摘要
将编码人单核细胞趋化蛋白－１（ＭＣＰ－１）的基因亚克隆到大肠杆菌表达载体ｐＥＸ３１Ａ中，在大肠杆菌中表达出ＭＳ２／ＭＣＰ－１融合蛋０白，该表达产物约占菌体总蛋白的１５％左右，Ｗｅｓｔｅｒｎｂｌｏｔ检测表明，表达产物可与ＭＣＰ－１抗体特异反应。采用琼脂糖平板法进行活性测定表明，表达产物具有明显的单核细胞趋化活性，说明Ｎ端融合一段细菌蛋白对ＭＣＰ－１有无趋化活性可能没有影响。
A gene fragment encoding human monocyte chemoattratctant protein-1 (MCP-1) was subcloned into pEX31A. MS2/MCP-1 fusion protein was expressed in E. coli and accounted for about 15% of total cell proteins. Western blot analysis indicated that the expression product reacted specifically with anti-MCP-1 antibodies. Detection of activity by the method of agarose plates showed that the expression product had obvious monocyte chemoattractant activity, suggesting that bacterial protein at N-terminus may not affect the chemoattractant activity of MCP-1.
关键词
人
单核细胞
趋化蛋白-1
融合蛋白
基因表达
Human monocyte chemoattractant protein-1
Gene cloning and expression
Fusion protein
