Skip to main content
Figure 3 | BMC Biotechnology

Figure 3

From: High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli

Figure 3

SDS-PAGE analysis of expression and purification of SUMO-FGF21. Bacterial containing pET-SUMO-FGF21 were induced by IPTG for 3 h or 4 h at 37°C in Figure 3A. The results from the different treatments are shown here. M: protein molecular weight markers;Lane 1: the supernatant of BL21 (DE3) containing pET-SUMO-FGF21 without IPTG;Lane 2: the supernatant of BL21 (DE3) containing pET- SUMO-FGF21 induced with 1 mM IPTG for 3 h; Lane 3: the supernatant of BL21 (DE3) containing pET- SUMO-FGF21 induced with 1 mM IPTG for 4 h; Lane 4: the precipitation of BL21 (DE3) containing pET-SUMO-FGF21 induced with 1 mM IPTG for 4 h. After recombinant bacteria were treated by sonication and centrifugation, the supernatants were loaded on a DEAE sepharose FF and Ni-NTA orderly. The purification results for SUMO-FGF21 are shown in the Figure 3B. Lane1: protein molecular weight marker, Lane2: purified SUMO-FGF21 eluted from Ni-NTA column; Lane3: SUMO-FGF21 eluted from DEAE sepharose FF column.

Back to article page

BMC Biotechnology

ISSN: 1472-6750

Contact us