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. Author manuscript; available in PMC: 2014 Nov 15.
Published in final edited form as: ACS Chem Biol. 2013 Sep 6;8(11):10.1021/cb4005707. doi: 10.1021/cb4005707

Figure 1.

Figure 1

Preparation of the GST-Mig6 semisynthetic proteins by expressed protein ligation (EPL). (a) Scheme for EPL to generate the semisynthetic GST-Mig6 segment 1+2 containing phosphorylated tyrosine in a full stoichiometry. The residue Tyr394 that can be phosphorylated by tyrosine kinases is highlighted in red. (b) Coomassie stained 10% SDS-PAGE of unligated and semisynthetic GST-Mig6 proteins. (c) The incorporation of phosphorylated Tyr394 into semisynthetic GST-Mig6 was verified with western blot using the antiphosphotyrosine antibody 4G10. The same amount of unligated(1), unphosphorylated (2), and phosphorylated (3) Mig6 proteins obtained via expressed protein ligation were analyzed by 10% SDS-PAGE and probed with 4G10 antibody.