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. 2013 Sep 5;8(9):e72455. doi: 10.1371/journal.pone.0072455

Figure 1. Expression and purification of recombinant GST-C2IN-p53.

Figure 1

A. Scheme of GST-C2IN-p53 fusion construct. B. Time course of GST-C2IN-p53 expression in E. coli Rosetta. Samples were harvested after time points indicated (0, 1, 3, 6 and 20 h) and subjected to SDS-PAGE followed by Coomassie staining (top) or Western blot analysis using a p53 antibody (bottom). GST-C2IN-p53 is denoted by an arrow. C. Purification of GST-C2IN-p53 fusion protein by heparin affinity chromatography. GST-C2IN-p53 was isolated from whole cell extracts by heparin-based chromatography and eluted by a linear salt gradient as monitored by UV absorbance. Subsequently, fractions collected during affinity chromatography were characterized by immunoblot analysis with p53 antibody.