{"title":"HIV-1重组Nef- MPER-V3蛋白原核表达系统的克隆、表达条件优化及纯化","authors":"A. Faghih, S. M. Sadat, A. Bolhassani, S. Irani","doi":"10.52547/jmj.17.2.46","DOIUrl":null,"url":null,"abstract":"a clear band of around 35 kDa in SDS-PAGE and was detectable using anti-Neff antibody in western blotting. Conclusion: Our results showed that the Nef-MPER-V3 protein was successfully expressed in prokaryotic system and purified protein may provide the antigen for future experiments for immunogenicity evaluation in mice is currently undertaken.","PeriodicalId":33852,"journal":{"name":"fSlnmh dnshgh `lwm pzshkhy jhrm","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2019-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Cloning, Optimization of Expression Condition and Purification of the Recombinant Nef- MPER-V3 Protein of HIV-1 in Prokaryotic Expression System\",\"authors\":\"A. Faghih, S. M. Sadat, A. Bolhassani, S. Irani\",\"doi\":\"10.52547/jmj.17.2.46\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"a clear band of around 35 kDa in SDS-PAGE and was detectable using anti-Neff antibody in western blotting. Conclusion: Our results showed that the Nef-MPER-V3 protein was successfully expressed in prokaryotic system and purified protein may provide the antigen for future experiments for immunogenicity evaluation in mice is currently undertaken.\",\"PeriodicalId\":33852,\"journal\":{\"name\":\"fSlnmh dnshgh `lwm pzshkhy jhrm\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"fSlnmh dnshgh `lwm pzshkhy jhrm\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.52547/jmj.17.2.46\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"fSlnmh dnshgh `lwm pzshkhy jhrm","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.52547/jmj.17.2.46","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Cloning, Optimization of Expression Condition and Purification of the Recombinant Nef- MPER-V3 Protein of HIV-1 in Prokaryotic Expression System
a clear band of around 35 kDa in SDS-PAGE and was detectable using anti-Neff antibody in western blotting. Conclusion: Our results showed that the Nef-MPER-V3 protein was successfully expressed in prokaryotic system and purified protein may provide the antigen for future experiments for immunogenicity evaluation in mice is currently undertaken.
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