ABSTRACT
<p><b>OBJECTIVE</b>To express and purify the recombinant human pigment epithelium-derived factor (PEDF) which inhibits the proliferation of the endothelium cells from blood vessel in E.coli.</p><p><b>METHODS</b>PEDF gene was inserted into the prokaryotic expression vector pGEX-4T-2. The recombinant protein PEDF was expressed in E.coli BL-21, and purified by the GST Sepharose 4B affinity column. The recombinant human PEDF protein was identified by Western blot and mass spectrum. The biological activity of the recombinant human PEDF protein was measured by using MTT.</p><p><b>RESULTS</b>The 46 kDa recombinant human PEDF protein was obtained. It significantly inhibited the proliferation of the human umbilical vein cell line HUVEC.</p><p><b>CONCLUSION</b>The recombinant human PEDF with anti-angiogenesis activity protein may be successfully purify through prokaryotic expression.</p>