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. 2011 Jun 15;6(6):e21018. doi: 10.1371/journal.pone.0021018

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This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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Eight recombinant proteins with different compositions of the three extracellular domains of ROR1 were constructed for this study and expressed in HEK 293F cells. ROR1 Ig, Fz, and Kr domains are shown as oval, triangle, and circle, respectively (gray). Seven recombinant proteins, including two that included all three extracellular domains of human (h) and mouse (m) ROR1 as well as five with just one or two extracellular domains of human ROR1, were generated as C-terminal fusion to the dimeric Fc domain of human IgG1 (white) and purified by Protein A affinity chromatography. Another recombinant protein composed of the three extracellular domains of human ROR1 alone (hROR1ECD) was purified by ion exchange and gel filtration chromatography.