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Gold Biotechnology Inc 5 bromo 4 chloro 3 indolyl β d galactoside x gal
5 Bromo 4 Chloro 3 Indolyl β D Galactoside X Gal, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Thermo Fisher 5 bromo 4 chloro 3 indolyl β d galactopyranoside x gal solution
(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.
5 Bromo 4 Chloro 3 Indolyl β D Galactopyranoside X Gal Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Amresco 5 bromo 4 chloro 3 indolyl β d galactopyranoside x gal
(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.
5 Bromo 4 Chloro 3 Indolyl β D Galactopyranoside X Gal, supplied by Amresco, 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/product/4+d+gal/pmc13128220-28-0-5?v=Amresco
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Fisher Scientific 5 bromo 4 chloro 3 indolyl beta d galacto pyranoside x gal
(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.
5 Bromo 4 Chloro 3 Indolyl Beta D Galacto Pyranoside X Gal, supplied by Fisher Scientific, 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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Tokyo Chemical Industry azidoethoxy ethoxy ethyl 2 3 4 6 tetra o acetyld galactopyranoside 2 3 4 6 tetra o acetyl d gal eg3n3
(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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Galectin Therapeutics gasdermin d mediated pore formation gal 1 gal 7gal 3 gal 8 gal 12gal 9 mhc ii tcr tim 3 cd45gal 4 cd4 cd8 cd4 cd8 cd4 cd8 cd8 cd4 naive cd4
(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.
Gasdermin D Mediated Pore Formation Gal 1 Gal 7gal 3 Gal 8 Gal 12gal 9 Mhc Ii Tcr Tim 3 Cd45gal 4 Cd4 Cd8 Cd4 Cd8 Cd4 Cd8 Cd8 Cd4 Naive Cd4, supplied by Galectin Therapeutics, 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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gasdermin d mediated pore formation gal 1 gal 7gal 3 gal 8 gal 12gal 9 mhc ii tcr tim 3 cd45gal 4 cd4 cd8 cd4 cd8 cd4 cd8 cd8 cd4 naive cd4 - by Bioz Stars, 2026-07
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Thermo Fisher x gal
(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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x gal - by Bioz Stars, 2026-07
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Thermo Fisher 5 bromo 4 chloro 3 indolyl β d galactopyranoside x gal
(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.
5 Bromo 4 Chloro 3 Indolyl β D Galactopyranoside X Gal, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, 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 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