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. 2015 Jan 15;26(2):359–372. doi: 10.1091/mbc.E14-05-0994

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© 2015 Gotoh, Vila-Caballer, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 3: — Relevance of hPer2-interacting domains for hp53 localization. H1299 cells were transfected with myc-tagged forms of hp53, hp53(ch)GST, hp53(ch)hPer2(356-574/683-872), NLS-hp53(ch)GST, and NLS-hp53(ch)hPer2(356-574/683-872) (i–v) or the untagged form of hp53(ch)hPer2 (vi). Proteins were visualized by confocal microscopy using α-myc-Cy3– conjugated primary antibody (i–v) or α-p53 and -Per2 primary antibodies and α-mouse Cy3– and α-rabbit Alexa Fluor 488 (Life Technologies)–conjugated secondary antibodies, respectively (vi). Actin fibers and DNA were stained with phalloidin Alexa Fluor 488 and Syto60 (Life Technologies), respectively. Merge images (right) were from protein staining, phalloidin, and DNA (i–v) and protein and DNA (vi). A Nikon ECLIPSE TE2000-E microscope and NIS-Elements AR 3.0 software were used to record images. Scale bars, 10 μm.