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目的将 CD2 0胞外区基因在大肠杆菌中表达 ,并研究表达产物作为抗原筛选抗体的可能性。方法设计引物从 p U C19/ CD2 0质粒上钓取 CD2 0胞外区基因 ,克隆到 p Ex Sec 载体上 ,在大肠杆菌中融合表达。结果表达产物的相对分子质量 ( Mr)约为 2 6 0 0 0 ,Western- blot鉴定能够为抗 CD2 0分子的 m Ab所识别。利用初步纯化的 CD2 0胞外区融合蛋白为抗原 ,建立了检测 CD2 0 m Ab的 EL ISA方法。结论为研制 CD2 0分子的 m Ab奠定了基础
Objective To express the extracellular domain of CD20 in Escherichia coli and to study the possibility of using the expressed product as an antigen to screen the antibody. Methods Primers were designed to capture the extracellular domain of CD20 from pU C19 / CD20 plasmid and cloned into p Ex Sec vector for expression in E. coli. Results The relative molecular mass (Mr) of the expressed product was about 26,000. Western blotting confirmed that it was recognized by anti-CD20 molecule m Ab. Using the purified CD20 extracellular fusion protein as an antigen, an ELISA method for detecting CD20m Ab was established. Conclusion The research laid the foundation for the development of m Ab of CD20 molecule