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基因工程技术构建的抗人ＴＮＦα单链抗体克隆入表达载体ｐＥＴ１５ｂＥｔａｇ 中， 在Ｔ７ 启动子的作用下， 经０１ ｍｍｏｌ／ＬＩＰＴＧ诱导， 在大肠杆菌ＢＬ２１ （ＤＥ３） 中获得高效表达， 其表达量占菌体总蛋白的３８％ ． 表达产物大部分以包涵体形式存在， 而一小部分以有活性的可溶性形式出现于细菌的外周质中． 这部分可溶性的表达产物占菌体总蛋白的６％ ， 经双抗体夹心法和斑点印迹分析表明它具有抗原结合活性
Gene engineering technology constructed anti-human TNF α single chain antibody cloned into the expression vector pET15b Etag, under the action of the T7 promoter, induced by 0.1 mmol / L IPTG, highly expressed in E. coli BL21 (DE3) , Its expression amount accounted for 38% of the total bacterial protein. Most of the expression products exist in the form of inclusion bodies, while a small fraction appears active in the soluble form of the outer periplasm of bacteria. This partially soluble expression product accounted for 6% of the total bacterial protein, which was identified by the double antibody sandwich method and dot blot analysis as having antigen-binding activity