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本研究构建了pBV220/CabpD-9k-βhCG表达质粒,在大肠杆菌TG-1中进行表达,得到了CabpD-9k-βhCG融合蛋白。SDS-PAGE分析显示融合蛋白的分子量约为34.5KD。West-ern blot结果表明,融合蛋白与兔抗人hCGIgG特异结合。用纯化的融合蛋白免疫C57BL小鼠,制备了多克隆抗体,这为进一步研究钙结 合蛋白D-9k在着床中的功能和子宫内膜Ca~(2+)信号转导奠定了基础。
In this study, the expression vector pBV220 / CabpD-9k-βhCG was constructed and expressed in Escherichia coli TG-1. The CabpD-9k-βhCG fusion protein was obtained. SDS-PAGE analysis showed that the molecular weight of the fusion protein was about 34.5KD. West-ern blot results show that the fusion protein and rabbit anti-human hCGIgG specific binding. The purified fusion protein was used to immunize C57BL mice to prepare polyclonal antibodies, which laid the foundation of further study on the function and endometrial Ca2 + signal transduction of calbindin D-9k in implantation.