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作 者:李侃 刘华[1] 费克香[1] 张道明[1] 郑小娟[1]
机构地区:[1]湖北省长江大学医学院分子医学中心实验室,荆州434000
出 处:《医学研究杂志》2007年第5期119-121,共3页Journal of Medical Research
摘 要:目的纯化兔抗人RBBP10多克隆抗体。方法在大肠杆菌中,表达重组PTC-hRBBP10融合蛋白,表达产物以直链淀粉树脂亲合柱和superose 12凝胶柱过滤纯化,将纯化的PTC-hRBBP10偶联于NHS-activated SepharoseTM上,制备亲合层析柱,纯化兔抗人RBBP10多克隆抗体。结果①表达、纯化的PTC-hRBBP10的相对分子质量(Mr)为80×103,纯度为95%;②从抗血清中纯化获得可与PTC-hRBBP10特异性结合的兔抗人RBBP10多克隆抗体。结论获得了特异性较好的纯化兔抗人RBBP多克隆抗体,为进一步研究该蛋白质的功能提供了条件,为肿瘤的诊断和治疗提供了新的理论和手段。Objective To purify rabbit anti - hRBBP10 polyclonal antibody. Methods The recombinant fusion protein PTC - hRBBP10 was expressed in the E. coli and was purified through amylose resin chromatography column and superose 12 gel titration . The purified PTC - hRBBP10 was coupled to the NHS - activated sepharose^TM to prepare affinity chromatography column to purify rabbit anti - hRBBP,0 polyclonal antibody. Results ① PTC - hRBBP10 was expressed and purified successfully with relative molecular mass(Mr) of 80 × 10^3 and its purity could reach about 95%. ② Purified Rabbit anti - hRBBP10 polyclonal antibody could bind Specifically to PTC - hRBBP10. Conclusions With better specificity, The purified rabbit anti - hRBBP10 polyclonal antibody provide condition for studying the function of the protein, and helps to develop new techniques of tumor diagnosis and treatment.
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