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denv1 ns1 v1  (Native Antigen Inc)


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    Structured Review

    Native Antigen Inc denv1 ns1 v1
    A Unnatural bases in XenoAptamers. The Ds−diol-Px pair is utilized in PCR as a third base pair in the ExSELEX process. B Secondary structures of three <t>XenoAptamers</t> <t>targeting</t> <t>DENV1-NS1-v1</t> (AptD1), DENV1-NS1-v1 and -v2 (AptD1c), and DENV2-NS1 (AptD2). C Binding analysis of anti-DENV1-NS1-XenoAptamers with the NS1 variants (DENV1-NS1-v1 and v2) by an electrophoretic mobility shift assay (EMSA) in the presence of 3 M urea at 30°C. The experiment was performed once. D EMSA-based binding analysis of AptD2 derivatives containing substituted Pa'35 variant bases. The experiment was performed in duplicate. E K D values of AptD2 and its derivatives, AptD2-Pa′ and AptD2-Pa′ (diol), determined by SPR.
    Denv1 Ns1 V1, supplied by Native Antigen Inc, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/denv1 ns1 v1/product/Native Antigen Inc
    Average 92 stars, based on 13 article reviews
    denv1 ns1 v1 - by Bioz Stars, 2026-02
    92/100 stars

    Images

    1) Product Images from "Expanded genetic alphabet increases structural and chemical diversity of six-letter DNA for high-affinity protein-targeting aptamers"

    Article Title: Expanded genetic alphabet increases structural and chemical diversity of six-letter DNA for high-affinity protein-targeting aptamers

    Journal: Nature Communications

    doi: 10.1038/s41467-025-67486-x

    A Unnatural bases in XenoAptamers. The Ds−diol-Px pair is utilized in PCR as a third base pair in the ExSELEX process. B Secondary structures of three XenoAptamers targeting DENV1-NS1-v1 (AptD1), DENV1-NS1-v1 and -v2 (AptD1c), and DENV2-NS1 (AptD2). C Binding analysis of anti-DENV1-NS1-XenoAptamers with the NS1 variants (DENV1-NS1-v1 and v2) by an electrophoretic mobility shift assay (EMSA) in the presence of 3 M urea at 30°C. The experiment was performed once. D EMSA-based binding analysis of AptD2 derivatives containing substituted Pa'35 variant bases. The experiment was performed in duplicate. E K D values of AptD2 and its derivatives, AptD2-Pa′ and AptD2-Pa′ (diol), determined by SPR.
    Figure Legend Snippet: A Unnatural bases in XenoAptamers. The Ds−diol-Px pair is utilized in PCR as a third base pair in the ExSELEX process. B Secondary structures of three XenoAptamers targeting DENV1-NS1-v1 (AptD1), DENV1-NS1-v1 and -v2 (AptD1c), and DENV2-NS1 (AptD2). C Binding analysis of anti-DENV1-NS1-XenoAptamers with the NS1 variants (DENV1-NS1-v1 and v2) by an electrophoretic mobility shift assay (EMSA) in the presence of 3 M urea at 30°C. The experiment was performed once. D EMSA-based binding analysis of AptD2 derivatives containing substituted Pa'35 variant bases. The experiment was performed in duplicate. E K D values of AptD2 and its derivatives, AptD2-Pa′ and AptD2-Pa′ (diol), determined by SPR.

    Techniques Used: Binding Assay, Electrophoretic Mobility Shift Assay, Variant Assay

    A–C Cryo-EM density maps of AptD1 with DENV1-NS1-v1 (hexamer) ( A ), AptD1c with DENV1-NS1-v2 (tetramer) ( B ), and AptD2 with DENV2-NS1 (dimer) ( C ). D–F Cryo-EM structures of XenoAptamers with their respective NS1 proteins. In the figures, only one XenoAptamer and one dimer of NS1 are shown. G – I The electrostatic surface potential models of NS1 show the XenoAptamers’ recognition of the positively charged surfaces of NS1 proteins ( G–I ). J–L Cryo-EM structures of XenoAptamers, in which the unnatural bases Ds and Pa′ are shown in yellow and black, respectively.
    Figure Legend Snippet: A–C Cryo-EM density maps of AptD1 with DENV1-NS1-v1 (hexamer) ( A ), AptD1c with DENV1-NS1-v2 (tetramer) ( B ), and AptD2 with DENV2-NS1 (dimer) ( C ). D–F Cryo-EM structures of XenoAptamers with their respective NS1 proteins. In the figures, only one XenoAptamer and one dimer of NS1 are shown. G – I The electrostatic surface potential models of NS1 show the XenoAptamers’ recognition of the positively charged surfaces of NS1 proteins ( G–I ). J–L Cryo-EM structures of XenoAptamers, in which the unnatural bases Ds and Pa′ are shown in yellow and black, respectively.

    Techniques Used: Cryo-EM Sample Prep

    A , B The overall structure of DENV1-NS1-v1 is complexed with AptD1 (green). In the XenoAptamer structures, the unnatural Ds bases are shown in yellow. One protomer of NS1 protein is colored dark blue (β-roll domain), orange (connector subdomain), yellow (wing domain), and pink (β-ladder domain), while the other is shown in light colors. The residues interacting with AptD1 are highlighted in red. C–E DENV1-NS1-v1 recognition of AptD1 in the positively-charged cleft ( C , D ) and at the outer surface ( E ).
    Figure Legend Snippet: A , B The overall structure of DENV1-NS1-v1 is complexed with AptD1 (green). In the XenoAptamer structures, the unnatural Ds bases are shown in yellow. One protomer of NS1 protein is colored dark blue (β-roll domain), orange (connector subdomain), yellow (wing domain), and pink (β-ladder domain), while the other is shown in light colors. The residues interacting with AptD1 are highlighted in red. C–E DENV1-NS1-v1 recognition of AptD1 in the positively-charged cleft ( C , D ) and at the outer surface ( E ).

    Techniques Used:

    A , B Overall structure ( A ) and cleft-focused structure ( B ) of DENV1-NS1-v2 with AptD1c (green). In the XenoAptamer structures, the unnatural bases Ds are shown in yellow. One protomer of NS1 protein is colored dark blue (β-roll domain), orange (connector subdomain), yellow (wing domain), and pink (β-ladder domain), while the other is shown in light colors. The residues interacting with AptD1 are highlighted in red. ( C–H ) DENV1-NS1-v1 recognition of AptD1c in the positively-charged cleft ( C–F ) and at the outer surface ( G , H ).
    Figure Legend Snippet: A , B Overall structure ( A ) and cleft-focused structure ( B ) of DENV1-NS1-v2 with AptD1c (green). In the XenoAptamer structures, the unnatural bases Ds are shown in yellow. One protomer of NS1 protein is colored dark blue (β-roll domain), orange (connector subdomain), yellow (wing domain), and pink (β-ladder domain), while the other is shown in light colors. The residues interacting with AptD1 are highlighted in red. ( C–H ) DENV1-NS1-v1 recognition of AptD1c in the positively-charged cleft ( C–F ) and at the outer surface ( G , H ).

    Techniques Used:



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    denv1 ns1 v1  (Native Antigen Inc)
    92
    Native Antigen Inc denv1 ns1 v1
    A Unnatural bases in XenoAptamers. The Ds−diol-Px pair is utilized in PCR as a third base pair in the ExSELEX process. B Secondary structures of three <t>XenoAptamers</t> <t>targeting</t> <t>DENV1-NS1-v1</t> (AptD1), DENV1-NS1-v1 and -v2 (AptD1c), and DENV2-NS1 (AptD2). C Binding analysis of anti-DENV1-NS1-XenoAptamers with the NS1 variants (DENV1-NS1-v1 and v2) by an electrophoretic mobility shift assay (EMSA) in the presence of 3 M urea at 30°C. The experiment was performed once. D EMSA-based binding analysis of AptD2 derivatives containing substituted Pa'35 variant bases. The experiment was performed in duplicate. E K D values of AptD2 and its derivatives, AptD2-Pa′ and AptD2-Pa′ (diol), determined by SPR.
    Denv1 Ns1 V1, supplied by Native Antigen Inc, 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/denv1 ns1 v1/product/Native Antigen Inc
    Average 92 stars, based on 1 article reviews
    denv1 ns1 v1 - by Bioz Stars, 2026-02
    92/100 stars
    		  Buy from Supplier
    denv1ns1 v1  (Native Antigen Inc)
    92
    Native Antigen Inc denv1ns1 v1
    A Unnatural bases in XenoAptamers. The Ds−diol-Px pair is utilized in PCR as a third base pair in the ExSELEX process. B Secondary structures of three <t>XenoAptamers</t> <t>targeting</t> <t>DENV1-NS1-v1</t> (AptD1), DENV1-NS1-v1 and -v2 (AptD1c), and DENV2-NS1 (AptD2). C Binding analysis of anti-DENV1-NS1-XenoAptamers with the NS1 variants (DENV1-NS1-v1 and v2) by an electrophoretic mobility shift assay (EMSA) in the presence of 3 M urea at 30°C. The experiment was performed once. D EMSA-based binding analysis of AptD2 derivatives containing substituted Pa'35 variant bases. The experiment was performed in duplicate. E K D values of AptD2 and its derivatives, AptD2-Pa′ and AptD2-Pa′ (diol), determined by SPR.
    Denv1ns1 V1, supplied by Native Antigen Inc, 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/denv1ns1 v1/product/Native Antigen Inc
    Average 92 stars, based on 1 article reviews
    denv1ns1 v1 - by Bioz Stars, 2026-02
    92/100 stars
    		  Buy from Supplier

    Image Search Results


    A Unnatural bases in XenoAptamers. The Ds−diol-Px pair is utilized in PCR as a third base pair in the ExSELEX process. B Secondary structures of three XenoAptamers targeting DENV1-NS1-v1 (AptD1), DENV1-NS1-v1 and -v2 (AptD1c), and DENV2-NS1 (AptD2). C Binding analysis of anti-DENV1-NS1-XenoAptamers with the NS1 variants (DENV1-NS1-v1 and v2) by an electrophoretic mobility shift assay (EMSA) in the presence of 3 M urea at 30°C. The experiment was performed once. D EMSA-based binding analysis of AptD2 derivatives containing substituted Pa'35 variant bases. The experiment was performed in duplicate. E K D values of AptD2 and its derivatives, AptD2-Pa′ and AptD2-Pa′ (diol), determined by SPR.

    Journal: Nature Communications

    Article Title: Expanded genetic alphabet increases structural and chemical diversity of six-letter DNA for high-affinity protein-targeting aptamers

    doi: 10.1038/s41467-025-67486-x

    Figure Lengend Snippet: A Unnatural bases in XenoAptamers. The Ds−diol-Px pair is utilized in PCR as a third base pair in the ExSELEX process. B Secondary structures of three XenoAptamers targeting DENV1-NS1-v1 (AptD1), DENV1-NS1-v1 and -v2 (AptD1c), and DENV2-NS1 (AptD2). C Binding analysis of anti-DENV1-NS1-XenoAptamers with the NS1 variants (DENV1-NS1-v1 and v2) by an electrophoretic mobility shift assay (EMSA) in the presence of 3 M urea at 30°C. The experiment was performed once. D EMSA-based binding analysis of AptD2 derivatives containing substituted Pa'35 variant bases. The experiment was performed in duplicate. E K D values of AptD2 and its derivatives, AptD2-Pa′ and AptD2-Pa′ (diol), determined by SPR.

    Article Snippet: Recombinant DENV-NS1 proteins with a C-terminal poly-histidine-tag were obtained from the Native Antigen Company (DENV2-NS1 and DENV1-NS1-v1) or produced in-house using a conventional CHO cell expression system (DENV1-NS1-v2) as described previously .

    Techniques: Binding Assay, Electrophoretic Mobility Shift Assay, Variant Assay

    A–C Cryo-EM density maps of AptD1 with DENV1-NS1-v1 (hexamer) ( A ), AptD1c with DENV1-NS1-v2 (tetramer) ( B ), and AptD2 with DENV2-NS1 (dimer) ( C ). D–F Cryo-EM structures of XenoAptamers with their respective NS1 proteins. In the figures, only one XenoAptamer and one dimer of NS1 are shown. G – I The electrostatic surface potential models of NS1 show the XenoAptamers’ recognition of the positively charged surfaces of NS1 proteins ( G–I ). J–L Cryo-EM structures of XenoAptamers, in which the unnatural bases Ds and Pa′ are shown in yellow and black, respectively.

    Journal: Nature Communications

    Article Title: Expanded genetic alphabet increases structural and chemical diversity of six-letter DNA for high-affinity protein-targeting aptamers

    doi: 10.1038/s41467-025-67486-x

    Figure Lengend Snippet: A–C Cryo-EM density maps of AptD1 with DENV1-NS1-v1 (hexamer) ( A ), AptD1c with DENV1-NS1-v2 (tetramer) ( B ), and AptD2 with DENV2-NS1 (dimer) ( C ). D–F Cryo-EM structures of XenoAptamers with their respective NS1 proteins. In the figures, only one XenoAptamer and one dimer of NS1 are shown. G – I The electrostatic surface potential models of NS1 show the XenoAptamers’ recognition of the positively charged surfaces of NS1 proteins ( G–I ). J–L Cryo-EM structures of XenoAptamers, in which the unnatural bases Ds and Pa′ are shown in yellow and black, respectively.

    Article Snippet: Recombinant DENV-NS1 proteins with a C-terminal poly-histidine-tag were obtained from the Native Antigen Company (DENV2-NS1 and DENV1-NS1-v1) or produced in-house using a conventional CHO cell expression system (DENV1-NS1-v2) as described previously .

    Techniques: Cryo-EM Sample Prep

    A , B The overall structure of DENV1-NS1-v1 is complexed with AptD1 (green). In the XenoAptamer structures, the unnatural Ds bases are shown in yellow. One protomer of NS1 protein is colored dark blue (β-roll domain), orange (connector subdomain), yellow (wing domain), and pink (β-ladder domain), while the other is shown in light colors. The residues interacting with AptD1 are highlighted in red. C–E DENV1-NS1-v1 recognition of AptD1 in the positively-charged cleft ( C , D ) and at the outer surface ( E ).

    Journal: Nature Communications

    Article Title: Expanded genetic alphabet increases structural and chemical diversity of six-letter DNA for high-affinity protein-targeting aptamers

    doi: 10.1038/s41467-025-67486-x

    Figure Lengend Snippet: A , B The overall structure of DENV1-NS1-v1 is complexed with AptD1 (green). In the XenoAptamer structures, the unnatural Ds bases are shown in yellow. One protomer of NS1 protein is colored dark blue (β-roll domain), orange (connector subdomain), yellow (wing domain), and pink (β-ladder domain), while the other is shown in light colors. The residues interacting with AptD1 are highlighted in red. C–E DENV1-NS1-v1 recognition of AptD1 in the positively-charged cleft ( C , D ) and at the outer surface ( E ).

    Article Snippet: Recombinant DENV-NS1 proteins with a C-terminal poly-histidine-tag were obtained from the Native Antigen Company (DENV2-NS1 and DENV1-NS1-v1) or produced in-house using a conventional CHO cell expression system (DENV1-NS1-v2) as described previously .

    Techniques:

    A , B Overall structure ( A ) and cleft-focused structure ( B ) of DENV1-NS1-v2 with AptD1c (green). In the XenoAptamer structures, the unnatural bases Ds are shown in yellow. One protomer of NS1 protein is colored dark blue (β-roll domain), orange (connector subdomain), yellow (wing domain), and pink (β-ladder domain), while the other is shown in light colors. The residues interacting with AptD1 are highlighted in red. ( C–H ) DENV1-NS1-v1 recognition of AptD1c in the positively-charged cleft ( C–F ) and at the outer surface ( G , H ).

    Journal: Nature Communications

    Article Title: Expanded genetic alphabet increases structural and chemical diversity of six-letter DNA for high-affinity protein-targeting aptamers

    doi: 10.1038/s41467-025-67486-x

    Figure Lengend Snippet: A , B Overall structure ( A ) and cleft-focused structure ( B ) of DENV1-NS1-v2 with AptD1c (green). In the XenoAptamer structures, the unnatural bases Ds are shown in yellow. One protomer of NS1 protein is colored dark blue (β-roll domain), orange (connector subdomain), yellow (wing domain), and pink (β-ladder domain), while the other is shown in light colors. The residues interacting with AptD1 are highlighted in red. ( C–H ) DENV1-NS1-v1 recognition of AptD1c in the positively-charged cleft ( C–F ) and at the outer surface ( G , H ).

    Article Snippet: Recombinant DENV-NS1 proteins with a C-terminal poly-histidine-tag were obtained from the Native Antigen Company (DENV2-NS1 and DENV1-NS1-v1) or produced in-house using a conventional CHO cell expression system (DENV1-NS1-v2) as described previously .

    Techniques: