kcnq3  (Alomone Labs)


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    Alomone Labs kcnq3
    Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and <t>KCNQ2/KCNQ3</t> potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P
    Kcnq3, 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
    https://www.bioz.com/result/kcnq3/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    kcnq3 - by Bioz Stars, 2022-05
    93/100 stars

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    1) Product Images from "Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G"

    Article Title: Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200805169

    Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and KCNQ2/KCNQ3 potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P
    Figure Legend Snippet: Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and KCNQ2/KCNQ3 potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P

    Techniques Used: Construct, Cell Culture, Expressing, Mutagenesis, Transfection, Staining, Fluorescence, MANN-WHITNEY

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    Alomone Labs kcnq3
    Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and <t>KCNQ2/KCNQ3</t> potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P
    Kcnq3, 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
    https://www.bioz.com/result/kcnq3/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    kcnq3 - by Bioz Stars, 2022-05
    93/100 stars
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    Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and KCNQ2/KCNQ3 potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P

    Journal: The Journal of Cell Biology

    Article Title: Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G

    doi: 10.1083/jcb.200805169

    Figure Lengend Snippet: Impact of K v 2.1-Na v 1.2 and of phosphorylation-deficient K v 2.1-Na v 1.2 constructs on the accumulation of sodium channels (Na v 1) and KCNQ2/KCNQ3 potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K v 2.1-Na v 1.2 expression perturbed Na v 1 accumulation at the AIS, unlike the phosphorylation-deficient K v 2.1-Na v 1.2 4SA mutant. Hippocampal neurons were transfected with either K v 2.1-Na v 1.2 or phosphorylation-deficient K v 2.1-Na v 1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na v 1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K v 2.1-Na v 1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K v 2.1-Na v 1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P

    Article Snippet: Rabbit polyclonal antibodies included MAP2 (1:500; Millipore), ankyrin G (1:500–1,000; a gift from G. Alcaraz, Institut National de la Santé et de la Recherche Médicale, Unité Mixte de Recherche 641, Marseille, France), and KCNQ3 (1:800; Alomone Labs).

    Techniques: Construct, Cell Culture, Expressing, Mutagenesis, Transfection, Staining, Fluorescence, MANN-WHITNEY