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. 2001 Apr 30;153(3):585–598. doi: 10.1083/jcb.153.3.585

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© 2001 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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The CH2 domain mediates the interaction with ILK. (A) GST–CH-ILKBP fusion proteins were separated on SDS-PAGE (10 μg/lane) and detected by Coomassie blue R-250 staining. The numbers in parentheses indicate CH-ILKBP residues. (B) ILK binding. C2C12 cell lysates (100 μg) were incubated with equal amount (10 μg) of GST or GST fusion proteins containing CH-ILKBP sequences as indicated in the figure. GST and the GST fusion proteins were precipitated with glutathione-Sepharose 4B beads. ILK was detected by Western blotting with anti-ILK antibody 65.1. (Lane 9) C2C12 cell lysates (10 μg/lane).