horseradish peroxidase-conjugated secondary antibodies Search Results


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  • 99
    Thermo Fisher hrp conjugated secondary antibodies
    Hrp Conjugated Secondary Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 8439 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore horseradish peroxidase conjugated secondary antibodies
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 2125 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher horseradish peroxidase conjugated secondary antibodies
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4722 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase conjugated secondary antibody
    Horseradish Peroxidase Conjugated Secondary Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 3205 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad hrp conjugated secondary antibody
    Hrp Conjugated Secondary Antibody, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 2129 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc horseradish peroxidase conjugated secondary antibodies
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 2145 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase hrp conjugated secondary antibody
    PepE target the <t>TrxR1</t> through binding its Sec residue. (A) Inhibition assay of purified recombinant human TrxR1 or TrxR1 without Sec498 residue (nSec498, 0.1 μM) by PepE. The NADPH-reduced proteins were incubated with the indicated concentrations of PepE, and the enzyme's activity was determined by the DTNB assay (Data are presented as mean ± SD, n = 6). (B) Molecular docking of PepE with TrxR1 was carried out using the covalent docking protocol in the Schrodinger Suite. The yellow line indicated the covalent carbon bond, the green dotted lines indicate the hydrogen bonds. (C) Comparison of the binding activity between PepE and TrxR1 protein (red line), PepE and TrxR1 nSec498 protein (blue line), and PepA and TrxR1 protein (black line) through BLI analysis. (D) Kinetic analysis of the interaction between NADPH reduced TrxR1 (0.9 μM) or NADPH reduced TrxR1 nSec498 (0.9 μM) protein and PepE by BLI. The Super Streptavidin (SSA) biosensor tips coated with proteins (0.9 μM) were dipped in increasing concentrations of PepE (0.625, 1.25, 2.5, 5 and 10 μM) to measure the binding affinity of PepE to the proteins (K on ) and subsequently moved to wells containing buffer to measure dissociation rates (K dis ). The affinity constant (K D ) was calculated as the ratio of the K dis to the K on. (E) Kinetic analysis of the interaction between TrxR1 (0.9 μM) and different concentrations of PepA (1.25, 2.5, 5, 10 and 20 μM) by BLI. (F) The interaction of the PepE with the Sec residue in the C -terminal active center of TrxR1. <t>HRP-conjugated</t> streptavidin (HRP-Strep) detection of BIAM labeling of free Selenol in TrxR1 enzyme at pH 6.5 after this enzyme was incubated with different concentrations of PepE (1, 5 and 10 μM), DMSO(negative control), and DNCB (positive control, 5 μM), ** P
    Horseradish Peroxidase Hrp Conjugated Secondary Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1725 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher horseradish peroxidase hrp conjugated secondary antibodies
    PepE target the <t>TrxR1</t> through binding its Sec residue. (A) Inhibition assay of purified recombinant human TrxR1 or TrxR1 without Sec498 residue (nSec498, 0.1 μM) by PepE. The NADPH-reduced proteins were incubated with the indicated concentrations of PepE, and the enzyme's activity was determined by the DTNB assay (Data are presented as mean ± SD, n = 6). (B) Molecular docking of PepE with TrxR1 was carried out using the covalent docking protocol in the Schrodinger Suite. The yellow line indicated the covalent carbon bond, the green dotted lines indicate the hydrogen bonds. (C) Comparison of the binding activity between PepE and TrxR1 protein (red line), PepE and TrxR1 nSec498 protein (blue line), and PepA and TrxR1 protein (black line) through BLI analysis. (D) Kinetic analysis of the interaction between NADPH reduced TrxR1 (0.9 μM) or NADPH reduced TrxR1 nSec498 (0.9 μM) protein and PepE by BLI. The Super Streptavidin (SSA) biosensor tips coated with proteins (0.9 μM) were dipped in increasing concentrations of PepE (0.625, 1.25, 2.5, 5 and 10 μM) to measure the binding affinity of PepE to the proteins (K on ) and subsequently moved to wells containing buffer to measure dissociation rates (K dis ). The affinity constant (K D ) was calculated as the ratio of the K dis to the K on. (E) Kinetic analysis of the interaction between TrxR1 (0.9 μM) and different concentrations of PepA (1.25, 2.5, 5, 10 and 20 μM) by BLI. (F) The interaction of the PepE with the Sec residue in the C -terminal active center of TrxR1. <t>HRP-conjugated</t> streptavidin (HRP-Strep) detection of BIAM labeling of free Selenol in TrxR1 enzyme at pH 6.5 after this enzyme was incubated with different concentrations of PepE (1, 5 and 10 μM), DMSO(negative control), and DNCB (positive control, 5 μM), ** P
    Horseradish Peroxidase Hrp Conjugated Secondary Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2005 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore peroxidase conjugated secondary antibody
    PepE target the <t>TrxR1</t> through binding its Sec residue. (A) Inhibition assay of purified recombinant human TrxR1 or TrxR1 without Sec498 residue (nSec498, 0.1 μM) by PepE. The NADPH-reduced proteins were incubated with the indicated concentrations of PepE, and the enzyme's activity was determined by the DTNB assay (Data are presented as mean ± SD, n = 6). (B) Molecular docking of PepE with TrxR1 was carried out using the covalent docking protocol in the Schrodinger Suite. The yellow line indicated the covalent carbon bond, the green dotted lines indicate the hydrogen bonds. (C) Comparison of the binding activity between PepE and TrxR1 protein (red line), PepE and TrxR1 nSec498 protein (blue line), and PepA and TrxR1 protein (black line) through BLI analysis. (D) Kinetic analysis of the interaction between NADPH reduced TrxR1 (0.9 μM) or NADPH reduced TrxR1 nSec498 (0.9 μM) protein and PepE by BLI. The Super Streptavidin (SSA) biosensor tips coated with proteins (0.9 μM) were dipped in increasing concentrations of PepE (0.625, 1.25, 2.5, 5 and 10 μM) to measure the binding affinity of PepE to the proteins (K on ) and subsequently moved to wells containing buffer to measure dissociation rates (K dis ). The affinity constant (K D ) was calculated as the ratio of the K dis to the K on. (E) Kinetic analysis of the interaction between TrxR1 (0.9 μM) and different concentrations of PepA (1.25, 2.5, 5, 10 and 20 μM) by BLI. (F) The interaction of the PepE with the Sec residue in the C -terminal active center of TrxR1. <t>HRP-conjugated</t> streptavidin (HRP-Strep) detection of BIAM labeling of free Selenol in TrxR1 enzyme at pH 6.5 after this enzyme was incubated with different concentrations of PepE (1, 5 and 10 μM), DMSO(negative control), and DNCB (positive control, 5 μM), ** P
    Peroxidase Conjugated Secondary Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2948 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad horseradish peroxidase conjugated secondary antibody
    PepE target the <t>TrxR1</t> through binding its Sec residue. (A) Inhibition assay of purified recombinant human TrxR1 or TrxR1 without Sec498 residue (nSec498, 0.1 μM) by PepE. The NADPH-reduced proteins were incubated with the indicated concentrations of PepE, and the enzyme's activity was determined by the DTNB assay (Data are presented as mean ± SD, n = 6). (B) Molecular docking of PepE with TrxR1 was carried out using the covalent docking protocol in the Schrodinger Suite. The yellow line indicated the covalent carbon bond, the green dotted lines indicate the hydrogen bonds. (C) Comparison of the binding activity between PepE and TrxR1 protein (red line), PepE and TrxR1 nSec498 protein (blue line), and PepA and TrxR1 protein (black line) through BLI analysis. (D) Kinetic analysis of the interaction between NADPH reduced TrxR1 (0.9 μM) or NADPH reduced TrxR1 nSec498 (0.9 μM) protein and PepE by BLI. The Super Streptavidin (SSA) biosensor tips coated with proteins (0.9 μM) were dipped in increasing concentrations of PepE (0.625, 1.25, 2.5, 5 and 10 μM) to measure the binding affinity of PepE to the proteins (K on ) and subsequently moved to wells containing buffer to measure dissociation rates (K dis ). The affinity constant (K D ) was calculated as the ratio of the K dis to the K on. (E) Kinetic analysis of the interaction between TrxR1 (0.9 μM) and different concentrations of PepA (1.25, 2.5, 5, 10 and 20 μM) by BLI. (F) The interaction of the PepE with the Sec residue in the C -terminal active center of TrxR1. <t>HRP-conjugated</t> streptavidin (HRP-Strep) detection of BIAM labeling of free Selenol in TrxR1 enzyme at pH 6.5 after this enzyme was incubated with different concentrations of PepE (1, 5 and 10 μM), DMSO(negative control), and DNCB (positive control, 5 μM), ** P
    Horseradish Peroxidase Conjugated Secondary Antibody, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1327 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore horseradish peroxidase hrp conjugated secondary antibodies
    PepE target the <t>TrxR1</t> through binding its Sec residue. (A) Inhibition assay of purified recombinant human TrxR1 or TrxR1 without Sec498 residue (nSec498, 0.1 μM) by PepE. The NADPH-reduced proteins were incubated with the indicated concentrations of PepE, and the enzyme's activity was determined by the DTNB assay (Data are presented as mean ± SD, n = 6). (B) Molecular docking of PepE with TrxR1 was carried out using the covalent docking protocol in the Schrodinger Suite. The yellow line indicated the covalent carbon bond, the green dotted lines indicate the hydrogen bonds. (C) Comparison of the binding activity between PepE and TrxR1 protein (red line), PepE and TrxR1 nSec498 protein (blue line), and PepA and TrxR1 protein (black line) through BLI analysis. (D) Kinetic analysis of the interaction between NADPH reduced TrxR1 (0.9 μM) or NADPH reduced TrxR1 nSec498 (0.9 μM) protein and PepE by BLI. The Super Streptavidin (SSA) biosensor tips coated with proteins (0.9 μM) were dipped in increasing concentrations of PepE (0.625, 1.25, 2.5, 5 and 10 μM) to measure the binding affinity of PepE to the proteins (K on ) and subsequently moved to wells containing buffer to measure dissociation rates (K dis ). The affinity constant (K D ) was calculated as the ratio of the K dis to the K on. (E) Kinetic analysis of the interaction between TrxR1 (0.9 μM) and different concentrations of PepA (1.25, 2.5, 5, 10 and 20 μM) by BLI. (F) The interaction of the PepE with the Sec residue in the C -terminal active center of TrxR1. <t>HRP-conjugated</t> streptavidin (HRP-Strep) detection of BIAM labeling of free Selenol in TrxR1 enzyme at pH 6.5 after this enzyme was incubated with different concentrations of PepE (1, 5 and 10 μM), DMSO(negative control), and DNCB (positive control, 5 μM), ** P
    Horseradish Peroxidase Hrp Conjugated Secondary Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1111 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies horseradish peroxidase conjugated secondary antibody
    PepE target the <t>TrxR1</t> through binding its Sec residue. (A) Inhibition assay of purified recombinant human TrxR1 or TrxR1 without Sec498 residue (nSec498, 0.1 μM) by PepE. The NADPH-reduced proteins were incubated with the indicated concentrations of PepE, and the enzyme's activity was determined by the DTNB assay (Data are presented as mean ± SD, n = 6). (B) Molecular docking of PepE with TrxR1 was carried out using the covalent docking protocol in the Schrodinger Suite. The yellow line indicated the covalent carbon bond, the green dotted lines indicate the hydrogen bonds. (C) Comparison of the binding activity between PepE and TrxR1 protein (red line), PepE and TrxR1 nSec498 protein (blue line), and PepA and TrxR1 protein (black line) through BLI analysis. (D) Kinetic analysis of the interaction between NADPH reduced TrxR1 (0.9 μM) or NADPH reduced TrxR1 nSec498 (0.9 μM) protein and PepE by BLI. The Super Streptavidin (SSA) biosensor tips coated with proteins (0.9 μM) were dipped in increasing concentrations of PepE (0.625, 1.25, 2.5, 5 and 10 μM) to measure the binding affinity of PepE to the proteins (K on ) and subsequently moved to wells containing buffer to measure dissociation rates (K dis ). The affinity constant (K D ) was calculated as the ratio of the K dis to the K on. (E) Kinetic analysis of the interaction between TrxR1 (0.9 μM) and different concentrations of PepA (1.25, 2.5, 5, 10 and 20 μM) by BLI. (F) The interaction of the PepE with the Sec residue in the C -terminal active center of TrxR1. <t>HRP-conjugated</t> streptavidin (HRP-Strep) detection of BIAM labeling of free Selenol in TrxR1 enzyme at pH 6.5 after this enzyme was incubated with different concentrations of PepE (1, 5 and 10 μM), DMSO(negative control), and DNCB (positive control, 5 μM), ** P
    Horseradish Peroxidase Conjugated Secondary Antibody, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 967 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies horseradish peroxidase hrp conjugated secondary antibodies
    Expression of cavin1-myc-BirA* as a tool to label caveolar proteins. A . Schematic representation of constructs used in this study. B . Expression of constructs used in this study, analysed by Western blotting with anti-myc antibodies. C . Distribution of biotin in transfected cells, compared with caveolae labelled with antibodies against caveolin1. Anti-myc antibodies reveal the location of the indicated BirA* construct. <t>Streptavidin</t> reveals the location of biotinylated proteins. Arrowheads highlight examples of streptavidin-stained caveolae. Bar is 20 microns. Single confocal sections acquired with 63x objective. D . Blot of biotinylated proteins labelled with <t>streptavidin-HRP.</t> Cells were transfected with the myc-BirA* construct indicated at the top of each lane on the blot, and incubated with exogenous biotin before solubilisation. The band labelled 1 in the cavin1-myc-BirA* lane is the correct size to be cavin1-myc-BirA*, 2 is the correct size to be endogenous cavin1, and 3 is the correct size to be caveolin1. E . Western blot labelled with caveolin1 antibody. Cells were transfected with cavin1-myc-BirA* and incubated with exogenous biotin for the times shown, before solubilisation and precipitation of biotinylated proteins with immobilised streptavidin.
    Horseradish Peroxidase Hrp Conjugated Secondary Antibodies, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 533 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam horseradish peroxidase conjugated secondary antibodies
    Expression of cavin1-myc-BirA* as a tool to label caveolar proteins. A . Schematic representation of constructs used in this study. B . Expression of constructs used in this study, analysed by Western blotting with anti-myc antibodies. C . Distribution of biotin in transfected cells, compared with caveolae labelled with antibodies against caveolin1. Anti-myc antibodies reveal the location of the indicated BirA* construct. <t>Streptavidin</t> reveals the location of biotinylated proteins. Arrowheads highlight examples of streptavidin-stained caveolae. Bar is 20 microns. Single confocal sections acquired with 63x objective. D . Blot of biotinylated proteins labelled with <t>streptavidin-HRP.</t> Cells were transfected with the myc-BirA* construct indicated at the top of each lane on the blot, and incubated with exogenous biotin before solubilisation. The band labelled 1 in the cavin1-myc-BirA* lane is the correct size to be cavin1-myc-BirA*, 2 is the correct size to be endogenous cavin1, and 3 is the correct size to be caveolin1. E . Western blot labelled with caveolin1 antibody. Cells were transfected with cavin1-myc-BirA* and incubated with exogenous biotin for the times shown, before solubilisation and precipitation of biotinylated proteins with immobilised streptavidin.
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 617 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam horseradish peroxidase hrp conjugated secondary antibodies
    Expression of cavin1-myc-BirA* as a tool to label caveolar proteins. A . Schematic representation of constructs used in this study. B . Expression of constructs used in this study, analysed by Western blotting with anti-myc antibodies. C . Distribution of biotin in transfected cells, compared with caveolae labelled with antibodies against caveolin1. Anti-myc antibodies reveal the location of the indicated BirA* construct. <t>Streptavidin</t> reveals the location of biotinylated proteins. Arrowheads highlight examples of streptavidin-stained caveolae. Bar is 20 microns. Single confocal sections acquired with 63x objective. D . Blot of biotinylated proteins labelled with <t>streptavidin-HRP.</t> Cells were transfected with the myc-BirA* construct indicated at the top of each lane on the blot, and incubated with exogenous biotin before solubilisation. The band labelled 1 in the cavin1-myc-BirA* lane is the correct size to be cavin1-myc-BirA*, 2 is the correct size to be endogenous cavin1, and 3 is the correct size to be caveolin1. E . Western blot labelled with caveolin1 antibody. Cells were transfected with cavin1-myc-BirA* and incubated with exogenous biotin for the times shown, before solubilisation and precipitation of biotinylated proteins with immobilised streptavidin.
    Horseradish Peroxidase Hrp Conjugated Secondary Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 452 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Beyotime horseradish peroxidase conjugated secondary antibodies
    Expression of cavin1-myc-BirA* as a tool to label caveolar proteins. A . Schematic representation of constructs used in this study. B . Expression of constructs used in this study, analysed by Western blotting with anti-myc antibodies. C . Distribution of biotin in transfected cells, compared with caveolae labelled with antibodies against caveolin1. Anti-myc antibodies reveal the location of the indicated BirA* construct. <t>Streptavidin</t> reveals the location of biotinylated proteins. Arrowheads highlight examples of streptavidin-stained caveolae. Bar is 20 microns. Single confocal sections acquired with 63x objective. D . Blot of biotinylated proteins labelled with <t>streptavidin-HRP.</t> Cells were transfected with the myc-BirA* construct indicated at the top of each lane on the blot, and incubated with exogenous biotin before solubilisation. The band labelled 1 in the cavin1-myc-BirA* lane is the correct size to be cavin1-myc-BirA*, 2 is the correct size to be endogenous cavin1, and 3 is the correct size to be caveolin1. E . Western blot labelled with caveolin1 antibody. Cells were transfected with cavin1-myc-BirA* and incubated with exogenous biotin for the times shown, before solubilisation and precipitation of biotinylated proteins with immobilised streptavidin.
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Beyotime, used in various techniques. Bioz Stars score: 92/100, based on 400 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega horseradish peroxidase conjugated secondary antibodies
    Expression of cavin1-myc-BirA* as a tool to label caveolar proteins. A . Schematic representation of constructs used in this study. B . Expression of constructs used in this study, analysed by Western blotting with anti-myc antibodies. C . Distribution of biotin in transfected cells, compared with caveolae labelled with antibodies against caveolin1. Anti-myc antibodies reveal the location of the indicated BirA* construct. <t>Streptavidin</t> reveals the location of biotinylated proteins. Arrowheads highlight examples of streptavidin-stained caveolae. Bar is 20 microns. Single confocal sections acquired with 63x objective. D . Blot of biotinylated proteins labelled with <t>streptavidin-HRP.</t> Cells were transfected with the myc-BirA* construct indicated at the top of each lane on the blot, and incubated with exogenous biotin before solubilisation. The band labelled 1 in the cavin1-myc-BirA* lane is the correct size to be cavin1-myc-BirA*, 2 is the correct size to be endogenous cavin1, and 3 is the correct size to be caveolin1. E . Western blot labelled with caveolin1 antibody. Cells were transfected with cavin1-myc-BirA* and incubated with exogenous biotin for the times shown, before solubilisation and precipitation of biotinylated proteins with immobilised streptavidin.
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 400 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Beyotime horseradish peroxidase hrp conjugated secondary antibodies
    Expression of cavin1-myc-BirA* as a tool to label caveolar proteins. A . Schematic representation of constructs used in this study. B . Expression of constructs used in this study, analysed by Western blotting with anti-myc antibodies. C . Distribution of biotin in transfected cells, compared with caveolae labelled with antibodies against caveolin1. Anti-myc antibodies reveal the location of the indicated BirA* construct. <t>Streptavidin</t> reveals the location of biotinylated proteins. Arrowheads highlight examples of streptavidin-stained caveolae. Bar is 20 microns. Single confocal sections acquired with 63x objective. D . Blot of biotinylated proteins labelled with <t>streptavidin-HRP.</t> Cells were transfected with the myc-BirA* construct indicated at the top of each lane on the blot, and incubated with exogenous biotin before solubilisation. The band labelled 1 in the cavin1-myc-BirA* lane is the correct size to be cavin1-myc-BirA*, 2 is the correct size to be endogenous cavin1, and 3 is the correct size to be caveolin1. E . Western blot labelled with caveolin1 antibody. Cells were transfected with cavin1-myc-BirA* and incubated with exogenous biotin for the times shown, before solubilisation and precipitation of biotinylated proteins with immobilised streptavidin.
    Horseradish Peroxidase Hrp Conjugated Secondary Antibodies, supplied by Beyotime, used in various techniques. Bioz Stars score: 92/100, based on 188 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    PepE target the TrxR1 through binding its Sec residue. (A) Inhibition assay of purified recombinant human TrxR1 or TrxR1 without Sec498 residue (nSec498, 0.1 μM) by PepE. The NADPH-reduced proteins were incubated with the indicated concentrations of PepE, and the enzyme's activity was determined by the DTNB assay (Data are presented as mean ± SD, n = 6). (B) Molecular docking of PepE with TrxR1 was carried out using the covalent docking protocol in the Schrodinger Suite. The yellow line indicated the covalent carbon bond, the green dotted lines indicate the hydrogen bonds. (C) Comparison of the binding activity between PepE and TrxR1 protein (red line), PepE and TrxR1 nSec498 protein (blue line), and PepA and TrxR1 protein (black line) through BLI analysis. (D) Kinetic analysis of the interaction between NADPH reduced TrxR1 (0.9 μM) or NADPH reduced TrxR1 nSec498 (0.9 μM) protein and PepE by BLI. The Super Streptavidin (SSA) biosensor tips coated with proteins (0.9 μM) were dipped in increasing concentrations of PepE (0.625, 1.25, 2.5, 5 and 10 μM) to measure the binding affinity of PepE to the proteins (K on ) and subsequently moved to wells containing buffer to measure dissociation rates (K dis ). The affinity constant (K D ) was calculated as the ratio of the K dis to the K on. (E) Kinetic analysis of the interaction between TrxR1 (0.9 μM) and different concentrations of PepA (1.25, 2.5, 5, 10 and 20 μM) by BLI. (F) The interaction of the PepE with the Sec residue in the C -terminal active center of TrxR1. HRP-conjugated streptavidin (HRP-Strep) detection of BIAM labeling of free Selenol in TrxR1 enzyme at pH 6.5 after this enzyme was incubated with different concentrations of PepE (1, 5 and 10 μM), DMSO(negative control), and DNCB (positive control, 5 μM), ** P

    Journal: Redox Biology

    Article Title: Peperomin E and its orally bioavailable analog induce oxidative stress-mediated apoptosis of acute myeloid leukemia progenitor cells by targeting thioredoxin reductase

    doi: 10.1016/j.redox.2019.101153

    Figure Lengend Snippet: PepE target the TrxR1 through binding its Sec residue. (A) Inhibition assay of purified recombinant human TrxR1 or TrxR1 without Sec498 residue (nSec498, 0.1 μM) by PepE. The NADPH-reduced proteins were incubated with the indicated concentrations of PepE, and the enzyme's activity was determined by the DTNB assay (Data are presented as mean ± SD, n = 6). (B) Molecular docking of PepE with TrxR1 was carried out using the covalent docking protocol in the Schrodinger Suite. The yellow line indicated the covalent carbon bond, the green dotted lines indicate the hydrogen bonds. (C) Comparison of the binding activity between PepE and TrxR1 protein (red line), PepE and TrxR1 nSec498 protein (blue line), and PepA and TrxR1 protein (black line) through BLI analysis. (D) Kinetic analysis of the interaction between NADPH reduced TrxR1 (0.9 μM) or NADPH reduced TrxR1 nSec498 (0.9 μM) protein and PepE by BLI. The Super Streptavidin (SSA) biosensor tips coated with proteins (0.9 μM) were dipped in increasing concentrations of PepE (0.625, 1.25, 2.5, 5 and 10 μM) to measure the binding affinity of PepE to the proteins (K on ) and subsequently moved to wells containing buffer to measure dissociation rates (K dis ). The affinity constant (K D ) was calculated as the ratio of the K dis to the K on. (E) Kinetic analysis of the interaction between TrxR1 (0.9 μM) and different concentrations of PepA (1.25, 2.5, 5, 10 and 20 μM) by BLI. (F) The interaction of the PepE with the Sec residue in the C -terminal active center of TrxR1. HRP-conjugated streptavidin (HRP-Strep) detection of BIAM labeling of free Selenol in TrxR1 enzyme at pH 6.5 after this enzyme was incubated with different concentrations of PepE (1, 5 and 10 μM), DMSO(negative control), and DNCB (positive control, 5 μM), ** P

    Article Snippet: Horseradish peroxidase (HRP)-conjugated secondary antibody (goat anti-rabbit), human TrxR1 shRNA plasmids, control shRNA plasmids, TrxR1 CRISPR activation plasmids, control CRISPR activation plasmids were obtained from Santa Cruz Biotech.

    Techniques: Binding Assay, Size-exclusion Chromatography, Inhibition, Purification, Recombinant, Incubation, Activity Assay, DTNB Assay, Labeling, Positive Control

    Expression of cavin1-myc-BirA* as a tool to label caveolar proteins. A . Schematic representation of constructs used in this study. B . Expression of constructs used in this study, analysed by Western blotting with anti-myc antibodies. C . Distribution of biotin in transfected cells, compared with caveolae labelled with antibodies against caveolin1. Anti-myc antibodies reveal the location of the indicated BirA* construct. Streptavidin reveals the location of biotinylated proteins. Arrowheads highlight examples of streptavidin-stained caveolae. Bar is 20 microns. Single confocal sections acquired with 63x objective. D . Blot of biotinylated proteins labelled with streptavidin-HRP. Cells were transfected with the myc-BirA* construct indicated at the top of each lane on the blot, and incubated with exogenous biotin before solubilisation. The band labelled 1 in the cavin1-myc-BirA* lane is the correct size to be cavin1-myc-BirA*, 2 is the correct size to be endogenous cavin1, and 3 is the correct size to be caveolin1. E . Western blot labelled with caveolin1 antibody. Cells were transfected with cavin1-myc-BirA* and incubated with exogenous biotin for the times shown, before solubilisation and precipitation of biotinylated proteins with immobilised streptavidin.

    Journal: PLoS ONE

    Article Title: BioID identifies proteins involved in the cell biology of caveolae

    doi: 10.1371/journal.pone.0209856

    Figure Lengend Snippet: Expression of cavin1-myc-BirA* as a tool to label caveolar proteins. A . Schematic representation of constructs used in this study. B . Expression of constructs used in this study, analysed by Western blotting with anti-myc antibodies. C . Distribution of biotin in transfected cells, compared with caveolae labelled with antibodies against caveolin1. Anti-myc antibodies reveal the location of the indicated BirA* construct. Streptavidin reveals the location of biotinylated proteins. Arrowheads highlight examples of streptavidin-stained caveolae. Bar is 20 microns. Single confocal sections acquired with 63x objective. D . Blot of biotinylated proteins labelled with streptavidin-HRP. Cells were transfected with the myc-BirA* construct indicated at the top of each lane on the blot, and incubated with exogenous biotin before solubilisation. The band labelled 1 in the cavin1-myc-BirA* lane is the correct size to be cavin1-myc-BirA*, 2 is the correct size to be endogenous cavin1, and 3 is the correct size to be caveolin1. E . Western blot labelled with caveolin1 antibody. Cells were transfected with cavin1-myc-BirA* and incubated with exogenous biotin for the times shown, before solubilisation and precipitation of biotinylated proteins with immobilised streptavidin.

    Article Snippet: Horseradish peroxidase (HRP)-conjugated secondary antibodies were from DAKO and Streptavidin HRP from Cell Signalling (Cat# 3999).

    Techniques: Expressing, Construct, Western Blot, Transfection, Staining, Incubation