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将PCR扩增的人白细胞介素-6（hIL-6）成熟肽基因与PJLA502表达载体重组，在大肠杆菌中高效表达出rhIL－6。经SDS－PAGE分析，rhIL－6表达量占菌体可溶性蛋白的40％以上。经免疫印迹证实，rhIL－6具有良好的抗原特异性。复性后，用MTT法测定IL－6依赖株7TD1细胞增殖活性，rhIL－6比活性达2．5×10~6u／mg蛋白。
Recombinant human interleukin-6 (hIL-6) mature peptide gene was recombined with PJLA502 expression vector and rhIL-6 was highly expressed in E. coli. After SDS-PAGE analysis, rhIL-6 expression accounted for more than 40% of bacterial soluble protein. Confirmed by Western blot, rhIL-6 has good antigen specificity. After renaturation, the proliferation activity of IL-6-dependent 7TD1 cells was assayed by MTT assay. The specific activity of rhIL-6 reached 2.5 × 10 ~ 6u / mg protein.