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bromo  (MedChemExpress)


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    Structured Review

    MedChemExpress bromo
    Bromo, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 95/100, based on 94 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bromo/product/MedChemExpress
    Average 95 stars, based on 94 article reviews
    bromo - by Bioz Stars, 2026-05
    95/100 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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    MedChemExpress cells expressing nphp3n akar2 cr
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    MedChemExpress 8 br camp
    (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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    MedChemExpress brcamp
    (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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    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