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将人单核细胞趋化蛋白－１（ＭＣＰ－１）的ｃＤＮＡ插入融合蛋白表达载体ｐＧＥＸ－４Ｔ－１中，构建成质粒ｐＧＥＸ／ＭＣＰ转化大肠杆菌ＪＭ１０９，经ＩＰＴＧ诱导后合成ＧＳＴ－ＭＣＰ－１融合蛋白。用１２％ＳＤＳ－ＰＡＧＥ检测在３０ｋＤ左右有新生蛋白条带出现，表达量约占菌体总蛋白的３１．７％。趋化实验证明，该产物具备明确的单核细胞趋化活性。
The cDNA of human monocyte chemoattractant protein-1 (MCP-1) was inserted into the fusion protein expression vector pGEX-4T-1 and transformed into E. coli JM109 with pGEX / MCP. After induced by IPTG, GST-MCP- Fusion protein. With 12% SDS-PAGE detected in about 30kD nascent protein bands appear, the expression amount of about 31.7% of total bacterial protein. Chemotaxis experiments show that the product has a clear monocyte chemotactic activity.