Calreticulin is an calcium binding protein existed in all animal cells. It was found that calreticulin and its N terminal 1～180 amino acid inhibit the proliferation of endothelial cells and angiogenesis. In order to search for efficient and small molecular angiogenesis inhibitor, the DNA sequence coding for the N terminal 122～180 amino acid was amplified by PCR and cloned into the prokaryotic vector pET-3c. The recombinant plasmid pET-N58 was transformed into E.coli BL21(DE3). The recombinant protein was expressed efficiently in E.coli BL21(DE3,pET-N58) as inclusion body with a yield of about 35.4% of the bacterial total protein. The partial purified recombinant protein inhibits the proliferation of human umbelical vein endothelial cells and the CAM angiogenesis. The recombinant protein also suppresses the growth of primary B16 murine melanoma in C57BL/6 mice.