1 2 d rotavirus wa strain (ATCC)
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1 2 d rotavirus wa strain
1 2 D Rotavirus Wa Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 378 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ma+2+1/MA-104+Clone+1/pmc11435836-108-53-63
Average 96 stars, based on 378 article reviews
1 2 D Rotavirus Wa Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 378 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ma+2+1/MA-104+Clone+1/pmc11435836-108-53-63
Average 96 stars, based on 378 article reviews
1 2 d rotavirus wa strain - by Bioz Stars,
2026-09
96/100 stars
Images
1) Product Images from "Molecular Design of Encapsulin Protein Nanoparticles to Display Rotavirus Antigens for Enhancing Immunogenicity"
Article Title: Molecular Design of Encapsulin Protein Nanoparticles to Display Rotavirus Antigens for Enhancing Immunogenicity
Journal: Vaccines
doi: 10.3390/vaccines12091020
Figure Legend Snippet: Design and soluble expression of the fusion protein of rotavirus receptor-binding domain and ENC nanoparticles. ( a ) Computational modeling and theoretical structure of ENC-RV VP8*. The predicted structure of ENC and linked VP8* are colored blue and green, respectively. The fusion protein of ENC-VP8* was predicted using SWISS-MODEL, Expasy. ( b ) Schematic designs of the protein structures. The size of proteins is shown under the name of each protein. ( c ) Expression of ENC and ENC-RV VP8* in the presence or absence of the RID fusion partner. The proteins were expressed at various vector constructions, and the cell lysates were separated into T, P, and S fractions via centrifugation and analyzed using 12% sodium dodecyl sulfate–polyacrylamide gel electrophoresis. ENC-VP8* with RID fusion partner is indicated by the red arrow. Lane M indicates molecular size markers. TEV SITE, tobacco etch virus (TEV) protease cleavage site; T, total fraction; P, insoluble pellet fraction; S, soluble fraction; ENC, encapsulin; RV, rotavirus vaccine, RID, RNA-interacting domain.
Techniques Used: Expressing, Binding Assay, Plasmid Preparation, Centrifugation, Polyacrylamide Gel Electrophoresis, Virus
Figure Legend Snippet: The addition of GS linker to the N-terminal of fusion protein increases the cleavage efficiency of TEV protease. ( a ) Schematic diagram of the expression vector system. The two linkers are shown in red (GS) 3 and white (Linker) and TEV SITE indicates the TEV protease recognition site. ( b ) Time-lapse 12% sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of TEV cleavage before (left panel) and after (right panel) the linker insertion. Lane M indicates molecular size markers. Proteins purified or separated until purification are indicated by red arrows. ( c ) Following IMAC elution, minor residual contaminants and non-target proteins were removed. Purified NPs (ENC NPs with and without VP8*) were negatively stained and analyzed via transmission electron microscopy. Scale bars = 100 nm and 200 nm. ENC, encapsulin; RV, rotavirus vaccine, RID, RNA-interacting domain; M, molecular weight marker; IMAC, elution with anion exchange chromatography.
Techniques Used: Expressing, Plasmid Preparation, Polyacrylamide Gel Electrophoresis, Purification, Staining, Transmission Assay, Electron Microscopy, Molecular Weight, Marker, Chromatography
Figure Legend Snippet: Linker affects the enhanced yield of nanoparticle (NP) antigen. ( a ) Schematic diagram of ENC-RV VP8* with inserted linker between ENC and VP8* antigen. Underlined L2 is colored as white. ENC and linked VP8* are colored blue and green, respectively. ( b ) The solubility of recombinant proteins fused with different linkers was analyzed with sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Protein expression is under the control of isopropyl-β-D-thiogalactopyranoside induction. NP protein was fused with the C-terminal antigen VP8* via the linkers, L1: (G 3 S) 3 SGGS linker (left) and L2: (G 3 S) 2 EAAAKG 3 S linker (right). The arrow indicates the band position of each recombinant protein. ( c ) Dynamic light scattering measurement profiles (three independent scans of the same sample) of particle sizes and distributions of ENC NPs with L1 (left) and L2 (right). ( d ) Purified NPs were negatively stained and analyzed via transmission electron microscopy. Scale bar = 200 nm. M, molecular weight marker; T, total fraction; P, insoluble pellet fraction; S, soluble fraction; L1, linker 1; L2, linker 2; ENC, encapsulin; RV, rotavirus vaccine, RID, RNA-interacting domain.
Techniques Used: Solubility, Recombinant, Polyacrylamide Gel Electrophoresis, Expressing, Control, Purification, Staining, Transmission Assay, Electron Microscopy, Molecular Weight, Marker
Figure Legend Snippet: Conformation of VP8* displayed with P2 on ENC was self-assembled into 60-mer nanoparticles (NPs). ( a ) Schematic diagram of ENC-RV VP8* with inserted linker between ENC and VP8* antigen. P2 is colored orange. ENC and linked VP8* are colored blue and green, respectively. ( b ) Purified recombinant proteins fused with different linkers were analyzed with sodium dodecyl sulfate–polyacrylamide gel electrophoresis. NP protein was fused with the C-terminal antigen VP8* via the L2 linker with P2 (right). The arrow indicates the band position of each recombinant protein. ( c ) Dynamic light scattering measurement profiles (three independent scans of the same sample) of particle sizes and distributions of ENC NPs with P2. ( d ) Purified NPs were negatively stained and analyzed via transmission electron microscopy. Scale bar = 50 nm. ENC, encapsulin; L2, linker 2; RV, rotavirus vaccine; RSD, relative standard deviation.
Techniques Used: Purification, Recombinant, Polyacrylamide Gel Electrophoresis, Staining, Transmission Assay, Electron Microscopy, Standard Deviation
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