Prokaryotic Ubiquitin-Like ThiS Fusion Enhances the Heterologous Protein Overexpression and Aggregation in Escherichia coli
Figure 2
Expression of Insulin chains fused with half-molecules of ThiS or Ubiquitin.
Insulin A chain (A) or B chain (B) fused with the N-terminal half (ThN-) or C terminal half (ThC-) of ThiS or the N-terminal half of ubiquitin (UbN-), were expressed in E. coli BL21 (DE3) pLysS. Total cell lysate from uninduced (−) or induced (+) cells with IPTG, and the soluble (S) or insoluble fraction (I) of induced cell were resolved on 15% SDS-PAGE, shown in left panels. M indicates Marker proteins. Western blot probed with anti His-tag antibody were shown in right panels. Arrowheads highlight observed positions of expressed proteins.