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. 2011 Jun 7;286(31):27081–27091. doi: 10.1074/jbc.M111.257378

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 6. — Oligomer formation of split Gluc-tagged Arctic E22G Aβ. A, scheme for split Gluc-tagged AβE22G. We generated luci-AβE22G and ferase-AβE22G transiently expressing HEK293 cells. B, immunoblotting of the CM from luci-AβE22G, ferase-AβE22G, and double (luci-AβE22G/ferase-AβE22G) and double (luci-Aβ/ferase-Aβ) transiently expressing HEK293 cells by anti-Aβ mAb 6E10. C, luciferase assay of the CM from luci-AβE22G, ferase-AβE22G, and double (luci-AβE22G/ferase-AβE22G) transiently expressing HEK293 cells. The luminescence ± S.D. in three independent experiments are shown. D, comparison of luciferase activity of the CM from double (luci-Aβ/ferase-Aβ and luci-AβE22G/ferase-AβE22G) transiently expressing HEK293 cells. The luminescence was standardized by the expression levels of split Gluc-tagged Aβ and shown as the ratio relative to the level of luminescence of the CM from double (luci-Aβ/ferase-Aβ) stably expressing HEK293 cells as 100%. The luminescence ± S.D. in three independent experiments are shown. ANOVA test p < 0.05 (*).