水稻SDG711蛋白C末端原核表达及多克隆抗体制备 |
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引用本文: | 张志刚,李超,林欣欣,巫光宏,杜平州,王玉琪.水稻SDG711蛋白C末端原核表达及多克隆抗体制备[J].安徽农业科学,2013,41(4):1435-1437. |
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作者姓名: | 张志刚 李超 林欣欣 巫光宏 杜平州 王玉琪 |
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作者单位: | 华南农业大学生命科学学院,广东广州,510642;华南农业大学生命科学学院,广东广州510642;广东省农业生物蛋白质功能与调控重点实验室,广东广州510642 |
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基金项目: | 广东省高等学校科技创新项目,国家自然科学基金 |
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摘 要: | 目的]对水稻SDG711蛋白C末端进行原核表达,并制备其多克隆抗体。方法]选取水稻SDG711蛋白抗原决定簇较密集的C末端进行原核表达,通过构建原核表达载体pET28a-711C,转化E.coli BL21(DE3)感受态细胞,IPTG诱导表达融合蛋白后进行纯化,再以纯化的融合蛋白为抗原免疫新西兰白兔,制备多克隆抗体,并对其进行Western-blot分析。结果]试验制备的多克隆抗体能有效地检测抗原的表达。结论]该研究为进一步深入研究SDG711蛋白的功能奠定了基础。
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关 键 词: | 水稻 SDG723 原核表达 多克隆抗体 |
Prokaryotic Expression and Polyclonal Antibody Preparation of SDG711 C-terminal from Rice |
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Institution: | ZHANG Zhi-gang et al (College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong 510642) |
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Abstract: | Objective] This study aimed to conduct prokaryotic expression of rice SDG711 C-terminal and prepare its polyclonal antibody. Method ] C-terminal of rice SDG711 containing relatively intensive antigen determinants was selected for prokaryotic expression, prokaryotic expression vector pET28a-711C was constructed and the recombinant plasmid was transformed into Escherichia coli BL21 (DE3) competent cells. The recombinant fusion protein was induced by IPTG and purified to immunize a New Zealand white rabbit as the antigen, and poly- clonal antibody was obtained for Westem-blot analysis. Result] The polyclonal antibody prepared could efficiently detect the antigen expres- sion. Conclusion] This study laid the foundation for further investigating the functions of SDG711 protein. |
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Keywords: | Rice SDG711 Prokaryotic expression Polyclonal antibody |
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