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. 2004 Sep 6;5:16. doi: 10.1186/1471-2199-5-16

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Copyright © 2004 Bannert et al; licensee BioMed Central Ltd.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Bel1/Tas interacts with GST-C/H1 fusion proteins detected by GST pull-down assays. The recombinant GST-C/H1 and GST-ΔC/H1-KIX proteins were expressed in E. coli BL21 cells and purified by binding to glutathione Sepharose 4B. Each GST-fusion protein bound to glutathione Sepharose 4B was separately mixed with lysates obtained from pbel1s-transfected 293T cells. After incubation and extensive washing with the binding buffer, bound proteins were eluted, separated by SDS-PAGE, and visualized by staining (upper panel); immunoblotting was carried out with an antibody against Bel1/Tas protein (lower panel).