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dc.contributor.authorVy, Tran Vu Thao
dc.date.accessioned2015-10-05T01:58:57Z
dc.date.accessioned2018-05-29T08:11:36Z
dc.date.available2015-10-05T01:58:57Z
dc.date.available2018-05-29T08:11:36Z
dc.date.issued2014
dc.identifier.urihttp://10.8.20.7:8080/xmlui/handle/123456789/1563
dc.description.abstractRecombinant human Interferon-β-1b (IFN-β-1b) is a non-glycosylated IFN-β that was found to be effective against multiple sclerosis. More recently, expression of IFN-β-1b in Escherichia coli (E. coli) has been reported; however, problems due to low yields and poor stability were described. This study was aim to clone and express of recombinant IFN-β-1b in E. coli using a novel synthetic gene with preferred codon usage of E. coli under the control of T7 promoter. Protein expression was induced with Isopropyl-thiogalactoside (IPTG) and lactose. The level of expression was analyzed by SDS-PAGE, Western blot, Bradford and ELISA. The effect of two factors including inducer concentration, and length of the induction on the expression of IFN-β-1b was investigated. As a result, we have successfully cloned the E. coli BL21 (DE3) stain that harbors gene encoding for rhIL-29. Results from SDS-PAGE, Western blot and ELISA show that IPTG of 1mM and induction duration of 6h had more effect on IFN-β-1b production. IFN- β-1b expression with the above condition yielded 17.39% of the total cell protein. Besides, under the induction of 0.25% lactose and 6 hours of incubation, IFN-β-1b production also achieved a high efficiency 13.4% of total cell protein, which promises for an effective way for industrial manufacture. Keywords: Expression, Interferon-β-1b, E. coli BL21 (DE3), T7 promoter, induction.en_US
dc.description.sponsorshipPhD. Do Minh Sien_US
dc.language.isoen_USen_US
dc.publisherInternational University HCMC, Vietnamen_US
dc.relation.ispartofseries;022001278
dc.subjectRecombinant human interferon-β-1ben_US
dc.titleCloning and expression recombinant human interferon-β-1b +CDen_US
dc.typeThesisen_US


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