Review



bnabs targeting ha stalk region  (Creative Biolabs)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 86
      Buy from Supplier

    Structured Review

    Creative Biolabs bnabs targeting ha stalk region
    Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of <t>bNAbs</t> <t>CR6261</t> ( D ), <t>CR9114</t> ( E ), and <t>FI6v3</t> ( F ). Structure 3UBE was used for modeling .
    Bnabs Targeting Ha Stalk Region, supplied by Creative Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bnabs targeting ha stalk region/product/Creative Biolabs
    Average 86 stars, based on 1 article reviews
    bnabs targeting ha stalk region - by Bioz Stars, 2026-05
    86/100 stars

    Images

    1) Product Images from "Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus"

    Article Title: Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus

    Journal: Viruses

    doi: 10.3390/v18010032

    Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of bNAbs CR6261 ( D ), CR9114 ( E ), and FI6v3 ( F ). Structure 3UBE was used for modeling .
    Figure Legend Snippet: Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of bNAbs CR6261 ( D ), CR9114 ( E ), and FI6v3 ( F ). Structure 3UBE was used for modeling .

    Techniques Used: Binding Assay

    Binding of stem-binding bNAbs to TN09 and PR18 viruses. Binding of mAbs to virus was analyzed by ELISA assay. CR6261 ( A , F ), CR9114 ( B , G ), FI6V3 ( C , H ), and CT149 ( E , I ) are broadly reactive antibodies targeting the central HA stem epitope. 2-12C ( E , J ) binds to HA globular head and was used as a control. ( A – E ) Binding to TN09 viruses. ( F – J ) Binding to PR18 viruses. The data was from two biological replicates. The error bars are the average with standard deviation. Ordinary two-way ANOVA was used for statistical analysis, followed by Tukey’s multiple comparison test. *** p < 0.001, **** p < 0.0001.
    Figure Legend Snippet: Binding of stem-binding bNAbs to TN09 and PR18 viruses. Binding of mAbs to virus was analyzed by ELISA assay. CR6261 ( A , F ), CR9114 ( B , G ), FI6V3 ( C , H ), and CT149 ( E , I ) are broadly reactive antibodies targeting the central HA stem epitope. 2-12C ( E , J ) binds to HA globular head and was used as a control. ( A – E ) Binding to TN09 viruses. ( F – J ) Binding to PR18 viruses. The data was from two biological replicates. The error bars are the average with standard deviation. Ordinary two-way ANOVA was used for statistical analysis, followed by Tukey’s multiple comparison test. *** p < 0.001, **** p < 0.0001.

    Techniques Used: Binding Assay, Virus, Enzyme-linked Immunosorbent Assay, Control, Standard Deviation, Comparison

    Binding of bNAbs to PR18-based viruses. The binding affinity was analyzed by ELISA assay. CR6261 ( A ), CR9114 ( B ), FI6V3 ( C ), and CT149 ( D ) are broadly reactive antibodies targeting on HA stalk region. 2-12C ( E ) binds to HA globular head as a control. Data was combined from two biological replicates. The error bars are the average with standard deviation. Two-way ANOVA with Tukey’s multiple comparison test was used for statistical analysis. ** p < 0.01, **** p < 0.0001.
    Figure Legend Snippet: Binding of bNAbs to PR18-based viruses. The binding affinity was analyzed by ELISA assay. CR6261 ( A ), CR9114 ( B ), FI6V3 ( C ), and CT149 ( D ) are broadly reactive antibodies targeting on HA stalk region. 2-12C ( E ) binds to HA globular head as a control. Data was combined from two biological replicates. The error bars are the average with standard deviation. Two-way ANOVA with Tukey’s multiple comparison test was used for statistical analysis. ** p < 0.01, **** p < 0.0001.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Control, Standard Deviation, Comparison



    Similar Products

    bnabs targeting ha stalk region  (Creative Biolabs)
    86
    Creative Biolabs bnabs targeting ha stalk region
    Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of <t>bNAbs</t> <t>CR6261</t> ( D ), <t>CR9114</t> ( E ), and <t>FI6v3</t> ( F ). Structure 3UBE was used for modeling .
    Bnabs Targeting Ha Stalk Region, supplied by Creative Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bnabs targeting ha stalk region/product/Creative Biolabs
    Average 86 stars, based on 1 article reviews
    bnabs targeting ha stalk region - by Bioz Stars, 2026-05
    86/100 stars
    		  Buy from Supplier

    Image Search Results


    Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of bNAbs CR6261 ( D ), CR9114 ( E ), and FI6v3 ( F ). Structure 3UBE was used for modeling .

    Journal: Viruses

    Article Title: Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus

    doi: 10.3390/v18010032

    Figure Lengend Snippet: Structure of the H1N1 HA trimer ectodomain, including bNAb epitopes and resistance mutations. For clarity, two protomers are colored gray while one is color-coded as follows: HA1 stem (blue), HA1 head (green), and HA2 ectodomain (orange). ( A ) HA ectodomain with α-helices A, C, and D notated along with residues HA2-A44, HA2-I77M, and HA1-E227 shown as magenta spheres. The residues constituting a binding pocket for A44 (HA2 W21, Y110, and N114) are shown as yellow spheres. ( B ) 45-degree rotation of the HA trimer showing the packing of A44 (magenta) into its pocket (yellow spheres). The dotted rectangle defines the zoomed-in focus of panels ( C – F ). ( C ) Close-up view of A44 in addition to identification of residues HA2-E47 and HA1-E31. ( D – F ) Binding sites of bNAbs CR6261 ( D ), CR9114 ( E ), and FI6v3 ( F ). Structure 3UBE was used for modeling .

    Article Snippet: Four bNAbs targeting HA stalk region (CR6261, CR9114, FI6V3, and CT149; Creative Biolabs, NY, USA), and one antibody targeting the head region (2-12C) were used in this study.

    Techniques: Binding Assay

    Binding of stem-binding bNAbs to TN09 and PR18 viruses. Binding of mAbs to virus was analyzed by ELISA assay. CR6261 ( A , F ), CR9114 ( B , G ), FI6V3 ( C , H ), and CT149 ( E , I ) are broadly reactive antibodies targeting the central HA stem epitope. 2-12C ( E , J ) binds to HA globular head and was used as a control. ( A – E ) Binding to TN09 viruses. ( F – J ) Binding to PR18 viruses. The data was from two biological replicates. The error bars are the average with standard deviation. Ordinary two-way ANOVA was used for statistical analysis, followed by Tukey’s multiple comparison test. *** p < 0.001, **** p < 0.0001.

    Journal: Viruses

    Article Title: Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus

    doi: 10.3390/v18010032

    Figure Lengend Snippet: Binding of stem-binding bNAbs to TN09 and PR18 viruses. Binding of mAbs to virus was analyzed by ELISA assay. CR6261 ( A , F ), CR9114 ( B , G ), FI6V3 ( C , H ), and CT149 ( E , I ) are broadly reactive antibodies targeting the central HA stem epitope. 2-12C ( E , J ) binds to HA globular head and was used as a control. ( A – E ) Binding to TN09 viruses. ( F – J ) Binding to PR18 viruses. The data was from two biological replicates. The error bars are the average with standard deviation. Ordinary two-way ANOVA was used for statistical analysis, followed by Tukey’s multiple comparison test. *** p < 0.001, **** p < 0.0001.

    Article Snippet: Four bNAbs targeting HA stalk region (CR6261, CR9114, FI6V3, and CT149; Creative Biolabs, NY, USA), and one antibody targeting the head region (2-12C) were used in this study.

    Techniques: Binding Assay, Virus, Enzyme-linked Immunosorbent Assay, Control, Standard Deviation, Comparison

    Binding of bNAbs to PR18-based viruses. The binding affinity was analyzed by ELISA assay. CR6261 ( A ), CR9114 ( B ), FI6V3 ( C ), and CT149 ( D ) are broadly reactive antibodies targeting on HA stalk region. 2-12C ( E ) binds to HA globular head as a control. Data was combined from two biological replicates. The error bars are the average with standard deviation. Two-way ANOVA with Tukey’s multiple comparison test was used for statistical analysis. ** p < 0.01, **** p < 0.0001.

    Journal: Viruses

    Article Title: Resistance Mutations to Broadly Neutralizing Antibodies Destabilize Hemagglutinin and Attenuate H1N1 Influenza Virus

    doi: 10.3390/v18010032

    Figure Lengend Snippet: Binding of bNAbs to PR18-based viruses. The binding affinity was analyzed by ELISA assay. CR6261 ( A ), CR9114 ( B ), FI6V3 ( C ), and CT149 ( D ) are broadly reactive antibodies targeting on HA stalk region. 2-12C ( E ) binds to HA globular head as a control. Data was combined from two biological replicates. The error bars are the average with standard deviation. Two-way ANOVA with Tukey’s multiple comparison test was used for statistical analysis. ** p < 0.01, **** p < 0.0001.

    Article Snippet: Four bNAbs targeting HA stalk region (CR6261, CR9114, FI6V3, and CT149; Creative Biolabs, NY, USA), and one antibody targeting the head region (2-12C) were used in this study.

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Control, Standard Deviation, Comparison