The vasoinhibins (VI) and vasostatin (VS) are N-terminal fragments released by proteolysis of the human prolactin and calreticulin, respectively. Those fragments have antiangiogenic activity and they have been proposed as therapeutic proteins in cancer therapy and vascular diseases. The aim of this work was the production of the fusion protein vasostatin_vasoinhibin (VS_VI) connected by the GGPGG bridge. The recombinant VS_VI was expressed in Escherichia coli BL21-SI using an expression vector driven by the T7 promoter and induced with NaCl. Recombinant VS_VI was produced and purified by nickel affinity chromatography. Biological activity was assed as the inhibition of proliferation of rat coronary endothelial cells (CEC). The results showed that recombinant VS_VI inhibited the proliferation of CEC in both cultures with or without the presence of the Bradykinin an endothelial growth factor. Acknowledgements: Partial financial support of CONACyT-Básicas Grant 18802.