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. 2012 Nov 22;41(2):881–899. doi: 10.1093/nar/gks1134

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Published by Oxford University Press 2012.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial reuse, 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 3. — RECQL5 physically interacts with WRN both in vivo and in vitro. (A) Co-immunoprecipitation of WRN and RECQL5 from whole-cell extracts of HeLa cells, performed in the presence of ethidium bromide. Lane 1: input; lane 2: immunoprecipitation (IP) using rabbit IgG; lanes 3–5: IP with anti-RECQL5 antibody. Cells were harvested without any treatment (lane 3); 4 h after release from HU treatment (5 mM for 18 h) (lane 4); after γ-irradiation with 10 Gy (lane 5). RECQL5 was confirmed in the pull down using rabbit true blot antibody (central panel); negative IP for BLM was shown in the lower panel. (B) FACS analysis validating the synchronization of HeLa cells in S-phase 4 hrs after removal of HU. (C) In vitro IP was performed using purified recombinant proteins RECQL5 and WRN (1.2 μg each). WRN was pulled down with RECQL5 antibody (lane 3), but not by IgG (lane 2).