Prokaryotic Expression and Purification of Vascular Endothelial Growth Factor D

To express,purify and identify VEGF-D fusion protein,E·coli BL21(DE3) containing recombinant plasmid pGEX-6p-1-VEGF-D was induced by IPTG.The bacteria was lyzed with lysozymc.Expressed product was purified by GST protein purification system.GST was cut by 3C-protease.And then the expressed fusion protein was identified by SDS-PAGE.The result showed that the relative molecular mass of expressed product was 56 000,which was consistent with that of GST-VEGF-D fusion protein.The VEGF-D protein without GST was successfully purified.The purified protein could be used to study biological activity of VEGF-D.