kv1 1 c terminus  (Alomone Labs)


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    Structured Review

    Alomone Labs kv1 1 c terminus
    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or <t>Kv1.1</t> GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Kv1 1 C Terminus, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin"

    Article Title: K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.4006-06.2007

    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Figure Legend Snippet: The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).

    Techniques Used: Immunoprecipitation, Recombinant, Staining, Concentration Assay, Transfection, Plasmid Preparation, Expressing

    kv1 1 c terminus  (Alomone Labs)


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    Alomone Labs kv1 1 c terminus
    (A) PC12 cells preloaded with [ 3 H]-NE and gently homogenized ( “cracked” cells), either underwent 15 min incubation in the presence of 2 mM MgATP and brain cytosol at 30°C (“priming”) or not, followed by either 15 min incubation with added 1.6 mM Ca 2+ (1 µM free Ca 2+ ; at 30° (“triggering”) or not, as indicated below the bars. Cells were pelleted and the secreted [ 3 H]-NE in the supernatant was quantified by scintillation counting and expressed as a percentage of the total [ 3 H]-NE in the cell. 10 6 cells per reaction were used. The difference between the amounts of [ 3 H]-NE secreted in the two reactions on the two bars on the right was defined and is referred to hereafter as the Ca 2+ -triggered release. (B) Cracked cells preloaded with [ 3 H]-NE underwent priming and triggering reactions in the absence or presence of 10–20 µM GST-fusion peptides corresponding to cytosolic parts of Kv2.1 and <t>Kv1.1</t> (shown in ) or to GST itself (as indicated below bars). Values of Ca 2+ -triggered release measured in the presence of the peptides (see ) were normalized to the control release determined in the absence of peptides (defined as 100%). Each bar in A and B depicts the mean±s.e.m from several independent experiments (numbers of experiments are in parentheses above bars). **, p <0.001 (compared with GST). (C) Cells were stimulated to release NE in the presence of increasing concentrations of GST-fused Kv2.1-C1 protein. Each point in the curve represents mean±s.e.m values from several independent experiments (numbers of experiments in parentheses above bars). **, p<0.001 (compared with 10 nM GST-C1).
    Kv1 1 C Terminus, supplied by Alomone Labs, 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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    Images

    1) Product Images from "Direct Interaction of Endogenous Kv Channels with Syntaxin Enhances Exocytosis by Neuroendocrine Cells"

    Article Title: Direct Interaction of Endogenous Kv Channels with Syntaxin Enhances Exocytosis by Neuroendocrine Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0001381

    (A) PC12 cells preloaded with [ 3 H]-NE and gently homogenized ( “cracked” cells), either underwent 15 min incubation in the presence of 2 mM MgATP and brain cytosol at 30°C (“priming”) or not, followed by either 15 min incubation with added 1.6 mM Ca 2+ (1 µM free Ca 2+ ; at 30° (“triggering”) or not, as indicated below the bars. Cells were pelleted and the secreted [ 3 H]-NE in the supernatant was quantified by scintillation counting and expressed as a percentage of the total [ 3 H]-NE in the cell. 10 6 cells per reaction were used. The difference between the amounts of [ 3 H]-NE secreted in the two reactions on the two bars on the right was defined and is referred to hereafter as the Ca 2+ -triggered release. (B) Cracked cells preloaded with [ 3 H]-NE underwent priming and triggering reactions in the absence or presence of 10–20 µM GST-fusion peptides corresponding to cytosolic parts of Kv2.1 and Kv1.1 (shown in ) or to GST itself (as indicated below bars). Values of Ca 2+ -triggered release measured in the presence of the peptides (see ) were normalized to the control release determined in the absence of peptides (defined as 100%). Each bar in A and B depicts the mean±s.e.m from several independent experiments (numbers of experiments are in parentheses above bars). **, p <0.001 (compared with GST). (C) Cells were stimulated to release NE in the presence of increasing concentrations of GST-fused Kv2.1-C1 protein. Each point in the curve represents mean±s.e.m values from several independent experiments (numbers of experiments in parentheses above bars). **, p<0.001 (compared with 10 nM GST-C1).
    Figure Legend Snippet: (A) PC12 cells preloaded with [ 3 H]-NE and gently homogenized ( “cracked” cells), either underwent 15 min incubation in the presence of 2 mM MgATP and brain cytosol at 30°C (“priming”) or not, followed by either 15 min incubation with added 1.6 mM Ca 2+ (1 µM free Ca 2+ ; at 30° (“triggering”) or not, as indicated below the bars. Cells were pelleted and the secreted [ 3 H]-NE in the supernatant was quantified by scintillation counting and expressed as a percentage of the total [ 3 H]-NE in the cell. 10 6 cells per reaction were used. The difference between the amounts of [ 3 H]-NE secreted in the two reactions on the two bars on the right was defined and is referred to hereafter as the Ca 2+ -triggered release. (B) Cracked cells preloaded with [ 3 H]-NE underwent priming and triggering reactions in the absence or presence of 10–20 µM GST-fusion peptides corresponding to cytosolic parts of Kv2.1 and Kv1.1 (shown in ) or to GST itself (as indicated below bars). Values of Ca 2+ -triggered release measured in the presence of the peptides (see ) were normalized to the control release determined in the absence of peptides (defined as 100%). Each bar in A and B depicts the mean±s.e.m from several independent experiments (numbers of experiments are in parentheses above bars). **, p <0.001 (compared with GST). (C) Cells were stimulated to release NE in the presence of increasing concentrations of GST-fused Kv2.1-C1 protein. Each point in the curve represents mean±s.e.m values from several independent experiments (numbers of experiments in parentheses above bars). **, p<0.001 (compared with 10 nM GST-C1).

    Techniques Used: Incubation

    kv1 1 c terminus  (Alomone Labs)


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    Structured Review

    Alomone Labs kv1 1 c terminus
    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or <t>Kv1.1</t> GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Kv1 1 C Terminus, supplied by Alomone Labs, 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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    Images

    1) Product Images from "K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin"

    Article Title: K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.4006-06.2007

    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Figure Legend Snippet: The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).

    Techniques Used: Immunoprecipitation, Recombinant, Staining, Concentration Assay, Transfection, Plasmid Preparation, Expressing

    kv1 1 c terminus  (Alomone Labs)


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    Alomone Labs kv1 1 c terminus
    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or <t>Kv1.1</t> GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Kv1 1 C Terminus, supplied by Alomone Labs, 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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    Images

    1) Product Images from "K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin"

    Article Title: K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.4006-06.2007

    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Figure Legend Snippet: The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).

    Techniques Used: Immunoprecipitation, Recombinant, Staining, Concentration Assay, Transfection, Plasmid Preparation, Expressing

    kv1 1 c terminus  (Alomone Labs)


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    Alomone Labs kv1 1 c terminus
    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or <t>Kv1.1</t> GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Kv1 1 C Terminus, supplied by Alomone Labs, 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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    1) Product Images from "K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin"

    Article Title: K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.4006-06.2007

    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Figure Legend Snippet: The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).

    Techniques Used: Immunoprecipitation, Recombinant, Staining, Concentration Assay, Transfection, Plasmid Preparation, Expressing

    kv1 1 c terminus  (Alomone Labs)


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    Alomone Labs kv1 1 c terminus
    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or <t>Kv1.1</t> GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
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    1) Product Images from "K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin"

    Article Title: K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.4006-06.2007

    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Figure Legend Snippet: The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).

    Techniques Used: Immunoprecipitation, Recombinant, Staining, Concentration Assay, Transfection, Plasmid Preparation, Expressing

    polyclonal kv1 1 c terminus  (Alomone Labs)


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    Alomone Labs polyclonal kv1 1 c terminus
    Polyclonal Kv1 1 C Terminus, supplied by Alomone Labs, 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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    kv1 1 c terminus  (Alomone Labs)


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    Alomone Labs kv1 1 c terminus
    <t>Kv1.1</t> and Kvβ proteins interact with syntaxin in fresh brain synaptosomes. A–C, The interaction with syntaxin also involves SNAP-25 and synaptotagmin. Fresh brain synaptosomal lysates were immunoprecipitated (IP) by Kv1.1, Kvβ, syntaxin 1A, or IgG (irrelevant) antibodies, as indicated above the lanes. The immunoprecipitated proteins were separated by SDS−PAGE, blotted, and detected by antibodies, as indicated at the sides of the blots.Syx, Syntaxin 1A (anti-HPC-1); Tagmin, synaptotagmin; SNAP, SNAP-25; HC, heavy chain of the antibodies used. Molecular weight markers are shown on theright in C. Each of the results shown inA and C is representative of four similar experiments performed using either 2% CHAPS or 1% Triton X-100. The result shown in B is representative of two similar experiments. For each IP reaction we used 200 μg of synaptosomes and loaded 0.5 or 45 μg of synaptosomes on Total (no immunoprecipitation was performed) lanes for blotting with syntaxin or Kvβ and Kv1.1, respectively. D, In intact fresh synaptosomes, interaction of Kv1.1 with syntaxin occurs in situ. Immunoprecipitations were performed with antibodies against synapsin and Kv1.1, after in situ cross-linking of intact synaptosomes. After solubilization by SDS, each reaction was performed with 100 μg of either DSP-treated or DMSO-treated synaptosomes (no cx). Total indicates that no immunoprecipitation was performed. In each reaction, the proteins were loaded on an 8.5% SDS gel before (−) or after (+) reduction with 100 mm DTT. The gel was blotted and processed for Western analysis using syntaxin antibodies (top panel). High molecular weight bands (marked byarrows) were detected. In an identical IP experiment, proteins were separated on 12.5% SDS gel and immunoblotted with syntaxin antibodies (bottom panel). Immunoreactivity with syntaxin was increased after reduction of the DSP-treated synaptosomes. E, Dynamic interaction between the Kv1.1 and syntaxin. Reciprocal coimmunoprecipitations by Kv1.1 (left panel) and syntaxin antibodies (right panel) were followed by SDS−PAGE, blotting, and detection by the indicated antibodies. Stimulation of the synaptosomes (incubation with 1.6 mm external Ca2+ and 60 mm external KCl; see Materials and Methods) before the immunoprecipitation was followed by a severalfold reduction in the interaction between syntaxin and Kv1.1 (compare 5 mm KCl and Stimulated lanes in both panels). For control, synaptosomes were incubated with either high concentrations of external KCl alone (30 mm KCl and 60 mm KCl) or with 2 mm EGTA (and 5 mm KCl) (No Ca2+). The same pattern was observed in four independent experiments; quantification of syntaxin normalized to Kv1.1 (left panel) and quantification of Kv1.1 and synaptotagmin, each normalized to syntaxin (right panel), are indicated below thelanes.
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    1) Product Images from "Direct Interaction of a Brain Voltage-Gated K + Channel with Syntaxin 1A: Functional Impact on Channel Gating"

    Article Title: Direct Interaction of a Brain Voltage-Gated K + Channel with Syntaxin 1A: Functional Impact on Channel Gating

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.21-06-01964.2001

    Kv1.1 and Kvβ proteins interact with syntaxin in fresh brain synaptosomes. A–C, The interaction with syntaxin also involves SNAP-25 and synaptotagmin. Fresh brain synaptosomal lysates were immunoprecipitated (IP) by Kv1.1, Kvβ, syntaxin 1A, or IgG (irrelevant) antibodies, as indicated above the lanes. The immunoprecipitated proteins were separated by SDS−PAGE, blotted, and detected by antibodies, as indicated at the sides of the blots.Syx, Syntaxin 1A (anti-HPC-1); Tagmin, synaptotagmin; SNAP, SNAP-25; HC, heavy chain of the antibodies used. Molecular weight markers are shown on theright in C. Each of the results shown inA and C is representative of four similar experiments performed using either 2% CHAPS or 1% Triton X-100. The result shown in B is representative of two similar experiments. For each IP reaction we used 200 μg of synaptosomes and loaded 0.5 or 45 μg of synaptosomes on Total (no immunoprecipitation was performed) lanes for blotting with syntaxin or Kvβ and Kv1.1, respectively. D, In intact fresh synaptosomes, interaction of Kv1.1 with syntaxin occurs in situ. Immunoprecipitations were performed with antibodies against synapsin and Kv1.1, after in situ cross-linking of intact synaptosomes. After solubilization by SDS, each reaction was performed with 100 μg of either DSP-treated or DMSO-treated synaptosomes (no cx). Total indicates that no immunoprecipitation was performed. In each reaction, the proteins were loaded on an 8.5% SDS gel before (−) or after (+) reduction with 100 mm DTT. The gel was blotted and processed for Western analysis using syntaxin antibodies (top panel). High molecular weight bands (marked byarrows) were detected. In an identical IP experiment, proteins were separated on 12.5% SDS gel and immunoblotted with syntaxin antibodies (bottom panel). Immunoreactivity with syntaxin was increased after reduction of the DSP-treated synaptosomes. E, Dynamic interaction between the Kv1.1 and syntaxin. Reciprocal coimmunoprecipitations by Kv1.1 (left panel) and syntaxin antibodies (right panel) were followed by SDS−PAGE, blotting, and detection by the indicated antibodies. Stimulation of the synaptosomes (incubation with 1.6 mm external Ca2+ and 60 mm external KCl; see Materials and Methods) before the immunoprecipitation was followed by a severalfold reduction in the interaction between syntaxin and Kv1.1 (compare 5 mm KCl and Stimulated lanes in both panels). For control, synaptosomes were incubated with either high concentrations of external KCl alone (30 mm KCl and 60 mm KCl) or with 2 mm EGTA (and 5 mm KCl) (No Ca2+). The same pattern was observed in four independent experiments; quantification of syntaxin normalized to Kv1.1 (left panel) and quantification of Kv1.1 and synaptotagmin, each normalized to syntaxin (right panel), are indicated below thelanes.
    Figure Legend Snippet: Kv1.1 and Kvβ proteins interact with syntaxin in fresh brain synaptosomes. A–C, The interaction with syntaxin also involves SNAP-25 and synaptotagmin. Fresh brain synaptosomal lysates were immunoprecipitated (IP) by Kv1.1, Kvβ, syntaxin 1A, or IgG (irrelevant) antibodies, as indicated above the lanes. The immunoprecipitated proteins were separated by SDS−PAGE, blotted, and detected by antibodies, as indicated at the sides of the blots.Syx, Syntaxin 1A (anti-HPC-1); Tagmin, synaptotagmin; SNAP, SNAP-25; HC, heavy chain of the antibodies used. Molecular weight markers are shown on theright in C. Each of the results shown inA and C is representative of four similar experiments performed using either 2% CHAPS or 1% Triton X-100. The result shown in B is representative of two similar experiments. For each IP reaction we used 200 μg of synaptosomes and loaded 0.5 or 45 μg of synaptosomes on Total (no immunoprecipitation was performed) lanes for blotting with syntaxin or Kvβ and Kv1.1, respectively. D, In intact fresh synaptosomes, interaction of Kv1.1 with syntaxin occurs in situ. Immunoprecipitations were performed with antibodies against synapsin and Kv1.1, after in situ cross-linking of intact synaptosomes. After solubilization by SDS, each reaction was performed with 100 μg of either DSP-treated or DMSO-treated synaptosomes (no cx). Total indicates that no immunoprecipitation was performed. In each reaction, the proteins were loaded on an 8.5% SDS gel before (−) or after (+) reduction with 100 mm DTT. The gel was blotted and processed for Western analysis using syntaxin antibodies (top panel). High molecular weight bands (marked byarrows) were detected. In an identical IP experiment, proteins were separated on 12.5% SDS gel and immunoblotted with syntaxin antibodies (bottom panel). Immunoreactivity with syntaxin was increased after reduction of the DSP-treated synaptosomes. E, Dynamic interaction between the Kv1.1 and syntaxin. Reciprocal coimmunoprecipitations by Kv1.1 (left panel) and syntaxin antibodies (right panel) were followed by SDS−PAGE, blotting, and detection by the indicated antibodies. Stimulation of the synaptosomes (incubation with 1.6 mm external Ca2+ and 60 mm external KCl; see Materials and Methods) before the immunoprecipitation was followed by a severalfold reduction in the interaction between syntaxin and Kv1.1 (compare 5 mm KCl and Stimulated lanes in both panels). For control, synaptosomes were incubated with either high concentrations of external KCl alone (30 mm KCl and 60 mm KCl) or with 2 mm EGTA (and 5 mm KCl) (No Ca2+). The same pattern was observed in four independent experiments; quantification of syntaxin normalized to Kv1.1 (left panel) and quantification of Kv1.1 and synaptotagmin, each normalized to syntaxin (right panel), are indicated below thelanes.

    Techniques Used: Immunoprecipitation, SDS Page, Molecular Weight, In Situ, SDS-Gel, Western Blot, Incubation

    Interaction of recombinant full-length Kvβ1.1 with syntaxin 1A. A, GST−Kvβ1.1 fusion protein pulls down syntaxin 1A from brain synaptosomes.GST−Kvβ1.1,GST−Kv1.1C (corresponding to the C terminus of Kv1.1), or GST immobilized on GSH−agarose beads (each at 150 pmol) was incubated with 2% CHAPS synaptosomal lysate (200 μg) for 12 hr at 4°C. Precipitated proteins were separated by SDS−PAGE (12% polyacrylamide) and immunoblotted (IB) with either anti-syntaxin 1A antibody (IB Syx; bottom left panel) or anti-GST antibodies (IB GST; bottom right panel). Normalized relative ECL signal intensities of bound syntaxin (derived from IB Syx) for each of the GST proteins normalized to its relative amount (derived from IB GST) were derived from four experiments (in one of which we used 4% Triton X-100, instead of CHAPS lysate) (top panel). The predicted position of the fusion protein is indicated by an asterisk. Numbers on theright refer to the mobility of prestained molecular weight standards. B, Direct interaction between syntaxin and the recombinant Kvβ1.1. A 200 pmol cytosolic syntaxin (amino acid 4–264), cleaved from the corresponding GST fusion protein by thrombin, was incubated with 200 pmol of the indicated GST fusion proteins (as inA;GST−L753–893corresponding to domain II−III of the L-type Ca2+channel was included for reference) immobilized on GSH−agarose beads in a 1 ml reaction volume. Binding of syntaxin was detected by Western analysis using syntaxin antibody. Top panel, Relative values of syntaxin-binding intensities for each of the GST fragments (bottom panel) normalized to the corresponding Ponceau S staining intensities (data not shown). The values shown are the mean results of three experiments, in one of which we used 5 μl of in vitro-synthesized 35S-labeled full-length syntaxin instead of the thrombinized syntaxin. GST−L753–893 was used in only one experiment.C, Stoichiometry of the binding of syntaxin 1A to Kvβ1.1, derived from binding curves that show saturation. Thrombinized cytosolic fragment of syntaxin at the indicated concentrations was bound to immobilized GST−Kvβ1.1 (10 pmol) in a 1 ml reaction volume. Bound syntaxin was determined by SDS−PAGE and immunoblotting with syntaxin antibody (inset), and GST−Kvβ1.1 was determined by immunoblotting with an anti-GST antibody (data not shown). ECL signal intensities were quantitated with TINA software and converted to picomoles by the use of standard curves for the corresponding proteins. The data were averaged from two independent experiments. D, Binding of syntaxin to Kvβ1.1 is blocked by the synprint peptide N718–963. Thrombinized cytoplasmic syntaxin was bound to immobilized GST−Kvβ1.1 (150 pmol) in the presence of either increasing His6−N718–963 concentrations or His6−N718–859 as control, as indicated. Thebar diagram shows the normalized syntaxin binding values, derived as in A, according to the intensity of immunostaining for syntaxin (Syx) and GST−Kvβ1.1 (below bars). The molar ratio in each of the reactions between GST−Kvβ1.1 and the His6-peptides is indicated below the corresponding bars (bottom panel).
    Figure Legend Snippet: Interaction of recombinant full-length Kvβ1.1 with syntaxin 1A. A, GST−Kvβ1.1 fusion protein pulls down syntaxin 1A from brain synaptosomes.GST−Kvβ1.1,GST−Kv1.1C (corresponding to the C terminus of Kv1.1), or GST immobilized on GSH−agarose beads (each at 150 pmol) was incubated with 2% CHAPS synaptosomal lysate (200 μg) for 12 hr at 4°C. Precipitated proteins were separated by SDS−PAGE (12% polyacrylamide) and immunoblotted (IB) with either anti-syntaxin 1A antibody (IB Syx; bottom left panel) or anti-GST antibodies (IB GST; bottom right panel). Normalized relative ECL signal intensities of bound syntaxin (derived from IB Syx) for each of the GST proteins normalized to its relative amount (derived from IB GST) were derived from four experiments (in one of which we used 4% Triton X-100, instead of CHAPS lysate) (top panel). The predicted position of the fusion protein is indicated by an asterisk. Numbers on theright refer to the mobility of prestained molecular weight standards. B, Direct interaction between syntaxin and the recombinant Kvβ1.1. A 200 pmol cytosolic syntaxin (amino acid 4–264), cleaved from the corresponding GST fusion protein by thrombin, was incubated with 200 pmol of the indicated GST fusion proteins (as inA;GST−L753–893corresponding to domain II−III of the L-type Ca2+channel was included for reference) immobilized on GSH−agarose beads in a 1 ml reaction volume. Binding of syntaxin was detected by Western analysis using syntaxin antibody. Top panel, Relative values of syntaxin-binding intensities for each of the GST fragments (bottom panel) normalized to the corresponding Ponceau S staining intensities (data not shown). The values shown are the mean results of three experiments, in one of which we used 5 μl of in vitro-synthesized 35S-labeled full-length syntaxin instead of the thrombinized syntaxin. GST−L753–893 was used in only one experiment.C, Stoichiometry of the binding of syntaxin 1A to Kvβ1.1, derived from binding curves that show saturation. Thrombinized cytosolic fragment of syntaxin at the indicated concentrations was bound to immobilized GST−Kvβ1.1 (10 pmol) in a 1 ml reaction volume. Bound syntaxin was determined by SDS−PAGE and immunoblotting with syntaxin antibody (inset), and GST−Kvβ1.1 was determined by immunoblotting with an anti-GST antibody (data not shown). ECL signal intensities were quantitated with TINA software and converted to picomoles by the use of standard curves for the corresponding proteins. The data were averaged from two independent experiments. D, Binding of syntaxin to Kvβ1.1 is blocked by the synprint peptide N718–963. Thrombinized cytoplasmic syntaxin was bound to immobilized GST−Kvβ1.1 (150 pmol) in the presence of either increasing His6−N718–963 concentrations or His6−N718–859 as control, as indicated. Thebar diagram shows the normalized syntaxin binding values, derived as in A, according to the intensity of immunostaining for syntaxin (Syx) and GST−Kvβ1.1 (below bars). The molar ratio in each of the reactions between GST−Kvβ1.1 and the His6-peptides is indicated below the corresponding bars (bottom panel).

    Techniques Used: Recombinant, Incubation, SDS Page, Derivative Assay, Molecular Weight, Binding Assay, Western Blot, Staining, In Vitro, Synthesized, Labeling, Software, Immunostaining

    The Kv1.1/Kvβ1.1 (αβ) channel interacts physically with syntaxin 1A in oocytes. A, Digitized Phosphorimager scan of SDS−PAGE analysis of [35S]Met/Cys-labeled αβ and syntaxin 1A proteins coprecipitated by α antibody (IP α) from homogenates of plasma membranes (PM) or internal fractions (IF) of oocytes that were uninjected (c), injected with α and β mRNAs only (αβ), coinjected with syntaxin 1A (2.5 ng/oocyte; αβ+syx), or injected with syntaxin alone (syx). The left lane shows syntaxin immunoprecipitated by syntaxin antibody from oocytes injected with syntaxin-1A mRNA alone to mark the migration of syntaxin. The protein samples were analyzed on a 5−15% gradient gel to separate between the lower band of β and the syntaxin band. Arrows indicate the relevant proteins. The results shown are from one of three independent experiments. B, Reciprocal coimmunoprecipitation in plasma membranes of oocytes from the same experiment, performed using a monoclonal syntaxin 1A antibody (IPsyx).
    Figure Legend Snippet: The Kv1.1/Kvβ1.1 (αβ) channel interacts physically with syntaxin 1A in oocytes. A, Digitized Phosphorimager scan of SDS−PAGE analysis of [35S]Met/Cys-labeled αβ and syntaxin 1A proteins coprecipitated by α antibody (IP α) from homogenates of plasma membranes (PM) or internal fractions (IF) of oocytes that were uninjected (c), injected with α and β mRNAs only (αβ), coinjected with syntaxin 1A (2.5 ng/oocyte; αβ+syx), or injected with syntaxin alone (syx). The left lane shows syntaxin immunoprecipitated by syntaxin antibody from oocytes injected with syntaxin-1A mRNA alone to mark the migration of syntaxin. The protein samples were analyzed on a 5−15% gradient gel to separate between the lower band of β and the syntaxin band. Arrows indicate the relevant proteins. The results shown are from one of three independent experiments. B, Reciprocal coimmunoprecipitation in plasma membranes of oocytes from the same experiment, performed using a monoclonal syntaxin 1A antibody (IPsyx).

    Techniques Used: SDS Page, Labeling, Injection, Immunoprecipitation, Migration

    Kv1.1/Kvβ1.1 and SNAP-25, but not GIRK1/2, colocalize with syntaxin 1A in plasma-membrane patches of oocytes. Shown are representative confocal microscopic images of membrane-cortex patches from an oocyte coexpressing syntaxin 1A (SYX) with Kv1.1/Kvβ1.1 (Kv1.1,top row, A) or with GIRK1/2 (bottom row, B). Kv1.1 and GIRK1/2 proteins are shown in red, and syntaxin 1A is shown ingreen. The overlay image (second panelfrom right, A) of syntaxin with Kv1.1 depicts colocalization of the two proteins (shown inyellow). In contrast, no colocalization of syntaxin 1A and GIRK1/2 could be detected (second panel fromright, B). In control oocytes (c, right panels) no labeling could be detected. Scale bars, 10 μm.
    Figure Legend Snippet: Kv1.1/Kvβ1.1 and SNAP-25, but not GIRK1/2, colocalize with syntaxin 1A in plasma-membrane patches of oocytes. Shown are representative confocal microscopic images of membrane-cortex patches from an oocyte coexpressing syntaxin 1A (SYX) with Kv1.1/Kvβ1.1 (Kv1.1,top row, A) or with GIRK1/2 (bottom row, B). Kv1.1 and GIRK1/2 proteins are shown in red, and syntaxin 1A is shown ingreen. The overlay image (second panelfrom right, A) of syntaxin with Kv1.1 depicts colocalization of the two proteins (shown inyellow). In contrast, no colocalization of syntaxin 1A and GIRK1/2 could be detected (second panel fromright, B). In control oocytes (c, right panels) no labeling could be detected. Scale bars, 10 μm.

    Techniques Used: Labeling

    kv1 1 c terminus  (Alomone Labs)


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    Alomone Labs kv1 1 c terminus
    Kv1 1 C Terminus, supplied by Alomone Labs, 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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    Alomone Labs kv1 1 c terminus
    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or <t>Kv1.1</t> GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Kv1 1 C Terminus, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Alomone Labs polyclonal kv1 1 c terminus
    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or <t>Kv1.1</t> GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).
    Polyclonal Kv1 1 C Terminus, supplied by Alomone Labs, 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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    The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).

    Journal: The Journal of Neuroscience

    Article Title: K + Channel Facilitation of Exocytosis by Dynamic Interaction with Syntaxin

    doi: 10.1523/JNEUROSCI.4006-06.2007

    Figure Lengend Snippet: The Kv2.1-C1a peptide competes with Kv2.1 for association with syntaxin to inhibit facilitation of release by Kv2.1. a, Schematic illustration of the Kv2.1 protein. Dashed segments are domains that bind syntaxin and were used in this study. b, Immunoprecipitation (IP) from PC12 cells was performed with anti-Kv2.1 antibody in the absence (control) or presence of recombinant Kv2.1 or Kv1.1 GST-fusion peptides, or the antigen (Ag) peptide for the Kv2.1 antibody, as indicated above the lanes. The immunoprecipitated Kv2.1 and the coimmunoprecipitated syntaxin (Kv2.1 and co-IPed Syx) proteins were detected by antibodies (IB), as indicated on the left side of the blots of the top panel. Molecular weights are also marked on the left. Glutathione-Sepharose beads were added to the supernatant to pulldown syntaxin (Pulled down Syx). Precipitated proteins were immunoblotted with anti-syntaxin antibody (IB Syx) or stained with ponceau S, as indicated on the left side of the bottom panel. c, f, g, Release induced by depolarization with 70 mm extracellular KCl concentration was assessed from PC12 cells (as in Fig. 2) that were transfected with empty vector (control; n = 9; c), with Kv2.1-C1a peptide (C1a; n = 15; c), with Kv2.1 alone (Kv2.1; n = 7; f) or with Kv2.1 together with Kv2.1-C1a (Kv2.1 + C1a; n = 6; f). *p < 0.05. Normalized release at 10 min after the onset of KCl application is shown in the bar diagram (g). In all cells the molar concentration of total transfected DNA was adjusted to be equal by the empty vector. d, Averaged current density at +35 mV in cells expressing Kv2.1 + C1a (n = 9) compared with those of control and Kv2.1 cells (the latter taken from Fig. 2b). e, The normalized conductance–voltage relationship from cells expressing Kv2.1 + C1a is superimposed on that of Kv2.1 (the latter taken from Fig. 2c).

    Article Snippet: The primary antibodies used were anti-Kv1.1–C terminus and anti-Kv2.1–C terminus (Alomone Labs, Jerusalem, Israel), monoclonal anti-HPC-1 (Sigma-Aldrich, Rehovot, Israel), and anti-synapsin (Calbiochem, La Jolla, CA).

    Techniques: Immunoprecipitation, Recombinant, Staining, Concentration Assay, Transfection, Plasmid Preparation, Expressing