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将hG－CSFCDNA片段克隆于T7噬菌体RNA聚合酶启动子系统的表达载体pJGW1中，并与可热诱导T7RNA聚合酶产生的质粒pGP1－2共同转化大肠杆菌DHSα。经化学诱导或温度诱导，hG－CSF重组蛋白表达率＞30％，并具有特异的生物活性。所构建的重组表达工程菌具有良好的稳定性。
The hG-CSF cDNA fragment was cloned into the expression vector pJGW1 of the T7 phage RNA polymerase promoter system and co-transformed into E. coli DHSα with the plasmid pGP1-2, which is produced by the heat-inducible T7 RNA polymerase. Induction of chemical or temperature, hG-CSF recombinant protein expression rate> 30%, and has specific biological activity. The constructed recombinant expression engineering bacteria have good stability.