length ha0  (Sino Biological)


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    Structured Review

    Sino Biological length ha0
    Binding of the sdAbs to the B-Victoria single residue mutant <t>HA0’s.</t> Candidate single residue mutations predicted to correlate with lineage-specific binding and a naturally occurring substitution H122Q, which differentiated between the B-Victoria and B-Yamagata strains, were generated and binding was tested using yeast display and flow cytometry. ( A ) Detection of the HA0 display level, using detection of the SV5 epitope tag attached to the HA0, showing that the mutations had no effect on the HA0 display level relative to the wild-type (wt) HA0 (indicated by vertical arrow). ( B ) Flow cytometry histograms showing binding of the Vic2a-6, Vic2a-20, Vic2b-3 and the YamNGS#1 to the wild-type HA (B/Brisbane/60/2008 precursor HA0) and selected mutants (the positive population is the right peak, whereas, the left peak shows the unbound and unstained populations). Mutations that completely eliminated sdAb binding are shown in red, those that partially affected binding are shown in orange and those that had no effect are shown in green. We determined the extent of sdAb binding by dividing the geometric mean fluorescence intensity (MFI) of each sdAb mutant pair by the value of the MFI of the wild-type B-Vic HA sdAb interaction and the resulting ratio, normalised to a percentage value of the wild-type interaction. Relative binding of the sdAbs was categorised as ‘no binding’ (in red)—
    Length Ha0, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/length ha0/product/Sino Biological
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    length ha0 - by Bioz Stars, 2021-02
    92/100 stars

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    b-victoria ha1
    ha1

    Images

    1) Product Images from "Cross-Reactive and Lineage-Specific Single Domain Antibodies against Influenza B Hemagglutinin"

    Article Title: Cross-Reactive and Lineage-Specific Single Domain Antibodies against Influenza B Hemagglutinin

    Journal: Antibodies

    doi: 10.3390/antib8010014

    Binding of the sdAbs to the B-Victoria single residue mutant HA0’s. Candidate single residue mutations predicted to correlate with lineage-specific binding and a naturally occurring substitution H122Q, which differentiated between the B-Victoria and B-Yamagata strains, were generated and binding was tested using yeast display and flow cytometry. ( A ) Detection of the HA0 display level, using detection of the SV5 epitope tag attached to the HA0, showing that the mutations had no effect on the HA0 display level relative to the wild-type (wt) HA0 (indicated by vertical arrow). ( B ) Flow cytometry histograms showing binding of the Vic2a-6, Vic2a-20, Vic2b-3 and the YamNGS#1 to the wild-type HA (B/Brisbane/60/2008 precursor HA0) and selected mutants (the positive population is the right peak, whereas, the left peak shows the unbound and unstained populations). Mutations that completely eliminated sdAb binding are shown in red, those that partially affected binding are shown in orange and those that had no effect are shown in green. We determined the extent of sdAb binding by dividing the geometric mean fluorescence intensity (MFI) of each sdAb mutant pair by the value of the MFI of the wild-type B-Vic HA sdAb interaction and the resulting ratio, normalised to a percentage value of the wild-type interaction. Relative binding of the sdAbs was categorised as ‘no binding’ (in red)—
    Figure Legend Snippet: Binding of the sdAbs to the B-Victoria single residue mutant HA0’s. Candidate single residue mutations predicted to correlate with lineage-specific binding and a naturally occurring substitution H122Q, which differentiated between the B-Victoria and B-Yamagata strains, were generated and binding was tested using yeast display and flow cytometry. ( A ) Detection of the HA0 display level, using detection of the SV5 epitope tag attached to the HA0, showing that the mutations had no effect on the HA0 display level relative to the wild-type (wt) HA0 (indicated by vertical arrow). ( B ) Flow cytometry histograms showing binding of the Vic2a-6, Vic2a-20, Vic2b-3 and the YamNGS#1 to the wild-type HA (B/Brisbane/60/2008 precursor HA0) and selected mutants (the positive population is the right peak, whereas, the left peak shows the unbound and unstained populations). Mutations that completely eliminated sdAb binding are shown in red, those that partially affected binding are shown in orange and those that had no effect are shown in green. We determined the extent of sdAb binding by dividing the geometric mean fluorescence intensity (MFI) of each sdAb mutant pair by the value of the MFI of the wild-type B-Vic HA sdAb interaction and the resulting ratio, normalised to a percentage value of the wild-type interaction. Relative binding of the sdAbs was categorised as ‘no binding’ (in red)—

    Techniques Used: Binding Assay, Mutagenesis, Generated, Flow Cytometry, Fluorescence

    Correlation of the sdAb epitopes with the Hemagglutinin structure. The structure of the HA0 monomer (B/Brisbane/60/2008 PDB structure 4FQM) is shown with the HA1 domain in blue, the stem region in grey, the 120 loop in yellow and the receptor binding site (RBS) in green. The residue of H122 and N129 associated with the B-Victoria lineage-specific binding of the sdAb Vic2a-6 or preferred binding of the Vic2a-20 are shown in red. The binding specificity of the sdAb panel are shown in relation to the HA head and stem region.
    Figure Legend Snippet: Correlation of the sdAb epitopes with the Hemagglutinin structure. The structure of the HA0 monomer (B/Brisbane/60/2008 PDB structure 4FQM) is shown with the HA1 domain in blue, the stem region in grey, the 120 loop in yellow and the receptor binding site (RBS) in green. The residue of H122 and N129 associated with the B-Victoria lineage-specific binding of the sdAb Vic2a-6 or preferred binding of the Vic2a-20 are shown in red. The binding specificity of the sdAb panel are shown in relation to the HA head and stem region.

    Techniques Used: Binding Assay

    ELISA showing sdAb binding to the recombinant hemagglutinin (HA0). sdAb binding to the recombinant HA0 from Influenza B-virus lineage representative strains used in immunisations and phage display library selections. B-Vic is B/Brisbane/60/2008, B-Yam is B/Florida/04/2006. Control sdAb A2c-3 is specific for influenza A hemagglutinin, PBS is a no sdAb negative control. ELISA signal is an average of 2 assays.
    Figure Legend Snippet: ELISA showing sdAb binding to the recombinant hemagglutinin (HA0). sdAb binding to the recombinant HA0 from Influenza B-virus lineage representative strains used in immunisations and phage display library selections. B-Vic is B/Brisbane/60/2008, B-Yam is B/Florida/04/2006. Control sdAb A2c-3 is specific for influenza A hemagglutinin, PBS is a no sdAb negative control. ELISA signal is an average of 2 assays.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Binding Assay, Recombinant, Negative Control

    Related Articles

    Recombinant:

    Article Title: Cross-Reactive and Lineage-Specific Single Domain Antibodies against Influenza B Hemagglutinin
    Article Snippet: .. Binding the full length HA0 or the head domain, HA1, of hemagglutinin was evaluated using the recombinant B-Victoria HA0, B/Brisbane/60/2008, and B-Yamagata HA0, B/Florida/04/2006, (Protein SciencesTM) or B-Victoria HA1, B/Brisbane/60/2008, and B-Yamagata HA1, B/Florida/04/2006 (Sino Biological Inc., Beijing, China). .. Next-Generation-Sequence-Assisted Single Domain Antibody Discovery Plasmid DNA was extracted from E. coli cultures grown from pre- and post-selection libraries , to obtain template DNA for the next-generation sequencing (NGS).

    Binding Assay:

    Article Title: Cross-Reactive and Lineage-Specific Single Domain Antibodies against Influenza B Hemagglutinin
    Article Snippet: .. Binding the full length HA0 or the head domain, HA1, of hemagglutinin was evaluated using the recombinant B-Victoria HA0, B/Brisbane/60/2008, and B-Yamagata HA0, B/Florida/04/2006, (Protein SciencesTM) or B-Victoria HA1, B/Brisbane/60/2008, and B-Yamagata HA1, B/Florida/04/2006 (Sino Biological Inc., Beijing, China). .. Next-Generation-Sequence-Assisted Single Domain Antibody Discovery Plasmid DNA was extracted from E. coli cultures grown from pre- and post-selection libraries , to obtain template DNA for the next-generation sequencing (NGS).

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    • length ha0  (Sino Biological)
    92
    Sino Biological length ha0
    Binding of the sdAbs to the B-Victoria single residue mutant <t>HA0’s.</t> Candidate single residue mutations predicted to correlate with lineage-specific binding and a naturally occurring substitution H122Q, which differentiated between the B-Victoria and B-Yamagata strains, were generated and binding was tested using yeast display and flow cytometry. ( A ) Detection of the HA0 display level, using detection of the SV5 epitope tag attached to the HA0, showing that the mutations had no effect on the HA0 display level relative to the wild-type (wt) HA0 (indicated by vertical arrow). ( B ) Flow cytometry histograms showing binding of the Vic2a-6, Vic2a-20, Vic2b-3 and the YamNGS#1 to the wild-type HA (B/Brisbane/60/2008 precursor HA0) and selected mutants (the positive population is the right peak, whereas, the left peak shows the unbound and unstained populations). Mutations that completely eliminated sdAb binding are shown in red, those that partially affected binding are shown in orange and those that had no effect are shown in green. We determined the extent of sdAb binding by dividing the geometric mean fluorescence intensity (MFI) of each sdAb mutant pair by the value of the MFI of the wild-type B-Vic HA sdAb interaction and the resulting ratio, normalised to a percentage value of the wild-type interaction. Relative binding of the sdAbs was categorised as ‘no binding’ (in red)—
    Length Ha0, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/length ha0/product/Sino Biological
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    length ha0 - by Bioz Stars, 2021-02
    92/100 stars
    		  Buy from Supplier

    Image Search Results


    Binding of the sdAbs to the B-Victoria single residue mutant HA0’s. Candidate single residue mutations predicted to correlate with lineage-specific binding and a naturally occurring substitution H122Q, which differentiated between the B-Victoria and B-Yamagata strains, were generated and binding was tested using yeast display and flow cytometry. ( A ) Detection of the HA0 display level, using detection of the SV5 epitope tag attached to the HA0, showing that the mutations had no effect on the HA0 display level relative to the wild-type (wt) HA0 (indicated by vertical arrow). ( B ) Flow cytometry histograms showing binding of the Vic2a-6, Vic2a-20, Vic2b-3 and the YamNGS#1 to the wild-type HA (B/Brisbane/60/2008 precursor HA0) and selected mutants (the positive population is the right peak, whereas, the left peak shows the unbound and unstained populations). Mutations that completely eliminated sdAb binding are shown in red, those that partially affected binding are shown in orange and those that had no effect are shown in green. We determined the extent of sdAb binding by dividing the geometric mean fluorescence intensity (MFI) of each sdAb mutant pair by the value of the MFI of the wild-type B-Vic HA sdAb interaction and the resulting ratio, normalised to a percentage value of the wild-type interaction. Relative binding of the sdAbs was categorised as ‘no binding’ (in red)—

    Journal: Antibodies

    Article Title: Cross-Reactive and Lineage-Specific Single Domain Antibodies against Influenza B Hemagglutinin

    doi: 10.3390/antib8010014

    Figure Lengend Snippet: Binding of the sdAbs to the B-Victoria single residue mutant HA0’s. Candidate single residue mutations predicted to correlate with lineage-specific binding and a naturally occurring substitution H122Q, which differentiated between the B-Victoria and B-Yamagata strains, were generated and binding was tested using yeast display and flow cytometry. ( A ) Detection of the HA0 display level, using detection of the SV5 epitope tag attached to the HA0, showing that the mutations had no effect on the HA0 display level relative to the wild-type (wt) HA0 (indicated by vertical arrow). ( B ) Flow cytometry histograms showing binding of the Vic2a-6, Vic2a-20, Vic2b-3 and the YamNGS#1 to the wild-type HA (B/Brisbane/60/2008 precursor HA0) and selected mutants (the positive population is the right peak, whereas, the left peak shows the unbound and unstained populations). Mutations that completely eliminated sdAb binding are shown in red, those that partially affected binding are shown in orange and those that had no effect are shown in green. We determined the extent of sdAb binding by dividing the geometric mean fluorescence intensity (MFI) of each sdAb mutant pair by the value of the MFI of the wild-type B-Vic HA sdAb interaction and the resulting ratio, normalised to a percentage value of the wild-type interaction. Relative binding of the sdAbs was categorised as ‘no binding’ (in red)—

    Article Snippet: Binding the full length HA0 or the head domain, HA1, of hemagglutinin was evaluated using the recombinant B-Victoria HA0, B/Brisbane/60/2008, and B-Yamagata HA0, B/Florida/04/2006, (Protein SciencesTM) or B-Victoria HA1, B/Brisbane/60/2008, and B-Yamagata HA1, B/Florida/04/2006 (Sino Biological Inc., Beijing, China).

    Techniques: Binding Assay, Mutagenesis, Generated, Flow Cytometry, Fluorescence

    Correlation of the sdAb epitopes with the Hemagglutinin structure. The structure of the HA0 monomer (B/Brisbane/60/2008 PDB structure 4FQM) is shown with the HA1 domain in blue, the stem region in grey, the 120 loop in yellow and the receptor binding site (RBS) in green. The residue of H122 and N129 associated with the B-Victoria lineage-specific binding of the sdAb Vic2a-6 or preferred binding of the Vic2a-20 are shown in red. The binding specificity of the sdAb panel are shown in relation to the HA head and stem region.

    Journal: Antibodies

    Article Title: Cross-Reactive and Lineage-Specific Single Domain Antibodies against Influenza B Hemagglutinin

    doi: 10.3390/antib8010014

    Figure Lengend Snippet: Correlation of the sdAb epitopes with the Hemagglutinin structure. The structure of the HA0 monomer (B/Brisbane/60/2008 PDB structure 4FQM) is shown with the HA1 domain in blue, the stem region in grey, the 120 loop in yellow and the receptor binding site (RBS) in green. The residue of H122 and N129 associated with the B-Victoria lineage-specific binding of the sdAb Vic2a-6 or preferred binding of the Vic2a-20 are shown in red. The binding specificity of the sdAb panel are shown in relation to the HA head and stem region.

    Article Snippet: Binding the full length HA0 or the head domain, HA1, of hemagglutinin was evaluated using the recombinant B-Victoria HA0, B/Brisbane/60/2008, and B-Yamagata HA0, B/Florida/04/2006, (Protein SciencesTM) or B-Victoria HA1, B/Brisbane/60/2008, and B-Yamagata HA1, B/Florida/04/2006 (Sino Biological Inc., Beijing, China).

    Techniques: Binding Assay

    ELISA showing sdAb binding to the recombinant hemagglutinin (HA0). sdAb binding to the recombinant HA0 from Influenza B-virus lineage representative strains used in immunisations and phage display library selections. B-Vic is B/Brisbane/60/2008, B-Yam is B/Florida/04/2006. Control sdAb A2c-3 is specific for influenza A hemagglutinin, PBS is a no sdAb negative control. ELISA signal is an average of 2 assays.

    Journal: Antibodies

    Article Title: Cross-Reactive and Lineage-Specific Single Domain Antibodies against Influenza B Hemagglutinin

    doi: 10.3390/antib8010014

    Figure Lengend Snippet: ELISA showing sdAb binding to the recombinant hemagglutinin (HA0). sdAb binding to the recombinant HA0 from Influenza B-virus lineage representative strains used in immunisations and phage display library selections. B-Vic is B/Brisbane/60/2008, B-Yam is B/Florida/04/2006. Control sdAb A2c-3 is specific for influenza A hemagglutinin, PBS is a no sdAb negative control. ELISA signal is an average of 2 assays.

    Article Snippet: Binding the full length HA0 or the head domain, HA1, of hemagglutinin was evaluated using the recombinant B-Victoria HA0, B/Brisbane/60/2008, and B-Yamagata HA0, B/Florida/04/2006, (Protein SciencesTM) or B-Victoria HA1, B/Brisbane/60/2008, and B-Yamagata HA1, B/Florida/04/2006 (Sino Biological Inc., Beijing, China).

    Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Recombinant, Negative Control