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human recombinant slc5a1 protein  (Novus Biologicals)


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    Novus Biologicals human recombinant slc5a1 protein
    Fig. 3. Ginsenoside Rd binds to <t>SLC5A1</t> with a high affinity. A. Predicted docking protein of ginsenoside Rd, by using TargetNet. B. Molecular docking of between ginsenoside Rd and SLC5A1. The estimated thee binding positions and related residuals within SLC5A1 were provided in the bottom panel. C. Left: schematic of proposed interactions between SLC5A1 and glucose by one previous study [25]. X, XI, XII and XIII are four translocation domains of SLC5A1. The magenta ellipse indicates the aromatic stacking with the hydrophobic surface of the pyranose. Right: Three-dimensional model of the glucose binding domains of SLC5A1 [25]. The same helical domains in the left and right panels are labeled with the same color. Residues on the external surface are highlighted with yellow boxes in the right panel. D. SPR analysis of ginsenoside Rd binding to human recombinant SLC5A1 protein. E-F. Representative images (E) and quantitation (F) of CETSA of SLC5A1 with 30 mM ginsenoside Rd. n ¼ 3 independent experiments. **p < 0.01, ***p < 0.001.
    Human Recombinant Slc5a1 Protein, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Ginsenoside Rd protects cerebral endothelial cells from oxygen-glucose deprivation/reoxygenation induced pyroptosis via inhibiting SLC5A1 mediated sodium influx."

    Article Title: Ginsenoside Rd protects cerebral endothelial cells from oxygen-glucose deprivation/reoxygenation induced pyroptosis via inhibiting SLC5A1 mediated sodium influx.

    Journal: Journal of ginseng research

    doi: 10.1016/j.jgr.2022.05.006

    Fig. 3. Ginsenoside Rd binds to SLC5A1 with a high affinity. A. Predicted docking protein of ginsenoside Rd, by using TargetNet. B. Molecular docking of between ginsenoside Rd and SLC5A1. The estimated thee binding positions and related residuals within SLC5A1 were provided in the bottom panel. C. Left: schematic of proposed interactions between SLC5A1 and glucose by one previous study [25]. X, XI, XII and XIII are four translocation domains of SLC5A1. The magenta ellipse indicates the aromatic stacking with the hydrophobic surface of the pyranose. Right: Three-dimensional model of the glucose binding domains of SLC5A1 [25]. The same helical domains in the left and right panels are labeled with the same color. Residues on the external surface are highlighted with yellow boxes in the right panel. D. SPR analysis of ginsenoside Rd binding to human recombinant SLC5A1 protein. E-F. Representative images (E) and quantitation (F) of CETSA of SLC5A1 with 30 mM ginsenoside Rd. n ¼ 3 independent experiments. **p < 0.01, ***p < 0.001.
    Figure Legend Snippet: Fig. 3. Ginsenoside Rd binds to SLC5A1 with a high affinity. A. Predicted docking protein of ginsenoside Rd, by using TargetNet. B. Molecular docking of between ginsenoside Rd and SLC5A1. The estimated thee binding positions and related residuals within SLC5A1 were provided in the bottom panel. C. Left: schematic of proposed interactions between SLC5A1 and glucose by one previous study [25]. X, XI, XII and XIII are four translocation domains of SLC5A1. The magenta ellipse indicates the aromatic stacking with the hydrophobic surface of the pyranose. Right: Three-dimensional model of the glucose binding domains of SLC5A1 [25]. The same helical domains in the left and right panels are labeled with the same color. Residues on the external surface are highlighted with yellow boxes in the right panel. D. SPR analysis of ginsenoside Rd binding to human recombinant SLC5A1 protein. E-F. Representative images (E) and quantitation (F) of CETSA of SLC5A1 with 30 mM ginsenoside Rd. n ¼ 3 independent experiments. **p < 0.01, ***p < 0.001.

    Techniques Used: Binding Assay, Translocation Assay, Labeling, Recombinant, Quantitation Assay

    Fig. 4. Ginsenoside Rd reduces OGD/R-induced sodium influx and potassium efflux in HBMECs. A. SLC5A1 mRNA expression in HBMECs after OGD/R stimulation, with or without treatment of ginsenoside Rd. B. SLC5A1 and SLC5A2 protein expression in HBMECs after OGD/R stimulation, with or without treatment of ginsenoside Rd. C-D. Relative intracellular Naþ (C) and Kþ (D) were detected in HBMECs after OGD(2 h)/R (1 h) stimulation, with or without the presence of ginsenoside Rd. E-F. Relative TEER values (E) and relative concentration of FITC-dextran (F) were calculated to assess the protective effect of phlorizin (25 and 50 mM) against OGD/R-induced damage of barrier function in different OGD/R time. G-J. Representative immunofluorescent images (G) and western blotting assays (HeJ) showing the expression of ZO-1 (green) and claudin-5 (red) in HBMECs after OGD(2 h)/R (12 h), with or without phlorizin treatment (50 mM). Scale bar ¼ 20 mm. Results were reported as mean ± SD (n ¼ 3). ***p < 0.001. n.s.: not significant.
    Figure Legend Snippet: Fig. 4. Ginsenoside Rd reduces OGD/R-induced sodium influx and potassium efflux in HBMECs. A. SLC5A1 mRNA expression in HBMECs after OGD/R stimulation, with or without treatment of ginsenoside Rd. B. SLC5A1 and SLC5A2 protein expression in HBMECs after OGD/R stimulation, with or without treatment of ginsenoside Rd. C-D. Relative intracellular Naþ (C) and Kþ (D) were detected in HBMECs after OGD(2 h)/R (1 h) stimulation, with or without the presence of ginsenoside Rd. E-F. Relative TEER values (E) and relative concentration of FITC-dextran (F) were calculated to assess the protective effect of phlorizin (25 and 50 mM) against OGD/R-induced damage of barrier function in different OGD/R time. G-J. Representative immunofluorescent images (G) and western blotting assays (HeJ) showing the expression of ZO-1 (green) and claudin-5 (red) in HBMECs after OGD(2 h)/R (12 h), with or without phlorizin treatment (50 mM). Scale bar ¼ 20 mm. Results were reported as mean ± SD (n ¼ 3). ***p < 0.001. n.s.: not significant.

    Techniques Used: Expressing, Concentration Assay, Western Blot

    Fig. 5. Inhibiting SLC5A1 suppresses OGD/R-activated NLRP3 inflammasome and pyroptosis in HBMECs. A-E. Representative blots (A) and quantitative analysis (BeE) of NLRP3, cleaved caspase-1, IL-1b and GSDMD-NT expression in HBMECs after OGD stimulation, with or without phlorizin treatment. F-G. Pyroptotic cells with the same treatment in panel A were assessed by caspase-1 and PI staining. Representative flow cytometric images (F) and quantitative data (G) of caspase-1þ/PI þ cell ratio were provided. Results were reported as mean ± SD (n ¼ 3). ***p < 0.001.
    Figure Legend Snippet: Fig. 5. Inhibiting SLC5A1 suppresses OGD/R-activated NLRP3 inflammasome and pyroptosis in HBMECs. A-E. Representative blots (A) and quantitative analysis (BeE) of NLRP3, cleaved caspase-1, IL-1b and GSDMD-NT expression in HBMECs after OGD stimulation, with or without phlorizin treatment. F-G. Pyroptotic cells with the same treatment in panel A were assessed by caspase-1 and PI staining. Representative flow cytometric images (F) and quantitative data (G) of caspase-1þ/PI þ cell ratio were provided. Results were reported as mean ± SD (n ¼ 3). ***p < 0.001.

    Techniques Used: Expressing, Staining



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    Fig. 3. Ginsenoside Rd binds to <t>SLC5A1</t> with a high affinity. A. Predicted docking protein of ginsenoside Rd, by using TargetNet. B. Molecular docking of between ginsenoside Rd and SLC5A1. The estimated thee binding positions and related residuals within SLC5A1 were provided in the bottom panel. C. Left: schematic of proposed interactions between SLC5A1 and glucose by one previous study [25]. X, XI, XII and XIII are four translocation domains of SLC5A1. The magenta ellipse indicates the aromatic stacking with the hydrophobic surface of the pyranose. Right: Three-dimensional model of the glucose binding domains of SLC5A1 [25]. The same helical domains in the left and right panels are labeled with the same color. Residues on the external surface are highlighted with yellow boxes in the right panel. D. SPR analysis of ginsenoside Rd binding to human recombinant SLC5A1 protein. E-F. Representative images (E) and quantitation (F) of CETSA of SLC5A1 with 30 mM ginsenoside Rd. n ¼ 3 independent experiments. **p < 0.01, ***p < 0.001.
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    Fig. 3. Ginsenoside Rd binds to <t>SLC5A1</t> with a high affinity. A. Predicted docking protein of ginsenoside Rd, by using TargetNet. B. Molecular docking of between ginsenoside Rd and SLC5A1. The estimated thee binding positions and related residuals within SLC5A1 were provided in the bottom panel. C. Left: schematic of proposed interactions between SLC5A1 and glucose by one previous study [25]. X, XI, XII and XIII are four translocation domains of SLC5A1. The magenta ellipse indicates the aromatic stacking with the hydrophobic surface of the pyranose. Right: Three-dimensional model of the glucose binding domains of SLC5A1 [25]. The same helical domains in the left and right panels are labeled with the same color. Residues on the external surface are highlighted with yellow boxes in the right panel. D. SPR analysis of ginsenoside Rd binding to human recombinant SLC5A1 protein. E-F. Representative images (E) and quantitation (F) of CETSA of SLC5A1 with 30 mM ginsenoside Rd. n ¼ 3 independent experiments. **p < 0.01, ***p < 0.001.
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    Image Search Results


    Fig. 3. Ginsenoside Rd binds to SLC5A1 with a high affinity. A. Predicted docking protein of ginsenoside Rd, by using TargetNet. B. Molecular docking of between ginsenoside Rd and SLC5A1. The estimated thee binding positions and related residuals within SLC5A1 were provided in the bottom panel. C. Left: schematic of proposed interactions between SLC5A1 and glucose by one previous study [25]. X, XI, XII and XIII are four translocation domains of SLC5A1. The magenta ellipse indicates the aromatic stacking with the hydrophobic surface of the pyranose. Right: Three-dimensional model of the glucose binding domains of SLC5A1 [25]. The same helical domains in the left and right panels are labeled with the same color. Residues on the external surface are highlighted with yellow boxes in the right panel. D. SPR analysis of ginsenoside Rd binding to human recombinant SLC5A1 protein. E-F. Representative images (E) and quantitation (F) of CETSA of SLC5A1 with 30 mM ginsenoside Rd. n ¼ 3 independent experiments. **p < 0.01, ***p < 0.001.

    Journal: Journal of ginseng research

    Article Title: Ginsenoside Rd protects cerebral endothelial cells from oxygen-glucose deprivation/reoxygenation induced pyroptosis via inhibiting SLC5A1 mediated sodium influx.

    doi: 10.1016/j.jgr.2022.05.006

    Figure Lengend Snippet: Fig. 3. Ginsenoside Rd binds to SLC5A1 with a high affinity. A. Predicted docking protein of ginsenoside Rd, by using TargetNet. B. Molecular docking of between ginsenoside Rd and SLC5A1. The estimated thee binding positions and related residuals within SLC5A1 were provided in the bottom panel. C. Left: schematic of proposed interactions between SLC5A1 and glucose by one previous study [25]. X, XI, XII and XIII are four translocation domains of SLC5A1. The magenta ellipse indicates the aromatic stacking with the hydrophobic surface of the pyranose. Right: Three-dimensional model of the glucose binding domains of SLC5A1 [25]. The same helical domains in the left and right panels are labeled with the same color. Residues on the external surface are highlighted with yellow boxes in the right panel. D. SPR analysis of ginsenoside Rd binding to human recombinant SLC5A1 protein. E-F. Representative images (E) and quantitation (F) of CETSA of SLC5A1 with 30 mM ginsenoside Rd. n ¼ 3 independent experiments. **p < 0.01, ***p < 0.001.

    Article Snippet: Human recombinant SLC5A1 protein (Novus Biologicals, Littleton, CO, USA) was captured on a CM5 chip via a standard amine coupling procedure.

    Techniques: Binding Assay, Translocation Assay, Labeling, Recombinant, Quantitation Assay

    Fig. 4. Ginsenoside Rd reduces OGD/R-induced sodium influx and potassium efflux in HBMECs. A. SLC5A1 mRNA expression in HBMECs after OGD/R stimulation, with or without treatment of ginsenoside Rd. B. SLC5A1 and SLC5A2 protein expression in HBMECs after OGD/R stimulation, with or without treatment of ginsenoside Rd. C-D. Relative intracellular Naþ (C) and Kþ (D) were detected in HBMECs after OGD(2 h)/R (1 h) stimulation, with or without the presence of ginsenoside Rd. E-F. Relative TEER values (E) and relative concentration of FITC-dextran (F) were calculated to assess the protective effect of phlorizin (25 and 50 mM) against OGD/R-induced damage of barrier function in different OGD/R time. G-J. Representative immunofluorescent images (G) and western blotting assays (HeJ) showing the expression of ZO-1 (green) and claudin-5 (red) in HBMECs after OGD(2 h)/R (12 h), with or without phlorizin treatment (50 mM). Scale bar ¼ 20 mm. Results were reported as mean ± SD (n ¼ 3). ***p < 0.001. n.s.: not significant.

    Journal: Journal of ginseng research

    Article Title: Ginsenoside Rd protects cerebral endothelial cells from oxygen-glucose deprivation/reoxygenation induced pyroptosis via inhibiting SLC5A1 mediated sodium influx.

    doi: 10.1016/j.jgr.2022.05.006

    Figure Lengend Snippet: Fig. 4. Ginsenoside Rd reduces OGD/R-induced sodium influx and potassium efflux in HBMECs. A. SLC5A1 mRNA expression in HBMECs after OGD/R stimulation, with or without treatment of ginsenoside Rd. B. SLC5A1 and SLC5A2 protein expression in HBMECs after OGD/R stimulation, with or without treatment of ginsenoside Rd. C-D. Relative intracellular Naþ (C) and Kþ (D) were detected in HBMECs after OGD(2 h)/R (1 h) stimulation, with or without the presence of ginsenoside Rd. E-F. Relative TEER values (E) and relative concentration of FITC-dextran (F) were calculated to assess the protective effect of phlorizin (25 and 50 mM) against OGD/R-induced damage of barrier function in different OGD/R time. G-J. Representative immunofluorescent images (G) and western blotting assays (HeJ) showing the expression of ZO-1 (green) and claudin-5 (red) in HBMECs after OGD(2 h)/R (12 h), with or without phlorizin treatment (50 mM). Scale bar ¼ 20 mm. Results were reported as mean ± SD (n ¼ 3). ***p < 0.001. n.s.: not significant.

    Article Snippet: Human recombinant SLC5A1 protein (Novus Biologicals, Littleton, CO, USA) was captured on a CM5 chip via a standard amine coupling procedure.

    Techniques: Expressing, Concentration Assay, Western Blot

    Fig. 5. Inhibiting SLC5A1 suppresses OGD/R-activated NLRP3 inflammasome and pyroptosis in HBMECs. A-E. Representative blots (A) and quantitative analysis (BeE) of NLRP3, cleaved caspase-1, IL-1b and GSDMD-NT expression in HBMECs after OGD stimulation, with or without phlorizin treatment. F-G. Pyroptotic cells with the same treatment in panel A were assessed by caspase-1 and PI staining. Representative flow cytometric images (F) and quantitative data (G) of caspase-1þ/PI þ cell ratio were provided. Results were reported as mean ± SD (n ¼ 3). ***p < 0.001.

    Journal: Journal of ginseng research

    Article Title: Ginsenoside Rd protects cerebral endothelial cells from oxygen-glucose deprivation/reoxygenation induced pyroptosis via inhibiting SLC5A1 mediated sodium influx.

    doi: 10.1016/j.jgr.2022.05.006

    Figure Lengend Snippet: Fig. 5. Inhibiting SLC5A1 suppresses OGD/R-activated NLRP3 inflammasome and pyroptosis in HBMECs. A-E. Representative blots (A) and quantitative analysis (BeE) of NLRP3, cleaved caspase-1, IL-1b and GSDMD-NT expression in HBMECs after OGD stimulation, with or without phlorizin treatment. F-G. Pyroptotic cells with the same treatment in panel A were assessed by caspase-1 and PI staining. Representative flow cytometric images (F) and quantitative data (G) of caspase-1þ/PI þ cell ratio were provided. Results were reported as mean ± SD (n ¼ 3). ***p < 0.001.

    Article Snippet: Human recombinant SLC5A1 protein (Novus Biologicals, Littleton, CO, USA) was captured on a CM5 chip via a standard amine coupling procedure.

    Techniques: Expressing, Staining