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cdnas encoding the ectodomains of lamp1  (GenScript corporation)

 
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    Structured Review

    GenScript corporation cdnas encoding the ectodomains of lamp1
    Sd a antigen expression reduces paramyxovirus HN and influenza HA binding to glycoprotein receptors. (A) <t>LAMP1</t> and LAMP1-Sd a glycoproteins were loaded onto the BLI sensor at comparable levels. (B) Lectin characterization of LAMP1 and LAMP1-Sd a using DBA and MAL I. MAL I recognizes Neu5Acα2-3Galβ1-4GlcNAc (a trisaccharide common in N-glycans). (C) BLI analysis to determine the binding kinetics of nanoparticles displaying paramyxovirus HN or influenza HA glycoproteins to LAMP1 and LAMP1-Sd a . Binding was assessed using an established HN-Ni NTA nanoparticle (HN-NPs) system using 3.5×10 10 HN-NPs or HA-NPs per well. Binding of NDV HN-NPs was additionally tested in the presence of site-I specific inhibitor BCX2798 (BCX). Each experiment was conducted at least twice, with representative results displayed here.
    Cdnas Encoding The Ectodomains Of Lamp1, supplied by GenScript corporation, 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/cdnas encoding the ectodomains of lamp1/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    cdnas encoding the ectodomains of lamp1 - by Bioz Stars, 2026-03
    90/100 stars

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    1) Product Images from "Identification of β4GALNT2 as an anti-hPIV3 factor through genome-wide CRISPR/Cas9 library screening"

    Article Title: Identification of β4GALNT2 as an anti-hPIV3 factor through genome-wide CRISPR/Cas9 library screening

    Journal: Emerging Microbes & Infections

    doi: 10.1080/22221751.2025.2529895

    Sd a antigen expression reduces paramyxovirus HN and influenza HA binding to glycoprotein receptors. (A) LAMP1 and LAMP1-Sd a glycoproteins were loaded onto the BLI sensor at comparable levels. (B) Lectin characterization of LAMP1 and LAMP1-Sd a using DBA and MAL I. MAL I recognizes Neu5Acα2-3Galβ1-4GlcNAc (a trisaccharide common in N-glycans). (C) BLI analysis to determine the binding kinetics of nanoparticles displaying paramyxovirus HN or influenza HA glycoproteins to LAMP1 and LAMP1-Sd a . Binding was assessed using an established HN-Ni NTA nanoparticle (HN-NPs) system using 3.5×10 10 HN-NPs or HA-NPs per well. Binding of NDV HN-NPs was additionally tested in the presence of site-I specific inhibitor BCX2798 (BCX). Each experiment was conducted at least twice, with representative results displayed here.
    Figure Legend Snippet: Sd a antigen expression reduces paramyxovirus HN and influenza HA binding to glycoprotein receptors. (A) LAMP1 and LAMP1-Sd a glycoproteins were loaded onto the BLI sensor at comparable levels. (B) Lectin characterization of LAMP1 and LAMP1-Sd a using DBA and MAL I. MAL I recognizes Neu5Acα2-3Galβ1-4GlcNAc (a trisaccharide common in N-glycans). (C) BLI analysis to determine the binding kinetics of nanoparticles displaying paramyxovirus HN or influenza HA glycoproteins to LAMP1 and LAMP1-Sd a . Binding was assessed using an established HN-Ni NTA nanoparticle (HN-NPs) system using 3.5×10 10 HN-NPs or HA-NPs per well. Binding of NDV HN-NPs was additionally tested in the presence of site-I specific inhibitor BCX2798 (BCX). Each experiment was conducted at least twice, with representative results displayed here.

    Techniques Used: Expressing, Binding Assay

    Structural basis for Sd a -mediated disruption of hPIV3 HN-glycan interactions. (A, B) Predicted interactions between hPIV3 HN monomer and ligands using Chai Discovery ( https://lab.chaidiscovery.com ) . Panel (A) illustrates the binding of HN to 3′-sialyl-N-acetyllactosamine (3'SLN), while panel (B) depicts the interaction with the Sd a glycotope. Aromatic residues W371, F372 and W428 are shown in red. (C) Overlay of the predicted interactions, highlighting the differences between the two ligands. The interaction between GalNAc and residues C214 and R129 induces a shift in the entire glycan chain, as indicated by the red arrow. (D) Binding analysis of hPIV3 HN wild-type (WT) and W371A mutant HN-NPs to 3'S(LN) 3 was conducted using BLI, in the presence or absence of the BCX2798 inhibitor, using 3.5×10 10 HN-NPs per well. The difference in the binding curve for hPIV3 HN-NPs compared to C results from the different receptors (LAMP1 vs 3’S[LN] 3 ) being used. All experiments were performed independently in triplicate, with representative data presented.
    Figure Legend Snippet: Structural basis for Sd a -mediated disruption of hPIV3 HN-glycan interactions. (A, B) Predicted interactions between hPIV3 HN monomer and ligands using Chai Discovery ( https://lab.chaidiscovery.com ) . Panel (A) illustrates the binding of HN to 3′-sialyl-N-acetyllactosamine (3'SLN), while panel (B) depicts the interaction with the Sd a glycotope. Aromatic residues W371, F372 and W428 are shown in red. (C) Overlay of the predicted interactions, highlighting the differences between the two ligands. The interaction between GalNAc and residues C214 and R129 induces a shift in the entire glycan chain, as indicated by the red arrow. (D) Binding analysis of hPIV3 HN wild-type (WT) and W371A mutant HN-NPs to 3'S(LN) 3 was conducted using BLI, in the presence or absence of the BCX2798 inhibitor, using 3.5×10 10 HN-NPs per well. The difference in the binding curve for hPIV3 HN-NPs compared to C results from the different receptors (LAMP1 vs 3’S[LN] 3 ) being used. All experiments were performed independently in triplicate, with representative data presented.

    Techniques Used: Disruption, Glycoproteomics, Binding Assay, Mutagenesis



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    cdnas encoding the ectodomains of lamp1  (GenScript corporation)
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    Sd a antigen expression reduces paramyxovirus HN and influenza HA binding to glycoprotein receptors. (A) <t>LAMP1</t> and LAMP1-Sd a glycoproteins were loaded onto the BLI sensor at comparable levels. (B) Lectin characterization of LAMP1 and LAMP1-Sd a using DBA and MAL I. MAL I recognizes Neu5Acα2-3Galβ1-4GlcNAc (a trisaccharide common in N-glycans). (C) BLI analysis to determine the binding kinetics of nanoparticles displaying paramyxovirus HN or influenza HA glycoproteins to LAMP1 and LAMP1-Sd a . Binding was assessed using an established HN-Ni NTA nanoparticle (HN-NPs) system using 3.5×10 10 HN-NPs or HA-NPs per well. Binding of NDV HN-NPs was additionally tested in the presence of site-I specific inhibitor BCX2798 (BCX). Each experiment was conducted at least twice, with representative results displayed here.
    Cdnas Encoding The Ectodomains Of Lamp1, supplied by GenScript corporation, 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/cdnas encoding the ectodomains of lamp1/product/GenScript corporation
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    glycoproteins lamp1 and glycophorin a ectodomain-encoding cdnas  (GenScript corporation)
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    Sd a antigen expression reduces paramyxovirus HN and influenza HA binding to glycoprotein receptors. (A) <t>LAMP1</t> and LAMP1-Sd a glycoproteins were loaded onto the BLI sensor at comparable levels. (B) Lectin characterization of LAMP1 and LAMP1-Sd a using DBA and MAL I. MAL I recognizes Neu5Acα2-3Galβ1-4GlcNAc (a trisaccharide common in N-glycans). (C) BLI analysis to determine the binding kinetics of nanoparticles displaying paramyxovirus HN or influenza HA glycoproteins to LAMP1 and LAMP1-Sd a . Binding was assessed using an established HN-Ni NTA nanoparticle (HN-NPs) system using 3.5×10 10 HN-NPs or HA-NPs per well. Binding of NDV HN-NPs was additionally tested in the presence of site-I specific inhibitor BCX2798 (BCX). Each experiment was conducted at least twice, with representative results displayed here.
    Glycoproteins Lamp1 And Glycophorin A Ectodomain Encoding Cdnas, supplied by GenScript corporation, 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/glycoproteins lamp1 and glycophorin a ectodomain-encoding cdnas/product/GenScript corporation
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    Image Search Results


    Sd a antigen expression reduces paramyxovirus HN and influenza HA binding to glycoprotein receptors. (A) LAMP1 and LAMP1-Sd a glycoproteins were loaded onto the BLI sensor at comparable levels. (B) Lectin characterization of LAMP1 and LAMP1-Sd a using DBA and MAL I. MAL I recognizes Neu5Acα2-3Galβ1-4GlcNAc (a trisaccharide common in N-glycans). (C) BLI analysis to determine the binding kinetics of nanoparticles displaying paramyxovirus HN or influenza HA glycoproteins to LAMP1 and LAMP1-Sd a . Binding was assessed using an established HN-Ni NTA nanoparticle (HN-NPs) system using 3.5×10 10 HN-NPs or HA-NPs per well. Binding of NDV HN-NPs was additionally tested in the presence of site-I specific inhibitor BCX2798 (BCX). Each experiment was conducted at least twice, with representative results displayed here.

    Journal: Emerging Microbes & Infections

    Article Title: Identification of β4GALNT2 as an anti-hPIV3 factor through genome-wide CRISPR/Cas9 library screening

    doi: 10.1080/22221751.2025.2529895

    Figure Lengend Snippet: Sd a antigen expression reduces paramyxovirus HN and influenza HA binding to glycoprotein receptors. (A) LAMP1 and LAMP1-Sd a glycoproteins were loaded onto the BLI sensor at comparable levels. (B) Lectin characterization of LAMP1 and LAMP1-Sd a using DBA and MAL I. MAL I recognizes Neu5Acα2-3Galβ1-4GlcNAc (a trisaccharide common in N-glycans). (C) BLI analysis to determine the binding kinetics of nanoparticles displaying paramyxovirus HN or influenza HA glycoproteins to LAMP1 and LAMP1-Sd a . Binding was assessed using an established HN-Ni NTA nanoparticle (HN-NPs) system using 3.5×10 10 HN-NPs or HA-NPs per well. Binding of NDV HN-NPs was additionally tested in the presence of site-I specific inhibitor BCX2798 (BCX). Each experiment was conducted at least twice, with representative results displayed here.

    Article Snippet: Human codon-optimized cDNAs encoding the ectodomains of LAMP1 (GenScript) were cloned into the pCAGGS vector ( pCAGGS-LAMP1 ), incorporating a C-terminal Twin-Strep tag, a biotin-acceptor peptide (BAP; GGLNDIFEAQKIEWH) for site-specific biotinylation by BirA, and a 6xHis tag for purification using Ni-NTA beads [ ].

    Techniques: Expressing, Binding Assay

    Structural basis for Sd a -mediated disruption of hPIV3 HN-glycan interactions. (A, B) Predicted interactions between hPIV3 HN monomer and ligands using Chai Discovery ( https://lab.chaidiscovery.com ) . Panel (A) illustrates the binding of HN to 3′-sialyl-N-acetyllactosamine (3'SLN), while panel (B) depicts the interaction with the Sd a glycotope. Aromatic residues W371, F372 and W428 are shown in red. (C) Overlay of the predicted interactions, highlighting the differences between the two ligands. The interaction between GalNAc and residues C214 and R129 induces a shift in the entire glycan chain, as indicated by the red arrow. (D) Binding analysis of hPIV3 HN wild-type (WT) and W371A mutant HN-NPs to 3'S(LN) 3 was conducted using BLI, in the presence or absence of the BCX2798 inhibitor, using 3.5×10 10 HN-NPs per well. The difference in the binding curve for hPIV3 HN-NPs compared to C results from the different receptors (LAMP1 vs 3’S[LN] 3 ) being used. All experiments were performed independently in triplicate, with representative data presented.

    Journal: Emerging Microbes & Infections

    Article Title: Identification of β4GALNT2 as an anti-hPIV3 factor through genome-wide CRISPR/Cas9 library screening

    doi: 10.1080/22221751.2025.2529895

    Figure Lengend Snippet: Structural basis for Sd a -mediated disruption of hPIV3 HN-glycan interactions. (A, B) Predicted interactions between hPIV3 HN monomer and ligands using Chai Discovery ( https://lab.chaidiscovery.com ) . Panel (A) illustrates the binding of HN to 3′-sialyl-N-acetyllactosamine (3'SLN), while panel (B) depicts the interaction with the Sd a glycotope. Aromatic residues W371, F372 and W428 are shown in red. (C) Overlay of the predicted interactions, highlighting the differences between the two ligands. The interaction between GalNAc and residues C214 and R129 induces a shift in the entire glycan chain, as indicated by the red arrow. (D) Binding analysis of hPIV3 HN wild-type (WT) and W371A mutant HN-NPs to 3'S(LN) 3 was conducted using BLI, in the presence or absence of the BCX2798 inhibitor, using 3.5×10 10 HN-NPs per well. The difference in the binding curve for hPIV3 HN-NPs compared to C results from the different receptors (LAMP1 vs 3’S[LN] 3 ) being used. All experiments were performed independently in triplicate, with representative data presented.

    Article Snippet: Human codon-optimized cDNAs encoding the ectodomains of LAMP1 (GenScript) were cloned into the pCAGGS vector ( pCAGGS-LAMP1 ), incorporating a C-terminal Twin-Strep tag, a biotin-acceptor peptide (BAP; GGLNDIFEAQKIEWH) for site-specific biotinylation by BirA, and a 6xHis tag for purification using Ni-NTA beads [ ].

    Techniques: Disruption, Glycoproteomics, Binding Assay, Mutagenesis