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重组人卵透明带蛋白3的制备及其免疫学活性分析
引用本文:郭焱,曲晓波,金宁一.重组人卵透明带蛋白3的制备及其免疫学活性分析[J].中国免疫学杂志,2009,25(12).
作者姓名:郭焱  曲晓波  金宁一
作者单位:1. 长春中医药大学,长春,130117
2. 中国人民解放军军事医学科学院军事兽医研究所全军基因工程重点实验室,长春,130021
基金项目:吉林省科技厅科研基金重大项目 
摘    要:目的:纯化制备rhuZP3,并分析其免疫学活性.方法:在含重组质粒pGEX4T-1/ huZP3 的大肠杆菌 BL21中,经IPTG诱导表达出GST-融合蛋白,蛋白经过一系列的纯化,然后SDS-PAGE电泳鉴定蛋白纯度.rhuZP3免疫小鼠,ELISA法检测抗血清对rhZP3的抗体反应.结果:表达出了可溶性融合蛋白,纯化后的rhuZP3纯度达95%.而且它在ELISA 鉴定实验中能被抗rhuZP3抗体识别.结论:通过原核表达系统制备的rhuZP3及其抗体具有免疫学活性.

关 键 词:人卵透明带蛋白3  表达  纯化  活性

Preparation of recombinant human zona pellucida 3 protein and its immunologic activity
GUO Yan,QU Xiao-Bo,JIN Ning-Yi.Preparation of recombinant human zona pellucida 3 protein and its immunologic activity[J].Chinese Journal of Immunology,2009,25(12).
Authors:GUO Yan  QU Xiao-Bo  JIN Ning-Yi
Abstract:Objective:To prepare and purify recombinant human zona pellucida 3 protein,and to study its immunologic activity.Methods:The E.coli BL21 containing recombinant plasmid pGEX4T-1/ huZP3 was induced to express GST-fusion protein by IPTG.After a series of purification procedure,the purified protein was analyzed by SDS-PAGE.After the mice immunized with rhuZP3,the antibody responses against rhuZP3 were detected by ELISA.Results:The soluble fusion protein was expressed,and purity of rhuZP3 was 95%.Moreover, purity of rhuZP3 could be recognized by anti-human ZP3 in ELISA.Conclusion:The rhuZP3 is obtained through the preparation of prokaryotic expression system and anti-rhuZP3 antibody has immunological activity.
Keywords:Human zona pellucida 3 (rhuZP3)  Expression  Purification  Activity
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