Biochemical investigation of wild-type and processed RNG2.

<p><b>(A)</b> Representation of the RNG2 constructs expressed in SF9 insect cells. <b>(B)</b> Insect cell protein expression and solubility of the RNG2 truncation variants, as assessed by Coomassie blue staining. <b>(C)</b> Protein expression and solubility...

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Bibliografische gegevens
Hoofdauteur: Romuald Haase (22339777) (author)
Andere auteurs: Bingjian Ren (22676577) (author), Albert Tell i Puig (22676580) (author), Alessandro Bonavoglia (19415718) (author), Jean-Baptiste Marq (375239) (author), Rémy Visentin (22676583) (author), Nicolas Dos Santos Pacheco (22676586) (author), Bohumil Maco (383443) (author), Ricardo Mondragón-Flores (10737057) (author), Oscar Vadas (2416228) (author), Dominique Soldati-Favre (79026) (author)
Gepubliceerd in: 2025
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Samenvatting:<p><b>(A)</b> Representation of the RNG2 constructs expressed in SF9 insect cells. <b>(B)</b> Insect cell protein expression and solubility of the RNG2 truncation variants, as assessed by Coomassie blue staining. <b>(C)</b> Protein expression and solubility of RNG2 truncation variants were assessed via western blotting. <b>(D)</b> Size-exclusion chromatography (SEC) chromatogram of the affinity-purified RNG2-ΔN+CTer variant obtained via Strep-tactin purification. A Coomassie-stained gel of the protein-containing fractions of the SEC is shown on the right. The data underlying this figure can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003506#pbio.3003506.s008" target="_blank">S2 Data</a>. <b>(E)</b> Co-purification assays using metal-affinity chromatography of cells co-infected with RNG2 fragments assessed by western blot analysis and Coomassie blue staining. All fragments have a C-terminal STREP-tag.</p>