antibodies against internal epitopes Search Results


monoclonal antibody against the v5 epitope tag  (MBL International)
90
MBL International monoclonal antibody against the v5 epitope tag
Genome structure of BVDV and synthesis of the region encoding the E2 glycoprotein. BVDV genome organization (not to scale) and polyprotein processing ( A ). Cloning strategy and synthesis of genes encoding the C-terminally truncated (transmembrane anchoring domains deleted) forms of the E2 glycoprotein (boxed areas) are shown, together with the signal peptide (horizontal hatching area) and the C-terminal <t>V5</t> <t>epitope</t> tag (slash area) ( B ). Cloning of truncated form of E2 glycoprotein into pJC3 expression vector. Plasmid pJC3 encodes a [GFP-T2A-mCherry] polyprotein encoded by a single open reading frame. Transcription is driven by the human cytomegalovirus enhancer/promoter and the mRNA polyadenylated by the bovine growth hormone polyadenylation signal. Sequences encoding the truncated form of E2 glycoprotein were excised by restriction with ApaI and PstI from the pGEM-T Easy Vector, then inserted to pJC3, similarly restricted, to remove mCherry FP and create plasmid [GFP-T2A-BVDV-E2 trunk] ( C ). The NetNGlyc-1.0 server ( https://services.healthtech.dtu.dk/service.php?NetNGlyc-1.0 ) was used to predict N-glycosylated sites from full-length E2 glycoproteins. An N-glycosylation potential of > 0.5 was the cut-off value for sequences ( D ).
Monoclonal Antibody Against The V5 Epitope Tag, supplied by MBL International, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/monoclonal antibody against the v5 epitope tag/product/MBL International
Average 90 stars, based on 1 article reviews
monoclonal antibody against the v5 epitope tag - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
speci®c igm against vp2 conformational epitopes  (Biotrin International)
90
Biotrin International speci®c igm against vp2 conformational epitopes
Genome structure of BVDV and synthesis of the region encoding the E2 glycoprotein. BVDV genome organization (not to scale) and polyprotein processing ( A ). Cloning strategy and synthesis of genes encoding the C-terminally truncated (transmembrane anchoring domains deleted) forms of the E2 glycoprotein (boxed areas) are shown, together with the signal peptide (horizontal hatching area) and the C-terminal <t>V5</t> <t>epitope</t> tag (slash area) ( B ). Cloning of truncated form of E2 glycoprotein into pJC3 expression vector. Plasmid pJC3 encodes a [GFP-T2A-mCherry] polyprotein encoded by a single open reading frame. Transcription is driven by the human cytomegalovirus enhancer/promoter and the mRNA polyadenylated by the bovine growth hormone polyadenylation signal. Sequences encoding the truncated form of E2 glycoprotein were excised by restriction with ApaI and PstI from the pGEM-T Easy Vector, then inserted to pJC3, similarly restricted, to remove mCherry FP and create plasmid [GFP-T2A-BVDV-E2 trunk] ( C ). The NetNGlyc-1.0 server ( https://services.healthtech.dtu.dk/service.php?NetNGlyc-1.0 ) was used to predict N-glycosylated sites from full-length E2 glycoproteins. An N-glycosylation potential of > 0.5 was the cut-off value for sequences ( D ).
Speci®C Igm Against Vp2 Conformational Epitopes, supplied by Biotrin International, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/speci®c igm against vp2 conformational epitopes/product/Biotrin International
Average 90 stars, based on 1 article reviews
speci®c igm against vp2 conformational epitopes - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier
specific antibodies against vp2 epitopes  (Biotrin International)
90
Biotrin International specific antibodies against vp2 epitopes
Genome structure of BVDV and synthesis of the region encoding the E2 glycoprotein. BVDV genome organization (not to scale) and polyprotein processing ( A ). Cloning strategy and synthesis of genes encoding the C-terminally truncated (transmembrane anchoring domains deleted) forms of the E2 glycoprotein (boxed areas) are shown, together with the signal peptide (horizontal hatching area) and the C-terminal <t>V5</t> <t>epitope</t> tag (slash area) ( B ). Cloning of truncated form of E2 glycoprotein into pJC3 expression vector. Plasmid pJC3 encodes a [GFP-T2A-mCherry] polyprotein encoded by a single open reading frame. Transcription is driven by the human cytomegalovirus enhancer/promoter and the mRNA polyadenylated by the bovine growth hormone polyadenylation signal. Sequences encoding the truncated form of E2 glycoprotein were excised by restriction with ApaI and PstI from the pGEM-T Easy Vector, then inserted to pJC3, similarly restricted, to remove mCherry FP and create plasmid [GFP-T2A-BVDV-E2 trunk] ( C ). The NetNGlyc-1.0 server ( https://services.healthtech.dtu.dk/service.php?NetNGlyc-1.0 ) was used to predict N-glycosylated sites from full-length E2 glycoproteins. An N-glycosylation potential of > 0.5 was the cut-off value for sequences ( D ).
Specific Antibodies Against Vp2 Epitopes, supplied by Biotrin International, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/specific antibodies against vp2 epitopes/product/Biotrin International
Average 90 stars, based on 1 article reviews
specific antibodies against vp2 epitopes - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


Genome structure of BVDV and synthesis of the region encoding the E2 glycoprotein. BVDV genome organization (not to scale) and polyprotein processing ( A ). Cloning strategy and synthesis of genes encoding the C-terminally truncated (transmembrane anchoring domains deleted) forms of the E2 glycoprotein (boxed areas) are shown, together with the signal peptide (horizontal hatching area) and the C-terminal V5 epitope tag (slash area) ( B ). Cloning of truncated form of E2 glycoprotein into pJC3 expression vector. Plasmid pJC3 encodes a [GFP-T2A-mCherry] polyprotein encoded by a single open reading frame. Transcription is driven by the human cytomegalovirus enhancer/promoter and the mRNA polyadenylated by the bovine growth hormone polyadenylation signal. Sequences encoding the truncated form of E2 glycoprotein were excised by restriction with ApaI and PstI from the pGEM-T Easy Vector, then inserted to pJC3, similarly restricted, to remove mCherry FP and create plasmid [GFP-T2A-BVDV-E2 trunk] ( C ). The NetNGlyc-1.0 server ( https://services.healthtech.dtu.dk/service.php?NetNGlyc-1.0 ) was used to predict N-glycosylated sites from full-length E2 glycoproteins. An N-glycosylation potential of > 0.5 was the cut-off value for sequences ( D ).

Journal: Scientific Reports

Article Title: Immunogenicity of a secreted, C-terminally truncated, form of bovine viral diarrhea virus E2 glycoprotein as a potential candidate in subunit vaccine development

doi: 10.1038/s41598-022-26766-y

Figure Lengend Snippet: Genome structure of BVDV and synthesis of the region encoding the E2 glycoprotein. BVDV genome organization (not to scale) and polyprotein processing ( A ). Cloning strategy and synthesis of genes encoding the C-terminally truncated (transmembrane anchoring domains deleted) forms of the E2 glycoprotein (boxed areas) are shown, together with the signal peptide (horizontal hatching area) and the C-terminal V5 epitope tag (slash area) ( B ). Cloning of truncated form of E2 glycoprotein into pJC3 expression vector. Plasmid pJC3 encodes a [GFP-T2A-mCherry] polyprotein encoded by a single open reading frame. Transcription is driven by the human cytomegalovirus enhancer/promoter and the mRNA polyadenylated by the bovine growth hormone polyadenylation signal. Sequences encoding the truncated form of E2 glycoprotein were excised by restriction with ApaI and PstI from the pGEM-T Easy Vector, then inserted to pJC3, similarly restricted, to remove mCherry FP and create plasmid [GFP-T2A-BVDV-E2 trunk] ( C ). The NetNGlyc-1.0 server ( https://services.healthtech.dtu.dk/service.php?NetNGlyc-1.0 ) was used to predict N-glycosylated sites from full-length E2 glycoproteins. An N-glycosylation potential of > 0.5 was the cut-off value for sequences ( D ).

Article Snippet: Supernatants were thawed on ice before being spotted onto a nitrocellulose membrane (0.2 μm; Bio-Rad, Hercules, CA, USA), where they were analyzed using dot blot assay with a monoclonal antibody against the V5 epitope tag (1:8000; MBL International, Nagoya, Japan) or mouse anti-BVDV antiserum (1:4000) as the primary antibody and horseradish peroxidase (HRP)-labelled goat anti-mouse IgG as the secondary antibody (1:8000; KPL, Gaithersburg, MD, USA).

Techniques: Cloning, Expressing, Plasmid Preparation, Glycoproteomics