D. S. Alrseetmiwe, A. A. Almayah, A. Nasser, M. H. Alnussairi, H. A. Zadeh, F. A. Mehrzi
{"title":"大肠杆菌bl21株干扰素α 2b (de3)的克隆与表达","authors":"D. S. Alrseetmiwe, A. A. Almayah, A. Nasser, M. H. Alnussairi, H. A. Zadeh, F. A. Mehrzi","doi":"10.59807/jlsar.v1i2.15","DOIUrl":null,"url":null,"abstract":"Concentrating on the interferon alpha 2b gene (INF 2b), a protein having antiviral and anticancer properties, could be beneficial therapeutically. It is advised to conduct an experimental examination of the target protein before having it produced on a big scale. The bacterial host is a good option since it allows us to gain a thorough understanding of the topic. The INF-2b sequence used in this study was obtained from the NCBI gene data library, and following optimization, it was cloned and expressed in pET28a+.Escherichia coli was chosen as the prokaryotic expression system for the target protein's initial analysis. Bacterial cells expressing the pET:IFN construct were IPTG-induced to produce the protein, which was then resolved using SDS-PAGE. During gel separation, the studied protein's anticipated size of roughly 24 kDa was seen. IFN 2b was successfully expressed, according to further evaluation by western blotting.","PeriodicalId":126839,"journal":{"name":"Journal of Life Science and Applied Research","volume":"1 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2020-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":"{\"title\":\"ESCHERICHIA COLI STRAIN BL21: CLONING AND EXPRESSION OF AN OPTIMIZED INTERFERON ALPHA 2B (DE3)\",\"authors\":\"D. S. Alrseetmiwe, A. A. Almayah, A. Nasser, M. H. Alnussairi, H. A. Zadeh, F. A. Mehrzi\",\"doi\":\"10.59807/jlsar.v1i2.15\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Concentrating on the interferon alpha 2b gene (INF 2b), a protein having antiviral and anticancer properties, could be beneficial therapeutically. It is advised to conduct an experimental examination of the target protein before having it produced on a big scale. The bacterial host is a good option since it allows us to gain a thorough understanding of the topic. The INF-2b sequence used in this study was obtained from the NCBI gene data library, and following optimization, it was cloned and expressed in pET28a+.Escherichia coli was chosen as the prokaryotic expression system for the target protein's initial analysis. Bacterial cells expressing the pET:IFN construct were IPTG-induced to produce the protein, which was then resolved using SDS-PAGE. During gel separation, the studied protein's anticipated size of roughly 24 kDa was seen. IFN 2b was successfully expressed, according to further evaluation by western blotting.\",\"PeriodicalId\":126839,\"journal\":{\"name\":\"Journal of Life Science and Applied Research\",\"volume\":\"1 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2020-12-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Life Science and Applied Research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.59807/jlsar.v1i2.15\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Life Science and Applied Research","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.59807/jlsar.v1i2.15","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
ESCHERICHIA COLI STRAIN BL21: CLONING AND EXPRESSION OF AN OPTIMIZED INTERFERON ALPHA 2B (DE3)
Concentrating on the interferon alpha 2b gene (INF 2b), a protein having antiviral and anticancer properties, could be beneficial therapeutically. It is advised to conduct an experimental examination of the target protein before having it produced on a big scale. The bacterial host is a good option since it allows us to gain a thorough understanding of the topic. The INF-2b sequence used in this study was obtained from the NCBI gene data library, and following optimization, it was cloned and expressed in pET28a+.Escherichia coli was chosen as the prokaryotic expression system for the target protein's initial analysis. Bacterial cells expressing the pET:IFN construct were IPTG-induced to produce the protein, which was then resolved using SDS-PAGE. During gel separation, the studied protein's anticipated size of roughly 24 kDa was seen. IFN 2b was successfully expressed, according to further evaluation by western blotting.