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将质粒ｐＢＶ－ｍＩＬ－５的小鼠白细胞介素５（ｍＩＬ－５）的ｃＤＮＡ插入表达载体ｐＥＸ３１ｂ，转化大肠杆菌ＲＲＩ，经热诱导获得高效表达，表达的重组蛋白占菌体总蛋白的４０％。该融合蛋白由大肠杆菌ＭＳ２聚合酶的９９个氨基酸和ｍＩＬ－５的１１３个氨基酸组成，在菌体中以包涵体的形式存在，用ＴｒｉｔｏｎＸ－１００、尿素洗涤包涵体，初步纯化的重组蛋白纯度达９０％，已用于制备抗ｍＩＬ－５的单克隆抗体。Ｗｅｓｔｅｒｎ－ｂｌｏｔ和ＥＬＩＳＡ证实ｍＩＬ－５重组蛋白能与抗ｍＩＬ－５多克隆ＩｇＧ特异结合。
The cDNA of mouse interleukin 5 (mIL-5) of plasmid pBV-mIL-5 was inserted into the expression vector pEX31b and transformed into E. coli RRI. The mIL-5 gene was highly expressed by heat induction. The expressed recombinant protein accounts for 40% . The fusion protein consists of 99 amino acids of Escherichia coli MS2 polymerase and 113 amino acids of mIL-5. The fusion protein exists as inclusion bodies in the bacterial cells. The inclusion bodies are washed with Triton X-100 and urea. The purity of the initially purified recombinant protein Up to 90%, has been used to prepare monoclonal antibodies against mIL-5. Western-blot and ELISA confirmed that the mIL-5 recombinant protein specifically binds to anti-mIL-5 polyclonal IgG.