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. 2011 Jul 5;3(7):834–847. doi: 10.3390/toxins3070834

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© 2011 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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(A) Schematic outline of ricin toxin A (RTA) variants used in this study.In each fusion protein, the type of endoplasmic reticulum (ER) retention signal fused to RTA (K/HDEL) and the total size (in bp) is indicated. Length of the (His)₆-tag and the mammalian- or yeast-specific ER retention motifs are also shown. RTA fusions were cloned into pET24a⁽⁺⁾ and expressed in E. coli; (B) RTA purification by Ni²⁺-NTA chromatography.Purified samples (15‑25 µg) were analyzed by SDS‑PAGE and Coomassie staining. Lane 1: PAGE Ruler prestained (Fermentas); Lane 2: unmodified RTA; Lane 3: RTA^HDEL; Lane 4: RTA^KDEL.