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Cloning and expression of recombinant human endostatin and its antiangiogenic activity

Objective To construct an engineering bacteria which can express human endostatin protein with biological activity. Methods Human endostatin gene fragment was acquired from human fetal liver total RNA by means of RT PCR. The gene was inserted into prokaryotic expressing vector pBV220 and transformed into E.coli DH5α. Endostatin was expressed in the E.coli and the inclusion body was isolated, solubilized and then refolded. Results SDS PAGE analysis showed that expressed product was about M r 20×10 3 and took up about 30% in bacterial total protein. Conclusion The recombinant human endostatin protein can inhibit proliferation of bovine capillary endothelial cells dependent on bFGF.