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. 2013 May 4;20(1):27. doi: 10.1186/1423-0127-20-27

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Copyright © 2013 Chang et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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CNBP is methylated in vivo and is recognized differentially by Sm1 due to its methylation status. HeLa cells were transfected with pFLAG-CNBP plasmids. The FLAG-tagged proteins were immunoprecipitated by anti-FLAG agarose. Proteins eluted by the FLAG peptide were then analyzed by Western blot analyses with anti-Sm1. The blot was stripped of the interacted antibodies and then probed with a mono- and di-methylarginine-specific antibody 7E6. The same blot was stripped and then re-probed with the anti-FLAG antibody. The internal blank region of the FLAG-CNBP signal of the AdOx- sample detected by anti-FLAG was due to previous stripping.