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. 2010 Jan 25;188(2):223–235. doi: 10.1083/jcb.200910042

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© 2010 Bernasconi et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 2. — Involvement of HRD1 in disposal of membrane-tethered and soluble BACE476. (A) Radiolabeled BACE476 was immunoisolated after the indicated chase times from wild-type MEFs (wt; lanes 1–3) or MEFs lacking HRD1 (Hrd1^−/−; lanes 4–6). Relevant bands were quantified and plotted. (B) Same as described in A for BACE476Δ. (C) Radiolabeled BACE476Δ was immunoisolated after the indicated chase times from cells lacking HRD1 transfected with an empty plasmid (mock; lanes 1–3), a plasmid for expression of wild-type HRD1 (lanes 4–6), or a plasmid for expression of inactive HRD1 (HRD1*; lanes 7–9). Relevant bands were quantified and plotted. Error bars represent standard deviation (n = 2). Molecular mass markers are shown on the left for all gels (given in kilodaltons).