kv1 1 Search Results


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Alomone Labs kv1
Kv1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Alomone Labs rabbit kcna1
Rabbit Kcna1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology anti kv11 1
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BPS Bioscience herg kv11 1 channels
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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: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Abbott Laboratories neutralization of the corresponding position in kv7.1
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).
Neutralization Of The Corresponding Position In Kv7.1, supplied by Abbott Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Trudeau Institute Inc kv11.1 channel
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).
Kv11.1 Channel, supplied by Trudeau Institute Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Photoswitch Biosciences channel-specific lumitoxins for kv1.1, kv1.2 and shaker
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).
Channel Specific Lumitoxins For Kv1.1, Kv1.2 And Shaker, supplied by Photoswitch Biosciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Issar Pharmaceuticals kv1.1 channels
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 Channels, supplied by Issar Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Upstate Biotechnology Inc antibody m α kv1.1
The source and dilutions of antibodies used in this study
Antibody M α Kv1.1, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Fukui Bank Ltd molecular expression of kv channels
The source and dilutions of antibodies used in this study
Molecular Expression Of Kv Channels, supplied by Fukui Bank Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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International Mouse Phenotyping Consortium knockout mice with kv7.3 and kv11.3
The source and dilutions of antibodies used in this study
Knockout Mice With Kv7.3 And Kv11.3, supplied by International Mouse Phenotyping Consortium, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


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

The source and dilutions of antibodies used in this study

Journal: The Journal of Neuroscience

Article Title: Genetic Dysmyelination Alters the Molecular Architecture of the Nodal Region

doi: 10.1523/JNEUROSCI.22-05-01726.2002

Figure Lengend Snippet: The source and dilutions of antibodies used in this study

Article Snippet: M α Kv1.1 , 1:50 , Upstate Biotechnology, Lake Placid, NY.

Techniques: