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azidoethoxy ethoxy ethyl 2 3 4 6 tetra o acetyld galactopyranoside 2 3 4 6 tetra o acetyl d gal eg3n3  (Tokyo Chemical Industry)

 
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    Tokyo Chemical Industry azidoethoxy ethoxy ethyl 2 3 4 6 tetra o acetyld galactopyranoside 2 3 4 6 tetra o acetyl d gal eg3n3
    Azidoethoxy Ethoxy Ethyl 2 3 4 6 Tetra O Acetyld Galactopyranoside 2 3 4 6 Tetra O Acetyl D Gal Eg3n3, supplied by Tokyo Chemical Industry, 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/azidoethoxy ethoxy ethyl 2 3 4 6 tetra o acetyld galactopyranoside 2 3 4 6 tetra o acetyl d gal eg3n3/product/Tokyo Chemical Industry
    Average 86 stars, based on 1 article reviews
    azidoethoxy ethoxy ethyl 2 3 4 6 tetra o acetyld galactopyranoside 2 3 4 6 tetra o acetyl d gal eg3n3 - by Bioz Stars, 2026-06
    86/100 stars

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    (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch <t>biosensor</t> <t>with</t> <t>5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside</t> (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.
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    (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch <t>biosensor</t> <t>with</t> <t>5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside</t> (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.
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    (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch <t>biosensor</t> <t>with</t> <t>5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside</t> (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.
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    (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch <t>biosensor</t> <t>with</t> <t>5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside</t> (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.
    Azidoethoxy Ethoxy Ethyl 2 3 4 6 Tetra O Acetyld Galactopyranoside 2 3 4 6 Tetra O Acetyl D Gal Eg3n3, supplied by Tokyo Chemical Industry, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch <t>biosensor</t> <t>with</t> <t>5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside</t> (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.
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    Schematic representation of ligands recognized by all three CRD domains in glycan-array experiments. The ligands are groupped according to a blood group antigen from which they are derived. The symbolic representation of saccharides: yellow circle <t>=</t> <t>D-galactose;</t> yellow square = N -acetyl-D-galactosamine; blue circle = D-glucose; blue square = N -acetyl-D-glucosamine; red rectangle = L-fucose; purple diamond = N -acetylneuraminic acid.
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    Schematic representation of ligands recognized by all three CRD domains in glycan-array experiments. The ligands are groupped according to a blood group antigen from which they are derived. The symbolic representation of saccharides: yellow circle <t>=</t> <t>D-galactose;</t> yellow square = N -acetyl-D-galactosamine; blue circle = D-glucose; blue square = N -acetyl-D-glucosamine; red rectangle = L-fucose; purple diamond = N -acetylneuraminic acid.
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    Thermo Fisher galactose gal
    Schematic representation of ligands recognized by all three CRD domains in glycan-array experiments. The ligands are groupped according to a blood group antigen from which they are derived. The symbolic representation of saccharides: yellow circle <t>=</t> <t>D-galactose;</t> yellow square = N -acetyl-D-galactosamine; blue circle = D-glucose; blue square = N -acetyl-D-glucosamine; red rectangle = L-fucose; purple diamond = N -acetylneuraminic acid.
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    Image Search Results


    (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch biosensor with 5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.

    Journal: bioRxiv

    Article Title: Selective Hydrolytic Defluorination of Branched Perfluorooctanoic Acid Isomers by a Haloacid Dehalogenase

    doi: 10.64898/2026.04.19.719434

    Figure Lengend Snippet: (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch biosensor with 5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.

    Article Snippet: 5-Bromo-4-chloro-3-indolyl-β-D-galactopyranoside (X-gal) solution (20 mg/mL; Thermo Fisher Scientific, RO941) and 10 mM Tris buffer (pH 8.0, prepared from a 1 M stock; Thermo Fisher Scientific, AM9855G) were used for enzyme assays.

    Techniques: Binding Assay, Concentration Assay, Incubation, Purification

    Schematic representation of ligands recognized by all three CRD domains in glycan-array experiments. The ligands are groupped according to a blood group antigen from which they are derived. The symbolic representation of saccharides: yellow circle = D-galactose; yellow square = N -acetyl-D-galactosamine; blue circle = D-glucose; blue square = N -acetyl-D-glucosamine; red rectangle = L-fucose; purple diamond = N -acetylneuraminic acid.

    Journal: bioRxiv

    Article Title: A newly identified three-domain C-type lectin associated with blood feeding in the tick Ixodes ricinus

    doi: 10.64898/2026.01.07.698205

    Figure Lengend Snippet: Schematic representation of ligands recognized by all three CRD domains in glycan-array experiments. The ligands are groupped according to a blood group antigen from which they are derived. The symbolic representation of saccharides: yellow circle = D-galactose; yellow square = N -acetyl-D-galactosamine; blue circle = D-glucose; blue square = N -acetyl-D-glucosamine; red rectangle = L-fucose; purple diamond = N -acetylneuraminic acid.

    Article Snippet: For the hemagglutination inhibition assay, 25 μL of the recombinant His-CRD1 or His-CRD2 was mixed with 25 μL of serially diluted saccharides (α-L-fucose (L-Fuc), α-D-galactose (D-Gal), N -acetyl-α-D-galactosamine (GalNAc) (Carbosynth Limited), α-L-galactose (L-Gal), α-D-glucose (D-Glc), α-D-mannose (D-Man) (Duchefa Biochemie) dissolved in buffer A. Mixtures were incubated for 15 min at room temperature.

    Techniques: Glycoproteomics, Derivative Assay