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. 2013 Dec 18;11:96. doi: 10.1186/1478-811X-11-96

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Copyright © 2013 Rajala 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. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Effect of a phosphorylated BPS region of Grb14 on IR kinase and PTP1B activity. The domain organization of Grb14 and length of the BPS region is depicted (A). IR kinase activity was measured in the presence of either GST or GST-BPS-SH2 or mutant GST-BPS-SH2 (E373Q) in both non-phosphorylated and phosphorylated states (B), immunoblot of expressed proteins with anti-PY99 antibody and the same blot stripped and reprobed with anti-GST antibody (C). The fusion proteins (12 μM) that were used in the IR kinase activity (B) were further examined for their effect on PTP1B activity (D). Data are mean ± S.D., n = 3, **p < 0.001; *p < 0.05, P-Phosphorylated.