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. 2015 Feb 18;11(2):458–467. doi: 10.4161/21645515.2014.990856

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© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC

© Terence L Kirley and Andrew B Norman

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 1. — 10% SDS-PAGE analysis of monoclonal antibody h2E2 with or without treatment with peptide N-glycosidase-F (PNGase-F) to remove all N-linked glycans. After overnight treatment with PNGase-F, either 5 (lanes 2-4), 10 (lanes 5-7), or 20 μg (lanes 8-10) of h2E2 antibody were reduced and denatured in SDS and loaded onto a 10% acrylamide gel, followed by staining with Coomassie Blue R-250. Control, untreated h2E2 (“Con”) along with PNGase-F (“+”) or sham treated (“−”) monoclonal antibody are shown, with the dashed line added to aid visualization of the small differences in electrophoretic mobility observed after N-glycan removal by PNGase-F. The migration positions of the heavy chain, light chain, and PNGase-F enzyme are indicated on the right hand side.