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将从抗体文库中筛选出的抗HBsAg Fab阳性克隆转化大肠肝杆菌 ,IPTG诱导表达 ,经Western blot鉴定 ,证实上清中含有可溶性抗HBsAg Fab片段 ,应用自制的羊抗人免疫球蛋白片段抗体 (anti Fab )与Gama bind交联制备的亲和层析柱纯化表达产物 ,所得纯化产物在SDS PAGE中形成单一条带 ,经Western blot证实具备良好抗原特异性 ,Dot blot证实具备良好抗原结合活性。
The anti-HBsAg Fab positive clones screened from the antibody library were transformed into E. coli and induced with IPTG. Western blot analysis confirmed that the supernatant contained soluble anti-HBsAg Fab fragment. The purified goat anti-human immunoglobulin fragment antibody anti Fab) was purified by affinity chromatography with Gama bind. The purified product was purified by SDS PAGE to form a single band. The result of Western blot showed good antigen specificity. Dot blot demonstrated good antigen binding activity.