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sa biosensor  (Sino Biological)


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    Sino Biological sa biosensor
    Sa Biosensor, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sa+biosensor/us12600794-599-17-8?v=Sino+Biological
    Average 94 stars, based on 7 article reviews
    sa biosensor - by Bioz Stars, 2026-07
    94/100 stars

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    A) Nucleotide composition across the 40-nt random region of the starting SELEX library (round 0) and after selection round 6. Grey shades indicate nucleotide identities as shown in the legend. B) NGS profiling showing sequence enrichment (frequency, %) of the top 10 candidates across SELEX rounds 2–6. C) Screening of selected sequences for binding to H1 hemagglutinin using BLI. Average BLI response after 98 s of association for sequences H1-1 and H1-3 containing histidine-modified uridines, immobilized on <t>streptavidin</t> BLI sensors and exposed to H1 hemagglutinin in solution at 150 nM (n = 3). D) Binding kinetics of aptamer H1-His-1 to H1 hemagglutinin measured by BLI. The biotinylated aptamer was immobilized on streptavidin-coated BLI sensors and exposed to a two-fold dilution of H1 hemagglutinin in solution starting at 150 nM. Association phase: 0–400 s; dissociation phase: 400–1600 s. Global fitting of association and dissociation curves (red lines) was performed using Evilfit accounting for surface effects. Residuals are shown below. E) Assessment of H1-1 aptamer specificity. Average BLI response after 98 s of association for sequence H1-1 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin and H5 hemagglutinin or a 300 nM nanobody control in solution (n = 3). F) Evaluation of the impact of uridine modifications on H1-1 aptamer binding. Average BLI response after 98 s of association for H1-1 containing histidine-modified uridines or substituted with leucine- or 2F’- modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin in solution (n = 3).
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    A) Nucleotide composition across the 40-nt random region of the starting SELEX library (round 0) and after selection round 6. Grey shades indicate nucleotide identities as shown in the legend. B) NGS profiling showing sequence enrichment (frequency, %) of the top 10 candidates across SELEX rounds 2–6. C) Screening of selected sequences for binding to H1 hemagglutinin using BLI. Average BLI response after 98 s of association for sequences H1-1 and H1-3 containing histidine-modified uridines, immobilized on <t>streptavidin</t> BLI sensors and exposed to H1 hemagglutinin in solution at 150 nM (n = 3). D) Binding kinetics of aptamer H1-His-1 to H1 hemagglutinin measured by BLI. The biotinylated aptamer was immobilized on streptavidin-coated BLI sensors and exposed to a two-fold dilution of H1 hemagglutinin in solution starting at 150 nM. Association phase: 0–400 s; dissociation phase: 400–1600 s. Global fitting of association and dissociation curves (red lines) was performed using Evilfit accounting for surface effects. Residuals are shown below. E) Assessment of H1-1 aptamer specificity. Average BLI response after 98 s of association for sequence H1-1 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin and H5 hemagglutinin or a 300 nM nanobody control in solution (n = 3). F) Evaluation of the impact of uridine modifications on H1-1 aptamer binding. Average BLI response after 98 s of association for H1-1 containing histidine-modified uridines or substituted with leucine- or 2F’- modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin in solution (n = 3).
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    A) Nucleotide composition across the 40-nt random region of the starting SELEX library (round 0) and after selection round 6. Grey shades indicate nucleotide identities as shown in the legend. B) NGS profiling showing sequence enrichment (frequency, %) of the top 10 candidates across SELEX rounds 2–6. C) Screening of selected sequences for binding to H1 hemagglutinin using BLI. Average BLI response after 98 s of association for sequences H1-1 and H1-3 containing histidine-modified uridines, immobilized on <t>streptavidin</t> BLI sensors and exposed to H1 hemagglutinin in solution at 150 nM (n = 3). D) Binding kinetics of aptamer H1-His-1 to H1 hemagglutinin measured by BLI. The biotinylated aptamer was immobilized on streptavidin-coated BLI sensors and exposed to a two-fold dilution of H1 hemagglutinin in solution starting at 150 nM. Association phase: 0–400 s; dissociation phase: 400–1600 s. Global fitting of association and dissociation curves (red lines) was performed using Evilfit accounting for surface effects. Residuals are shown below. E) Assessment of H1-1 aptamer specificity. Average BLI response after 98 s of association for sequence H1-1 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin and H5 hemagglutinin or a 300 nM nanobody control in solution (n = 3). F) Evaluation of the impact of uridine modifications on H1-1 aptamer binding. Average BLI response after 98 s of association for H1-1 containing histidine-modified uridines or substituted with leucine- or 2F’- modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin in solution (n = 3).
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    A) Nucleotide composition across the 40-nt random region of the starting SELEX library (round 0) and after selection round 6. Grey shades indicate nucleotide identities as shown in the legend. B) NGS profiling showing sequence enrichment (frequency, %) of the top 10 candidates across SELEX rounds 2–6. C) Screening of selected sequences for binding to H1 hemagglutinin using BLI. Average BLI response after 98 s of association for sequences H1-1 and H1-3 containing histidine-modified uridines, immobilized on <t>streptavidin</t> BLI sensors and exposed to H1 hemagglutinin in solution at 150 nM (n = 3). D) Binding kinetics of aptamer H1-His-1 to H1 hemagglutinin measured by BLI. The biotinylated aptamer was immobilized on streptavidin-coated BLI sensors and exposed to a two-fold dilution of H1 hemagglutinin in solution starting at 150 nM. Association phase: 0–400 s; dissociation phase: 400–1600 s. Global fitting of association and dissociation curves (red lines) was performed using Evilfit accounting for surface effects. Residuals are shown below. E) Assessment of H1-1 aptamer specificity. Average BLI response after 98 s of association for sequence H1-1 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin and H5 hemagglutinin or a 300 nM nanobody control in solution (n = 3). F) Evaluation of the impact of uridine modifications on H1-1 aptamer binding. Average BLI response after 98 s of association for H1-1 containing histidine-modified uridines or substituted with leucine- or 2F’- modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin in solution (n = 3).
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    A) Nucleotide composition across the 40-nt random region of the starting SELEX library (round 0) and after selection round 6. Grey shades indicate nucleotide identities as shown in the legend. B) NGS profiling showing sequence enrichment (frequency, %) of the top 10 candidates across SELEX rounds 2–6. C) Screening of selected sequences for binding to H1 hemagglutinin using BLI. Average BLI response after 98 s of association for sequences H1-1 and H1-3 containing histidine-modified uridines, immobilized on <t>streptavidin</t> BLI sensors and exposed to H1 hemagglutinin in solution at 150 nM (n = 3). D) Binding kinetics of aptamer H1-His-1 to H1 hemagglutinin measured by BLI. The biotinylated aptamer was immobilized on streptavidin-coated BLI sensors and exposed to a two-fold dilution of H1 hemagglutinin in solution starting at 150 nM. Association phase: 0–400 s; dissociation phase: 400–1600 s. Global fitting of association and dissociation curves (red lines) was performed using Evilfit accounting for surface effects. Residuals are shown below. E) Assessment of H1-1 aptamer specificity. Average BLI response after 98 s of association for sequence H1-1 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin and H5 hemagglutinin or a 300 nM nanobody control in solution (n = 3). F) Evaluation of the impact of uridine modifications on H1-1 aptamer binding. Average BLI response after 98 s of association for H1-1 containing histidine-modified uridines or substituted with leucine- or 2F’- modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin in solution (n = 3).
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    A) Nucleotide composition across the 40-nt random region of the starting SELEX library (round 0) and after selection round 6. Grey shades indicate nucleotide identities as shown in the legend. B) NGS profiling showing sequence enrichment (frequency, %) of the top 10 candidates across SELEX rounds 2–6. C) Screening of selected sequences for binding to H1 hemagglutinin using BLI. Average BLI response after 98 s of association for sequences H1-1 and H1-3 containing histidine-modified uridines, immobilized on <t>streptavidin</t> BLI sensors and exposed to H1 hemagglutinin in solution at 150 nM (n = 3). D) Binding kinetics of aptamer H1-His-1 to H1 hemagglutinin measured by BLI. The biotinylated aptamer was immobilized on streptavidin-coated BLI sensors and exposed to a two-fold dilution of H1 hemagglutinin in solution starting at 150 nM. Association phase: 0–400 s; dissociation phase: 400–1600 s. Global fitting of association and dissociation curves (red lines) was performed using Evilfit accounting for surface effects. Residuals are shown below. E) Assessment of H1-1 aptamer specificity. Average BLI response after 98 s of association for sequence H1-1 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin and H5 hemagglutinin or a 300 nM nanobody control in solution (n = 3). F) Evaluation of the impact of uridine modifications on H1-1 aptamer binding. Average BLI response after 98 s of association for H1-1 containing histidine-modified uridines or substituted with leucine- or 2F’- modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin in solution (n = 3).
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    A) Nucleotide composition across the 40-nt random region of the starting SELEX library (round 0) and after selection round 6. Grey shades indicate nucleotide identities as shown in the legend. B) NGS profiling showing sequence enrichment (frequency, %) of the top 10 candidates across SELEX rounds 2–6. C) Screening of selected sequences for binding to H1 hemagglutinin using BLI. Average BLI response after 98 s of association for sequences H1-1 and H1-3 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to H1 hemagglutinin in solution at 150 nM (n = 3). D) Binding kinetics of aptamer H1-His-1 to H1 hemagglutinin measured by BLI. The biotinylated aptamer was immobilized on streptavidin-coated BLI sensors and exposed to a two-fold dilution of H1 hemagglutinin in solution starting at 150 nM. Association phase: 0–400 s; dissociation phase: 400–1600 s. Global fitting of association and dissociation curves (red lines) was performed using Evilfit accounting for surface effects. Residuals are shown below. E) Assessment of H1-1 aptamer specificity. Average BLI response after 98 s of association for sequence H1-1 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin and H5 hemagglutinin or a 300 nM nanobody control in solution (n = 3). F) Evaluation of the impact of uridine modifications on H1-1 aptamer binding. Average BLI response after 98 s of association for H1-1 containing histidine-modified uridines or substituted with leucine- or 2F’- modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin in solution (n = 3).

    Journal: bioRxiv

    Article Title: Expanding the chemical diversity of RNA by transcriptional incorporation of amino acid- and glycosyl-modified nucleotides

    doi: 10.64898/2026.04.22.720138

    Figure Lengend Snippet: A) Nucleotide composition across the 40-nt random region of the starting SELEX library (round 0) and after selection round 6. Grey shades indicate nucleotide identities as shown in the legend. B) NGS profiling showing sequence enrichment (frequency, %) of the top 10 candidates across SELEX rounds 2–6. C) Screening of selected sequences for binding to H1 hemagglutinin using BLI. Average BLI response after 98 s of association for sequences H1-1 and H1-3 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to H1 hemagglutinin in solution at 150 nM (n = 3). D) Binding kinetics of aptamer H1-His-1 to H1 hemagglutinin measured by BLI. The biotinylated aptamer was immobilized on streptavidin-coated BLI sensors and exposed to a two-fold dilution of H1 hemagglutinin in solution starting at 150 nM. Association phase: 0–400 s; dissociation phase: 400–1600 s. Global fitting of association and dissociation curves (red lines) was performed using Evilfit accounting for surface effects. Residuals are shown below. E) Assessment of H1-1 aptamer specificity. Average BLI response after 98 s of association for sequence H1-1 containing histidine-modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin and H5 hemagglutinin or a 300 nM nanobody control in solution (n = 3). F) Evaluation of the impact of uridine modifications on H1-1 aptamer binding. Average BLI response after 98 s of association for H1-1 containing histidine-modified uridines or substituted with leucine- or 2F’- modified uridines, immobilized on streptavidin BLI sensors and exposed to 150 nM H1 hemagglutinin in solution (n = 3).

    Article Snippet: Refolded, biotinylated RNA aptamer were immobilized on Octet® Streptavidin (SA) Biosensors (Sartorius).

    Techniques: Selection, Sequencing, Binding Assay, Modification, Control