Fig. 1
From: Effective production of human growth factors in Escherichia coli by fusing with small protein 6HFh8
Schematic illustration of the GF production approach. GFs were fused with 6HFh8 via S5N10 linker sequence and TEV protease cleavage site. The fusion proteins were expressed in soluble form in the cytoplasm. They were first purified by HisTrap chromatography, and the target proteins were obtained by TEV protease cleavage. The proteins were then purified by IEX (HiTrap CM or HiTrap SP) chromatography based on the pI value. Dashed lines (bottom panel) indicate disulfide bonds