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dc.contributor.advisorFranta, Zdeněk
dc.contributor.authorManoczki, Nelli Vanessza
dc.date.accessioned2023-03-07T11:02:32Z
dc.date.available2023-03-07T11:02:32Z
dc.date.issued2019
dc.date.submitted2019-05-14
dc.identifier.urihttps://dspace.jcu.cz/handle/20.500.14390/40748
dc.description.abstractA gene fragment encoding the C-terminal domain of the sigmaNS protein of the avian reovirus was amplified via PCR. The amplicon was cloned using BsaI restriction enzyme into the pASKIBA37+ expression vector and transformed into One ShotTM TOP 10 Chemically Competent E.coli cells. Colony PCR was performed and plasmids were sent for sequencing. Sequence verified plasmids were transformed into One ShotTM BL21 (DE3) or Rosetta-gami B (DE3) Chemically Competent E.coli cells. During Pilot expressions the conditions for production of soluble recombinant protein were optimized and according to them the recombinant protein was produced in large scale. The presence of the sigmaNS-terminal domain was verfied by Western Blot.cze
dc.format38 p. (59 898 characters)
dc.format38 p. (59 898 characters)
dc.language.isoeng
dc.publisherJihočeská univerzitacze
dc.rightsBez omezení
dc.titleMechanisms of dsRNA virus replication: Cloning, production and structural characterization of C-terminal domain of sigmaNS.cze
dc.title.alternativeMechanisms of dsRNA virus replication: Cloning, production and structural characterization of C-terminal domain of sigmaNS.eng
dc.typebakalářská prácecze
dc.identifier.stag52812
dc.description.abstract-translatedA gene fragment encoding the C-terminal domain of the sigmaNS protein of the avian reovirus was amplified via PCR. The amplicon was cloned using BsaI restriction enzyme into the pASKIBA37+ expression vector and transformed into One ShotTM TOP 10 Chemically Competent E.coli cells. Colony PCR was performed and plasmids were sent for sequencing. Sequence verified plasmids were transformed into One ShotTM BL21 (DE3) or Rosetta-gami B (DE3) Chemically Competent E.coli cells. During Pilot expressions the conditions for production of soluble recombinant protein were optimized and according to them the recombinant protein was produced in large scale. The presence of the sigmaNS-terminal domain was verfied by Western Blot.eng
dc.date.accepted2019-06-17
dc.description.departmentPřírodovědecká fakultacze
dc.thesis.degree-disciplineBiological Chemistrycze
dc.thesis.degree-grantorJihočeská univerzita. Přírodovědecká fakultacze
dc.thesis.degree-nameBc.
dc.thesis.degree-programBiochemistrycze
dc.description.gradeDokončená práce s úspěšnou obhajoboucze
dc.contributor.refereeChmelař, Jindřich


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