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. 2010 Mar 10;19(11):2239–2250. doi: 10.1093/hmg/ddq103

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© The Author 2010. Published by Oxford University Press

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Comparison of the intracellular localization of DDR2 wild-type and SMED-SL patient mutant variants with the ER marker. HeLa cells were transiently transfected with plasmids encoding the indicated HA-tagged DDR2 protein, fixed and stained with antibodies against the HA-tag (monoclonal) and calnexin (polyclonal) as described in Materials and Methods. (A), (D), (G), (J) and (M) show the distribution of over-expressed HA-tagged DDR2 proteins. (B), (E), (H), (K) and (N) show the distribution of calnexin, which is predominantly localized to the ER, while (C), (F), (I), (L) and (O) show the extent of co-localization of DDR2 proteins with calnexin.