for three biological replicates. (F) Western blot analysis of HEK293T shLuc (expressed shRNA targeted luciferase mRNA (negative control)), HEK293T shTERC1 and HEK293T shTERC2 (expressed shRNAs targeted hTERC) for the presence of hTERP. GAPDH staining was used as a loading control.