Prokaryotic Ubiquitin-Like ThiS Fusion Enhances the Heterologous Protein Overexpression and Aggregation in Escherichia coli
Figure 5
Folded EGFP proteins with or without ThiS fusion retained their native states during SDS-PAGE.
Purified EGFP and ThiS-EGFP from supernatants (expressed at room temperature), as well as the proteins solubilized from inclusion bodies (I), were resolved on 12% SDS-PAGE, with (+) or without (−) boiling the samples. The gel was photographed under UV illumination (right panel), then stained by Coomassie blue (left panel). Purified native proteins migrated at faster rate and retained fluorescence after SDS-PAGE, if not heat denatured.