anti na v 1 3  (Alomone Labs)


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    Alomone Labs anti na v 1 3
    Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.
    Anti Na V 1 3, 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/anti na v 1 3/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti na v 1 3 - by Bioz Stars, 2023-09
    93/100 stars

    Images

    1) Product Images from "Pharmacological Dissection of the Crosstalk between Na V and Ca V Channels in GH3b6 Cells"

    Article Title: Pharmacological Dissection of the Crosstalk between Na V and Ca V Channels in GH3b6 Cells

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms23020827

    Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.
    Figure Legend Snippet: Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.

    Techniques Used: Expressing, Quantitative RT-PCR, Western Blot, SDS Page, Fluorescence, Labeling, Staining

    Effects of ICA-121431, a selective inhibitor of Na V 1.3 channels, on I Na recorded in GH3b6 cells by manual patch-clamp. ( A , B ) To illustrate the effects of ICA-121431, examples of superimposed I Na elicited by 500 ms depolarizing pulses (at −20, 0, and +20 mV) and examples of superimposed I Na elicited by depolarizing pulse at 0 mV immediately after a 500 ms prepulse (−120, −60, and −50 mV) are shown. The control traces are in blue (CTRL) and red traces correspond to I Na after ICA-121431 application (1 µM). ( B ) Current–voltage relationships and ( C ) activation/inactivation curves of I Na recorded before (blue circles) and after 1 µM ICA-121431 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.
    Figure Legend Snippet: Effects of ICA-121431, a selective inhibitor of Na V 1.3 channels, on I Na recorded in GH3b6 cells by manual patch-clamp. ( A , B ) To illustrate the effects of ICA-121431, examples of superimposed I Na elicited by 500 ms depolarizing pulses (at −20, 0, and +20 mV) and examples of superimposed I Na elicited by depolarizing pulse at 0 mV immediately after a 500 ms prepulse (−120, −60, and −50 mV) are shown. The control traces are in blue (CTRL) and red traces correspond to I Na after ICA-121431 application (1 µM). ( B ) Current–voltage relationships and ( C ) activation/inactivation curves of I Na recorded before (blue circles) and after 1 µM ICA-121431 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.

    Techniques Used: Patch Clamp, Activation Assay, Two Tailed Test

    Effects of Tf2, a selective β-scorpion toxin of Na V 1.3 channels, on I Na recorded in GH3b6 cells by automated patch-clamp. ( A ) Representative examples of I Na elicited by 50 ms depolarization steps (protocol inset), in the absence and presence of 1 nM Tf2. To illustrate the strong effect of 1 nM Tf2, superimposed I Na traces at −45 mV are shown. ( B ) Current–voltage relationships ( C ) and activation/inactivation curves of I Na recorded before (blue circles) and after 1 nM Tf2 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.
    Figure Legend Snippet: Effects of Tf2, a selective β-scorpion toxin of Na V 1.3 channels, on I Na recorded in GH3b6 cells by automated patch-clamp. ( A ) Representative examples of I Na elicited by 50 ms depolarization steps (protocol inset), in the absence and presence of 1 nM Tf2. To illustrate the strong effect of 1 nM Tf2, superimposed I Na traces at −45 mV are shown. ( B ) Current–voltage relationships ( C ) and activation/inactivation curves of I Na recorded before (blue circles) and after 1 nM Tf2 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.

    Techniques Used: Patch Clamp, Activation Assay, Two Tailed Test

    Effect of Tf2, a selective β-scorpion toxin of Na V 1.3, on the intracellular Ca 2+ level in GH3b6 cells. ( A ) Representative kinetics of Fura-2 fluorescence emission in GH3b6 cells treated with increasing concentrations of Tf2. ( B ) The Ca 2+ responses induced by Tf2 are concentration dependent. The concentration–response relationships were analyzed using the Hill–Langmuir equation with variable slope. The values of EC 50 and the Hill coefficient were 17.51 ± 1.4 nM and 1.378 (R 2 = 0.99). ( C ) TTX inhibits in a concentration-dependent manner the Ca 2+ responses elicited by 0.5 µM of Tf2 with an IC 50 value of 7.9 ± 2.1 nM and a Hill coefficient of 1.31 ± 0.135, R 2 = 0.94. The data represent the mean ± SEM ( n = 3 wells) and are representative of at least two independent experiments.
    Figure Legend Snippet: Effect of Tf2, a selective β-scorpion toxin of Na V 1.3, on the intracellular Ca 2+ level in GH3b6 cells. ( A ) Representative kinetics of Fura-2 fluorescence emission in GH3b6 cells treated with increasing concentrations of Tf2. ( B ) The Ca 2+ responses induced by Tf2 are concentration dependent. The concentration–response relationships were analyzed using the Hill–Langmuir equation with variable slope. The values of EC 50 and the Hill coefficient were 17.51 ± 1.4 nM and 1.378 (R 2 = 0.99). ( C ) TTX inhibits in a concentration-dependent manner the Ca 2+ responses elicited by 0.5 µM of Tf2 with an IC 50 value of 7.9 ± 2.1 nM and a Hill coefficient of 1.31 ± 0.135, R 2 = 0.94. The data represent the mean ± SEM ( n = 3 wells) and are representative of at least two independent experiments.

    Techniques Used: Fluorescence, Concentration Assay

    anti na v 1 3 rabbit polyclonal  (Alomone Labs)


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    Alomone Labs anti na v 1 3 rabbit polyclonal
    The Na v 1.3/1.1 selective blocker ICA-121431, but not the Na v 1.2/1.6 Na + channel blocker S-Lic reverses enhanced dendritic excitability. ( A and E ) Representative examples of the effects of the Na v 1.2/1.6 Na + channel blocker S-Lic (300 µM) on dendritic spikes ( insets show magnification of the fast phase of the dendritic spike), and on the first derivation of the voltage trace (d V /d t ) in sham-control ( A ) and epileptic ( E ) animals. ( B and F ) Effects of S-Lic on the maximal rate of rise of the dendritic spike in sham-control ( B ) and epileptic mice ( F ). ( C and G ) Representative examples of effects on the dendritic spike threshold in sham-control and epileptic mice (arrows indicate occurrence of dendritic spikes and dashed lines indicate thresholds). ( D and H ) Quantification showing the lack of significant effects on the dendritic spike threshold in sham-control ( D ) and epileptic mice ( H ) with S-Lic application. Two-way ANOVA revealed no significant effects of S-Lic on the rate of rise or threshold of dendritic spikes in control ( B and D ) and epileptic ( F and H ) animals. ( I – K ) Effects of S-Lic on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of S-Lic (violet, I ). Effects of S-Lic on firing induced by current injection at which firing frequency was maximal under ACSF conditions, control and epileptic animals ( I and K, respectively). Asterisks indicate Bonferroni’s post-test P = 0.0034. ( L – S ) Effects of the Na v 1.3/1.1 Na + channel blocker ICA-121431 (100 nM) in sham-control ( L – O ) and epileptic animals ( P – S ), depicted in the same manner as in panels ( A – H ). Asterisks indicate Bonferroni’s post-test, P = 0.023 ( Q ) and P = 0.0050 ( S ). ( T – V ) Lack of effects of ICA-121431 on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of ICA-121431 (blue, T ). Lack of effects of ICA-121431 on the maximal firing frequency of CA1 neurons ( U and V ).
    Anti Na V 1 3 Rabbit Polyclonal, 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
    https://www.bioz.com/result/anti na v 1 3 rabbit polyclonal/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti na v 1 3 rabbit polyclonal - by Bioz Stars, 2023-09
    86/100 stars

    Images

    1) Product Images from "Targeting aberrant dendritic integration to treat cognitive comorbidities of epilepsy"

    Article Title: Targeting aberrant dendritic integration to treat cognitive comorbidities of epilepsy

    Journal: Brain

    doi: 10.1093/brain/awac455

    The Na v 1.3/1.1 selective blocker ICA-121431, but not the Na v 1.2/1.6 Na + channel blocker S-Lic reverses enhanced dendritic excitability. ( A and E ) Representative examples of the effects of the Na v 1.2/1.6 Na + channel blocker S-Lic (300 µM) on dendritic spikes ( insets show magnification of the fast phase of the dendritic spike), and on the first derivation of the voltage trace (d V /d t ) in sham-control ( A ) and epileptic ( E ) animals. ( B and F ) Effects of S-Lic on the maximal rate of rise of the dendritic spike in sham-control ( B ) and epileptic mice ( F ). ( C and G ) Representative examples of effects on the dendritic spike threshold in sham-control and epileptic mice (arrows indicate occurrence of dendritic spikes and dashed lines indicate thresholds). ( D and H ) Quantification showing the lack of significant effects on the dendritic spike threshold in sham-control ( D ) and epileptic mice ( H ) with S-Lic application. Two-way ANOVA revealed no significant effects of S-Lic on the rate of rise or threshold of dendritic spikes in control ( B and D ) and epileptic ( F and H ) animals. ( I – K ) Effects of S-Lic on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of S-Lic (violet, I ). Effects of S-Lic on firing induced by current injection at which firing frequency was maximal under ACSF conditions, control and epileptic animals ( I and K, respectively). Asterisks indicate Bonferroni’s post-test P = 0.0034. ( L – S ) Effects of the Na v 1.3/1.1 Na + channel blocker ICA-121431 (100 nM) in sham-control ( L – O ) and epileptic animals ( P – S ), depicted in the same manner as in panels ( A – H ). Asterisks indicate Bonferroni’s post-test, P = 0.023 ( Q ) and P = 0.0050 ( S ). ( T – V ) Lack of effects of ICA-121431 on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of ICA-121431 (blue, T ). Lack of effects of ICA-121431 on the maximal firing frequency of CA1 neurons ( U and V ).
    Figure Legend Snippet: The Na v 1.3/1.1 selective blocker ICA-121431, but not the Na v 1.2/1.6 Na + channel blocker S-Lic reverses enhanced dendritic excitability. ( A and E ) Representative examples of the effects of the Na v 1.2/1.6 Na + channel blocker S-Lic (300 µM) on dendritic spikes ( insets show magnification of the fast phase of the dendritic spike), and on the first derivation of the voltage trace (d V /d t ) in sham-control ( A ) and epileptic ( E ) animals. ( B and F ) Effects of S-Lic on the maximal rate of rise of the dendritic spike in sham-control ( B ) and epileptic mice ( F ). ( C and G ) Representative examples of effects on the dendritic spike threshold in sham-control and epileptic mice (arrows indicate occurrence of dendritic spikes and dashed lines indicate thresholds). ( D and H ) Quantification showing the lack of significant effects on the dendritic spike threshold in sham-control ( D ) and epileptic mice ( H ) with S-Lic application. Two-way ANOVA revealed no significant effects of S-Lic on the rate of rise or threshold of dendritic spikes in control ( B and D ) and epileptic ( F and H ) animals. ( I – K ) Effects of S-Lic on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of S-Lic (violet, I ). Effects of S-Lic on firing induced by current injection at which firing frequency was maximal under ACSF conditions, control and epileptic animals ( I and K, respectively). Asterisks indicate Bonferroni’s post-test P = 0.0034. ( L – S ) Effects of the Na v 1.3/1.1 Na + channel blocker ICA-121431 (100 nM) in sham-control ( L – O ) and epileptic animals ( P – S ), depicted in the same manner as in panels ( A – H ). Asterisks indicate Bonferroni’s post-test, P = 0.023 ( Q ) and P = 0.0050 ( S ). ( T – V ) Lack of effects of ICA-121431 on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of ICA-121431 (blue, T ). Lack of effects of ICA-121431 on the maximal firing frequency of CA1 neurons ( U and V ).

    Techniques Used: Injection

    Scn3a expression is increased at the mRNA and protein level in the hippocampal CA1 region of epileptic mice . ( A – D ) Multiplex fluorescent mRNA in-situ hybridization for Scn3a in hippocampal CA1 region. ( A and B ) Representative fluorescent images showing labelling of nuclei with DAPI (blue), labelling of GABAergic neurons (GAD) with a probe for Gad1/2 mRNA (green) and of Scn3a mRNA (red) in hippocampal slices from sham-control and epileptic animals, scale bar 500 µm. Close up ( right ) of the boxed areas, scale bar = 100 µm. ( C ) Cumulative distribution of Scn3a punctae per nucleus colocalized excitatory pyramidal cells (excluding GAD-labelled putative interneurons). The amount of punctae was significantly higher in epileptic animals (2979 cells in six animals and 3669 cells in five animals, for sham-control and epileptic mice, respectively; asterisks indicate Kolmogorov–Smirnov two-tailed test P < 0.0001). ( D ) Cumulative distribution of Scn3a punctae per nucleus colocalized in GAD+ interneurons. The amount of punctae was significantly lower in epileptic animals (253 cells in five animals and 141 cells in five animals, for sham-control and epileptic mice, respectively; asterisks indicate Kolmogorov–Smirnov two-tailed test P < 0.001). ( E – H ) Western blots for Na v 1.3 and Na v 1.2 in hippocampal CA1 region. ( E ) Representative Western blots of Na v 1.3 (indicated with arrrowhead) and the housekeeping protein GAPDH, used as loading control in sham-control and epileptic mice. ( F ) Quantitative analysis of the Na v 1.2 protein obtained by band intensity analysis from E (normalized Na v 1.2/GAPDH ratio of 1.0 ± 0.36 in sham-control n = 4 and 3.64 ± 0.85 in epileptic mice n = 4; unpaired Student’s t -test P = 0.029; data represent mean ± SEM). ( G ) Representative Western blots of Na v 1.2 (indicated with arrrowhead) and the housekeeping protein GAPDH, used as loading control in sham-control and epileptic mice. ( H ) Quantitative analysis of the Na v 1.2 protein obtained by band intensity analysis from G (normalized Na v 1.2/GAPDH ratio of 1.0 ± 0.05 in sham-control n = 3 and 0.93 ± 0.052 in epileptic mice n = 3; unpaired Student’s t -test P = 0.38).
    Figure Legend Snippet: Scn3a expression is increased at the mRNA and protein level in the hippocampal CA1 region of epileptic mice . ( A – D ) Multiplex fluorescent mRNA in-situ hybridization for Scn3a in hippocampal CA1 region. ( A and B ) Representative fluorescent images showing labelling of nuclei with DAPI (blue), labelling of GABAergic neurons (GAD) with a probe for Gad1/2 mRNA (green) and of Scn3a mRNA (red) in hippocampal slices from sham-control and epileptic animals, scale bar 500 µm. Close up ( right ) of the boxed areas, scale bar = 100 µm. ( C ) Cumulative distribution of Scn3a punctae per nucleus colocalized excitatory pyramidal cells (excluding GAD-labelled putative interneurons). The amount of punctae was significantly higher in epileptic animals (2979 cells in six animals and 3669 cells in five animals, for sham-control and epileptic mice, respectively; asterisks indicate Kolmogorov–Smirnov two-tailed test P < 0.0001). ( D ) Cumulative distribution of Scn3a punctae per nucleus colocalized in GAD+ interneurons. The amount of punctae was significantly lower in epileptic animals (253 cells in five animals and 141 cells in five animals, for sham-control and epileptic mice, respectively; asterisks indicate Kolmogorov–Smirnov two-tailed test P < 0.001). ( E – H ) Western blots for Na v 1.3 and Na v 1.2 in hippocampal CA1 region. ( E ) Representative Western blots of Na v 1.3 (indicated with arrrowhead) and the housekeeping protein GAPDH, used as loading control in sham-control and epileptic mice. ( F ) Quantitative analysis of the Na v 1.2 protein obtained by band intensity analysis from E (normalized Na v 1.2/GAPDH ratio of 1.0 ± 0.36 in sham-control n = 4 and 3.64 ± 0.85 in epileptic mice n = 4; unpaired Student’s t -test P = 0.029; data represent mean ± SEM). ( G ) Representative Western blots of Na v 1.2 (indicated with arrrowhead) and the housekeeping protein GAPDH, used as loading control in sham-control and epileptic mice. ( H ) Quantitative analysis of the Na v 1.2 protein obtained by band intensity analysis from G (normalized Na v 1.2/GAPDH ratio of 1.0 ± 0.05 in sham-control n = 3 and 0.93 ± 0.052 in epileptic mice n = 3; unpaired Student’s t -test P = 0.38).

    Techniques Used: Expressing, Multiplex Assay, In Situ Hybridization, Two Tailed Test, Western Blot

    na v 1 3  (Alomone Labs)


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    Alomone Labs na v 1 3
    Na V 1 3, 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
    https://www.bioz.com/result/na v 1 3/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    na v 1 3 - by Bioz Stars, 2023-09
    86/100 stars

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    anti na v 1 3  (Alomone Labs)


    Bioz Verified Symbol Alomone Labs is a verified supplier
    Bioz Manufacturer Symbol Alomone Labs manufactures this product  
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    Structured Review

    Alomone Labs anti na v 1 3
    Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.
    Anti Na V 1 3, 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/anti na v 1 3/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti na v 1 3 - by Bioz Stars, 2023-09
    93/100 stars

    Images

    1) Product Images from "Pharmacological Dissection of the Crosstalk between Na V and Ca V Channels in GH3b6 Cells"

    Article Title: Pharmacological Dissection of the Crosstalk between Na V and Ca V Channels in GH3b6 Cells

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms23020827

    Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.
    Figure Legend Snippet: Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.

    Techniques Used: Expressing, Quantitative RT-PCR, Western Blot, SDS Page, Fluorescence, Labeling, Staining

    Effects of ICA-121431, a selective inhibitor of Na V 1.3 channels, on I Na recorded in GH3b6 cells by manual patch-clamp. ( A , B ) To illustrate the effects of ICA-121431, examples of superimposed I Na elicited by 500 ms depolarizing pulses (at −20, 0, and +20 mV) and examples of superimposed I Na elicited by depolarizing pulse at 0 mV immediately after a 500 ms prepulse (−120, −60, and −50 mV) are shown. The control traces are in blue (CTRL) and red traces correspond to I Na after ICA-121431 application (1 µM). ( B ) Current–voltage relationships and ( C ) activation/inactivation curves of I Na recorded before (blue circles) and after 1 µM ICA-121431 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.
    Figure Legend Snippet: Effects of ICA-121431, a selective inhibitor of Na V 1.3 channels, on I Na recorded in GH3b6 cells by manual patch-clamp. ( A , B ) To illustrate the effects of ICA-121431, examples of superimposed I Na elicited by 500 ms depolarizing pulses (at −20, 0, and +20 mV) and examples of superimposed I Na elicited by depolarizing pulse at 0 mV immediately after a 500 ms prepulse (−120, −60, and −50 mV) are shown. The control traces are in blue (CTRL) and red traces correspond to I Na after ICA-121431 application (1 µM). ( B ) Current–voltage relationships and ( C ) activation/inactivation curves of I Na recorded before (blue circles) and after 1 µM ICA-121431 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.

    Techniques Used: Patch Clamp, Activation Assay, Two Tailed Test

    Effects of Tf2, a selective β-scorpion toxin of Na V 1.3 channels, on I Na recorded in GH3b6 cells by automated patch-clamp. ( A ) Representative examples of I Na elicited by 50 ms depolarization steps (protocol inset), in the absence and presence of 1 nM Tf2. To illustrate the strong effect of 1 nM Tf2, superimposed I Na traces at −45 mV are shown. ( B ) Current–voltage relationships ( C ) and activation/inactivation curves of I Na recorded before (blue circles) and after 1 nM Tf2 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.
    Figure Legend Snippet: Effects of Tf2, a selective β-scorpion toxin of Na V 1.3 channels, on I Na recorded in GH3b6 cells by automated patch-clamp. ( A ) Representative examples of I Na elicited by 50 ms depolarization steps (protocol inset), in the absence and presence of 1 nM Tf2. To illustrate the strong effect of 1 nM Tf2, superimposed I Na traces at −45 mV are shown. ( B ) Current–voltage relationships ( C ) and activation/inactivation curves of I Na recorded before (blue circles) and after 1 nM Tf2 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.

    Techniques Used: Patch Clamp, Activation Assay, Two Tailed Test

    Effect of Tf2, a selective β-scorpion toxin of Na V 1.3, on the intracellular Ca 2+ level in GH3b6 cells. ( A ) Representative kinetics of Fura-2 fluorescence emission in GH3b6 cells treated with increasing concentrations of Tf2. ( B ) The Ca 2+ responses induced by Tf2 are concentration dependent. The concentration–response relationships were analyzed using the Hill–Langmuir equation with variable slope. The values of EC 50 and the Hill coefficient were 17.51 ± 1.4 nM and 1.378 (R 2 = 0.99). ( C ) TTX inhibits in a concentration-dependent manner the Ca 2+ responses elicited by 0.5 µM of Tf2 with an IC 50 value of 7.9 ± 2.1 nM and a Hill coefficient of 1.31 ± 0.135, R 2 = 0.94. The data represent the mean ± SEM ( n = 3 wells) and are representative of at least two independent experiments.
    Figure Legend Snippet: Effect of Tf2, a selective β-scorpion toxin of Na V 1.3, on the intracellular Ca 2+ level in GH3b6 cells. ( A ) Representative kinetics of Fura-2 fluorescence emission in GH3b6 cells treated with increasing concentrations of Tf2. ( B ) The Ca 2+ responses induced by Tf2 are concentration dependent. The concentration–response relationships were analyzed using the Hill–Langmuir equation with variable slope. The values of EC 50 and the Hill coefficient were 17.51 ± 1.4 nM and 1.378 (R 2 = 0.99). ( C ) TTX inhibits in a concentration-dependent manner the Ca 2+ responses elicited by 0.5 µM of Tf2 with an IC 50 value of 7.9 ± 2.1 nM and a Hill coefficient of 1.31 ± 0.135, R 2 = 0.94. The data represent the mean ± SEM ( n = 3 wells) and are representative of at least two independent experiments.

    Techniques Used: Fluorescence, Concentration Assay

    na v 1 3  (Alomone Labs)


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    Alomone Labs na v 1 3
    Na V 1 3, 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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    na v 1 3  (Alomone Labs)


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    Alomone Labs na v 1 3
    Interaction of myh9 and myh10 with Na v 1.3 subunits expressed in the postnatal day 3 (P3) rat brain tissues. P3 rat brain tissue lysates (In, lane 1) were PC with mouse IgG2b isotypes (PC, lane 2) prior to IP using mouse anti-myh9 (IP, lane 3) and mouse anti-myh10 (IP, lane 4) antibodies of the IgG2b isotypes. Loading of mIgG2b (PC) complexes in the gel preceded those of the IP complexes. Myh9 and myh10 coimmunoprecipitated Na v 1.3 subunits (i) expressed in P3 rat brain tissues. Myh9 and myh10 also coimmunoprecipitated β-actin (ii) and MRLCs (iii) expressed in P3 rat brain tissues. The MRLC immunoreactive signal from the rat tissue lysates is barely detectable and is indicated with an asterisk (*). The denatured mouse IgG-LC (iii) separated from their intact immunoglobulins (i.e., used for PC or IP) could be seen in the immunoblot, as this section of the blot is probed with mouse anti-MRLC antibodies. IgG-LC: immunoglobulin light chain; In: lysate input; IP: immunoprecipitation; mIgG2b: mouse immunoglobulin isotype 2b; MRLC: myosin regulatory light chain; myh: myosin heavy chain; Na v : voltage-sensitive sodium channel; PC: precleared.
    Na V 1 3, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Nonmuscle myosin II isoforms interact with sodium channel alpha subunits"

    Article Title: Nonmuscle myosin II isoforms interact with sodium channel alpha subunits

    Journal: Molecular Pain

    doi: 10.1177/1744806918788638

    Interaction of myh9 and myh10 with Na v 1.3 subunits expressed in the postnatal day 3 (P3) rat brain tissues. P3 rat brain tissue lysates (In, lane 1) were PC with mouse IgG2b isotypes (PC, lane 2) prior to IP using mouse anti-myh9 (IP, lane 3) and mouse anti-myh10 (IP, lane 4) antibodies of the IgG2b isotypes. Loading of mIgG2b (PC) complexes in the gel preceded those of the IP complexes. Myh9 and myh10 coimmunoprecipitated Na v 1.3 subunits (i) expressed in P3 rat brain tissues. Myh9 and myh10 also coimmunoprecipitated β-actin (ii) and MRLCs (iii) expressed in P3 rat brain tissues. The MRLC immunoreactive signal from the rat tissue lysates is barely detectable and is indicated with an asterisk (*). The denatured mouse IgG-LC (iii) separated from their intact immunoglobulins (i.e., used for PC or IP) could be seen in the immunoblot, as this section of the blot is probed with mouse anti-MRLC antibodies. IgG-LC: immunoglobulin light chain; In: lysate input; IP: immunoprecipitation; mIgG2b: mouse immunoglobulin isotype 2b; MRLC: myosin regulatory light chain; myh: myosin heavy chain; Na v : voltage-sensitive sodium channel; PC: precleared.
    Figure Legend Snippet: Interaction of myh9 and myh10 with Na v 1.3 subunits expressed in the postnatal day 3 (P3) rat brain tissues. P3 rat brain tissue lysates (In, lane 1) were PC with mouse IgG2b isotypes (PC, lane 2) prior to IP using mouse anti-myh9 (IP, lane 3) and mouse anti-myh10 (IP, lane 4) antibodies of the IgG2b isotypes. Loading of mIgG2b (PC) complexes in the gel preceded those of the IP complexes. Myh9 and myh10 coimmunoprecipitated Na v 1.3 subunits (i) expressed in P3 rat brain tissues. Myh9 and myh10 also coimmunoprecipitated β-actin (ii) and MRLCs (iii) expressed in P3 rat brain tissues. The MRLC immunoreactive signal from the rat tissue lysates is barely detectable and is indicated with an asterisk (*). The denatured mouse IgG-LC (iii) separated from their intact immunoglobulins (i.e., used for PC or IP) could be seen in the immunoblot, as this section of the blot is probed with mouse anti-MRLC antibodies. IgG-LC: immunoglobulin light chain; In: lysate input; IP: immunoprecipitation; mIgG2b: mouse immunoglobulin isotype 2b; MRLC: myosin regulatory light chain; myh: myosin heavy chain; Na v : voltage-sensitive sodium channel; PC: precleared.

    Techniques Used: Western Blot, Immunoprecipitation

    na v 1 3  (Alomone Labs)


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    Alomone Labs na v 1 3
    Quantitative RT-PCR of different Na v isoforms in main olfactory epithelium (MOE) and vomeronasal organ (VNO). Comparison of Na v channel mRNA frequency in the (A) MOE and (B) VNO using quantitative RT-PCR. Na v 1.7 is the most abundant isoform in both subsystems and displays on average at least 5-fold higher copy numbers than other Na v isoforms. The column diagrams show mean copy numbers ± SD from two to four independent experiments, each carried out as triplicates using total RNA of adult C57/B6 mice ( Y -axis). Na v channel isoforms ( X -axis). (A) Copy numbers per ng total RNA in the MOE for Na v 1.1 (2.6 ± 0.72), Na v 1.2 (4.99 ± 0.62), Na v 1.3 (51.80 ± 7.75), Na v 1.5 (113.17 ± 27.35), Na v 1.6 (41.19 ± 10.65), Na v 1.7 (983.44 ± 221.34). (B) Copy numbers per ng total RNA in the VNO for Na v 1.1 (0.80 ± 0.42), Na v 1.2 (10.16 ± 2.10), Na v 1.3 (142.70 ± 29.05), Na v 1.5 (128.13 ± 25.56), Na v 1.6 (38.17 ± 5.39), Na v 1.7 (701.06 ± 203.50).
    Na V 1 3, 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 "Organization and Plasticity of Sodium Channel Expression in the Mouse Olfactory and Vomeronasal Epithelia"

    Article Title: Organization and Plasticity of Sodium Channel Expression in the Mouse Olfactory and Vomeronasal Epithelia

    Journal: Frontiers in Neuroanatomy

    doi: 10.3389/fnana.2017.00028

    Quantitative RT-PCR of different Na v isoforms in main olfactory epithelium (MOE) and vomeronasal organ (VNO). Comparison of Na v channel mRNA frequency in the (A) MOE and (B) VNO using quantitative RT-PCR. Na v 1.7 is the most abundant isoform in both subsystems and displays on average at least 5-fold higher copy numbers than other Na v isoforms. The column diagrams show mean copy numbers ± SD from two to four independent experiments, each carried out as triplicates using total RNA of adult C57/B6 mice ( Y -axis). Na v channel isoforms ( X -axis). (A) Copy numbers per ng total RNA in the MOE for Na v 1.1 (2.6 ± 0.72), Na v 1.2 (4.99 ± 0.62), Na v 1.3 (51.80 ± 7.75), Na v 1.5 (113.17 ± 27.35), Na v 1.6 (41.19 ± 10.65), Na v 1.7 (983.44 ± 221.34). (B) Copy numbers per ng total RNA in the VNO for Na v 1.1 (0.80 ± 0.42), Na v 1.2 (10.16 ± 2.10), Na v 1.3 (142.70 ± 29.05), Na v 1.5 (128.13 ± 25.56), Na v 1.6 (38.17 ± 5.39), Na v 1.7 (701.06 ± 203.50).
    Figure Legend Snippet: Quantitative RT-PCR of different Na v isoforms in main olfactory epithelium (MOE) and vomeronasal organ (VNO). Comparison of Na v channel mRNA frequency in the (A) MOE and (B) VNO using quantitative RT-PCR. Na v 1.7 is the most abundant isoform in both subsystems and displays on average at least 5-fold higher copy numbers than other Na v isoforms. The column diagrams show mean copy numbers ± SD from two to four independent experiments, each carried out as triplicates using total RNA of adult C57/B6 mice ( Y -axis). Na v channel isoforms ( X -axis). (A) Copy numbers per ng total RNA in the MOE for Na v 1.1 (2.6 ± 0.72), Na v 1.2 (4.99 ± 0.62), Na v 1.3 (51.80 ± 7.75), Na v 1.5 (113.17 ± 27.35), Na v 1.6 (41.19 ± 10.65), Na v 1.7 (983.44 ± 221.34). (B) Copy numbers per ng total RNA in the VNO for Na v 1.1 (0.80 ± 0.42), Na v 1.2 (10.16 ± 2.10), Na v 1.3 (142.70 ± 29.05), Na v 1.5 (128.13 ± 25.56), Na v 1.6 (38.17 ± 5.39), Na v 1.7 (701.06 ± 203.50).

    Techniques Used: Quantitative RT-PCR

    Analysis of Na v channel expression in MOE of adult mice. Confocal images showing immunoreactivity (red) for (A) Na v 1.2, (B) Na v 1.3, (C) Na v 1.6, and (D) Na v 1.7. We used coronal MOE cryosections (12 μm) of adult OMP-GFP mice (left, overviews; right, magnifications). Endogenous GFP (green) is located to mature, OMP + OSNs as shown in the magnifications at the right. (A) Na v 1.2 staining is restricted to microvillar cells (arrowheads) but absent from OSNs or axon bundles (dotted circles) identified by OMP-GFP labeling. (B) Robust Na v 1.3 staining is present in axon bundles (arrows, left) that colocalize with OMP-GFP (dotted circles, right). (C) Na v 1.6 labeling of the MOE surface (left, arrow heads) corresponds to sustentacular cells (right). OSNs and axon bundles (dotted line) lack Na v 1.6 staining. (D) Na v 1.7 immunoreactivity is profound in axon bundles, and occasionally found in microvillar cells (asterisk). (E,F,H,I) Blocking peptide control experiments lack immunoreactivity. (G) Na v 1.3 immunoreactivity is present in cNa v 1.7 −/− mice. (J) Na v 1.7 immunoreactivity is absent in cNa v 1.7 −/− mice. Images for each Na v channel immunostaining are representatives of n ≥ 3 mice and n = 20 sections per mouse. Scale bars overviews 100 μm, and magnifications 20 μm.
    Figure Legend Snippet: Analysis of Na v channel expression in MOE of adult mice. Confocal images showing immunoreactivity (red) for (A) Na v 1.2, (B) Na v 1.3, (C) Na v 1.6, and (D) Na v 1.7. We used coronal MOE cryosections (12 μm) of adult OMP-GFP mice (left, overviews; right, magnifications). Endogenous GFP (green) is located to mature, OMP + OSNs as shown in the magnifications at the right. (A) Na v 1.2 staining is restricted to microvillar cells (arrowheads) but absent from OSNs or axon bundles (dotted circles) identified by OMP-GFP labeling. (B) Robust Na v 1.3 staining is present in axon bundles (arrows, left) that colocalize with OMP-GFP (dotted circles, right). (C) Na v 1.6 labeling of the MOE surface (left, arrow heads) corresponds to sustentacular cells (right). OSNs and axon bundles (dotted line) lack Na v 1.6 staining. (D) Na v 1.7 immunoreactivity is profound in axon bundles, and occasionally found in microvillar cells (asterisk). (E,F,H,I) Blocking peptide control experiments lack immunoreactivity. (G) Na v 1.3 immunoreactivity is present in cNa v 1.7 −/− mice. (J) Na v 1.7 immunoreactivity is absent in cNa v 1.7 −/− mice. Images for each Na v channel immunostaining are representatives of n ≥ 3 mice and n = 20 sections per mouse. Scale bars overviews 100 μm, and magnifications 20 μm.

    Techniques Used: Expressing, Staining, Labeling, Blocking Assay, Immunostaining

    Analysis of Na v channel expression in VNO of adult and early postnatal mice. (A–H) Confocal images showing immunoreactivity (red) observed for (A) Na v 1.2, (B) Na v 1.3, (C) Na v 1.6, and (D) Na v 1.7 in 12 μm coronal VNO cryosections of adult mice (left, overviews; right, magnifications). (A) Na v 1.2 staining is present in VSN knobs (arrowheads), dendrites and somata of basal (b) VSNs but absent in apical (a) VSNs (overview left). The magnification at the right shows colocalization of Na v 1.2 with V2R2 (green). (B) Na v 1.3 staining is moderate in VSN knobs (arrowheads), dendrites and somata and robust in axon bundles as identified in OMP-GFP mice (green signal). (C) Na v 1.6 is strong in knobs (arrowheads) and somata (bracket). The magnification and colocalization with OMP-GFP shows a decline in Na v 1.6 intensity from basal to apical. (D) Na v 1.7 staining is prominent in VSN knobs (arrowheads) and axon bundles (arrows). Peptide control experiments (E,F,G) lack immunoreactivity. (H) Na v 1.7 staining (top) is absent in axon bundles (arrows) of cNa v 1.7 −/− mice, visualized by OMP staining (bottom). (I-L) Immunoreactivity (red) for (I) Na v 1.2, (J) Na v 1.3, (K) Na v 1.6, and (L) Na v 1.7 at postnatal (P) day 2, P7, and P14. (I) Onset of Na v 1.2 in P2 VSNs (asterisks). At P7 and P14, basal (b) confinement of Na v 1.2 somata and labeled knobs (arrowheads; a). (J) Na v 1.3 is visible in single somata (asterisks) and axon bundles (arrows) at P7, and shows diffuse staining of the apical VNO (arrowheads) starting at P2. (K) Onset of Na v 1.6 in somata (asterisks) at P2 with increasing numbers at P7 and P14 throughout the VNO (brackets). (L) Na v 1.7 in single VSN somata (asterisks) and axon bundles (arrows) starts at P2. The knob area is substantially stained from P7 onwards. Images are representatives of n ≥ 3 adult mice ( n = 20 sections per mouse) and n = 2 juvenile mice each at P2, P7, and P14 ( n ≥ 10 sections per mouse). Scale bars overviews ( A–H , left) and (E–H) 100 μm; magnifications (A–D) and (I–L) 20 μm.
    Figure Legend Snippet: Analysis of Na v channel expression in VNO of adult and early postnatal mice. (A–H) Confocal images showing immunoreactivity (red) observed for (A) Na v 1.2, (B) Na v 1.3, (C) Na v 1.6, and (D) Na v 1.7 in 12 μm coronal VNO cryosections of adult mice (left, overviews; right, magnifications). (A) Na v 1.2 staining is present in VSN knobs (arrowheads), dendrites and somata of basal (b) VSNs but absent in apical (a) VSNs (overview left). The magnification at the right shows colocalization of Na v 1.2 with V2R2 (green). (B) Na v 1.3 staining is moderate in VSN knobs (arrowheads), dendrites and somata and robust in axon bundles as identified in OMP-GFP mice (green signal). (C) Na v 1.6 is strong in knobs (arrowheads) and somata (bracket). The magnification and colocalization with OMP-GFP shows a decline in Na v 1.6 intensity from basal to apical. (D) Na v 1.7 staining is prominent in VSN knobs (arrowheads) and axon bundles (arrows). Peptide control experiments (E,F,G) lack immunoreactivity. (H) Na v 1.7 staining (top) is absent in axon bundles (arrows) of cNa v 1.7 −/− mice, visualized by OMP staining (bottom). (I-L) Immunoreactivity (red) for (I) Na v 1.2, (J) Na v 1.3, (K) Na v 1.6, and (L) Na v 1.7 at postnatal (P) day 2, P7, and P14. (I) Onset of Na v 1.2 in P2 VSNs (asterisks). At P7 and P14, basal (b) confinement of Na v 1.2 somata and labeled knobs (arrowheads; a). (J) Na v 1.3 is visible in single somata (asterisks) and axon bundles (arrows) at P7, and shows diffuse staining of the apical VNO (arrowheads) starting at P2. (K) Onset of Na v 1.6 in somata (asterisks) at P2 with increasing numbers at P7 and P14 throughout the VNO (brackets). (L) Na v 1.7 in single VSN somata (asterisks) and axon bundles (arrows) starts at P2. The knob area is substantially stained from P7 onwards. Images are representatives of n ≥ 3 adult mice ( n = 20 sections per mouse) and n = 2 juvenile mice each at P2, P7, and P14 ( n ≥ 10 sections per mouse). Scale bars overviews ( A–H , left) and (E–H) 100 μm; magnifications (A–D) and (I–L) 20 μm.

    Techniques Used: Expressing, Staining, Labeling

    Subcellular localization of Na v 1.7 and Na v 1.3 staining during mouse MOE development. (A,B) Coronal tissue sections showing the dorsal aspect of the left nasal cavity (septum to the left) of a postnatal day 7 (P7) mouse. A strip of strong immunoreactivity is visible for (A) Na v 1.7 and (B) Na v 1.3 in the most apical MOE layer (arrowheads) and in axon bundles (arrows). (C,D) Higher magnifications of the MOE derived at different mouse ages stained with antibodies for (C) Na v 1.7 and (D) Na v 1.3. The confocal images show strongly stained OSN somata solely in the apical MOE. Somatic OSN staining is visible at embryonic day 18 (E18), P2, and P7, declines at about P14 and is nearly diminished at P21. Axon bundles stain early on (arrows) and increase in size with age in relation to epithelial thickness. Images are representatives of ( n ≥ 2) mice at each age with n ≥ 10 sections per mouse. Scale bars (A,B) 200 μm, (C,D) 20 μm.
    Figure Legend Snippet: Subcellular localization of Na v 1.7 and Na v 1.3 staining during mouse MOE development. (A,B) Coronal tissue sections showing the dorsal aspect of the left nasal cavity (septum to the left) of a postnatal day 7 (P7) mouse. A strip of strong immunoreactivity is visible for (A) Na v 1.7 and (B) Na v 1.3 in the most apical MOE layer (arrowheads) and in axon bundles (arrows). (C,D) Higher magnifications of the MOE derived at different mouse ages stained with antibodies for (C) Na v 1.7 and (D) Na v 1.3. The confocal images show strongly stained OSN somata solely in the apical MOE. Somatic OSN staining is visible at embryonic day 18 (E18), P2, and P7, declines at about P14 and is nearly diminished at P21. Axon bundles stain early on (arrows) and increase in size with age in relation to epithelial thickness. Images are representatives of ( n ≥ 2) mice at each age with n ≥ 10 sections per mouse. Scale bars (A,B) 200 μm, (C,D) 20 μm.

    Techniques Used: Staining, Stripping Membranes, Derivative Assay

    Somatic expression of Na v 1.3 and Na v 1.7 occurs in mature OSNs. Colocalization of Na v 1.3, GAP43, and Na v 1.7 in the olfactory epithelium of a P7 OMP-GFP mouse (endogenous fluorescence, green). (A) Single fluorescence images for Na v 1.3 (red), OMP-GFP (green), and GAP43 (blue). (B) Magnified merge of the images in (A) shows that Na v 1.3 colocalizes with OMP-GFP (arrows) in mature OSN somata located in the apical layer (dotted line). Occasionally, triple-labeled OSNs, positive for Na v 1.3, OMP-GFP, and GAP43 were detected (asterisk). (C) Colocalization of Na v 1.3 (red) and Na v 1.7 (blue) in OMP-GFP + OSNs (asterisks) intermingle with singly, OMP-GFP labeled OSNs (arrowhead). Images are representatives of ( n = 2) mice with n ≥ 10 sections per mouse. Scale bars, 20 μm.
    Figure Legend Snippet: Somatic expression of Na v 1.3 and Na v 1.7 occurs in mature OSNs. Colocalization of Na v 1.3, GAP43, and Na v 1.7 in the olfactory epithelium of a P7 OMP-GFP mouse (endogenous fluorescence, green). (A) Single fluorescence images for Na v 1.3 (red), OMP-GFP (green), and GAP43 (blue). (B) Magnified merge of the images in (A) shows that Na v 1.3 colocalizes with OMP-GFP (arrows) in mature OSN somata located in the apical layer (dotted line). Occasionally, triple-labeled OSNs, positive for Na v 1.3, OMP-GFP, and GAP43 were detected (asterisk). (C) Colocalization of Na v 1.3 (red) and Na v 1.7 (blue) in OMP-GFP + OSNs (asterisks) intermingle with singly, OMP-GFP labeled OSNs (arrowhead). Images are representatives of ( n = 2) mice with n ≥ 10 sections per mouse. Scale bars, 20 μm.

    Techniques Used: Expressing, Fluorescence, Labeling

    Recovery of Na v 1.3 and Na v 1.7 expression in OSN somata during regeneration from chemical ablation. (A–C) Coronal MOE sections of the anterior left nasal cavity (septum to the left) of OMP-GFP mice. (A) Untreated control mice display OMP-GFP labeling of OSNs throughout the MOE (arrowheads). Inset magnification exemplifies regular thickness of axon bundles (arrows) and the MOE (double arrow, 80 μm). (B) Severely damaged MOE 2 weeks post-lesion. Small patch of unlesioned MOE at the septal wall (asterisk). The inset magnification depicts the reduced thickness of axon bundles (arrows) and the MOE (double arrow, 35 μm) 2 weeks post-lesion. Few newly generated OMP-GFP positive OSNs are visible (arrowheads). (C) The MOE has largely recovered 8 weeks post-lesion (arrowheads). The inset magnification shows that the thickness of axon bundles (arrows) and the MOE (double arrow, 70 μm) is increased. Basal membrane (dotted line). (D) Immunoreactivity for Na v 1.3 and Na v 1.7 in the intact, unlesioned MOE shows strong labeling of axon bundles (asterisks). (E) Eight weeks post-lesion, tissue stretches with heavy immunolabeling for Na v 1.3 and Na v 1.7 in OSN somata (arrowheads) reside side-by-side with areas devoid of any somatic immunoreactivity (arrows). This pattern likely coincides with the different levels of initial damage yielding various levels of MOE regeneration. (F,G) Magnifications of the MOE at 6, 8, and 10 weeks post-lesion showing somatic staining for (F) Na v 1.3 (red) and (G) Na v 1.7 (red) colocalizing with OMP-GFP (green). Images are representatives of ( n = 2) mice at each recovery time point with n ≥ 20 sections per mouse. Scale bars (A–C) 200 μm, (D,E) 50 μm (F,G) 20 μm.
    Figure Legend Snippet: Recovery of Na v 1.3 and Na v 1.7 expression in OSN somata during regeneration from chemical ablation. (A–C) Coronal MOE sections of the anterior left nasal cavity (septum to the left) of OMP-GFP mice. (A) Untreated control mice display OMP-GFP labeling of OSNs throughout the MOE (arrowheads). Inset magnification exemplifies regular thickness of axon bundles (arrows) and the MOE (double arrow, 80 μm). (B) Severely damaged MOE 2 weeks post-lesion. Small patch of unlesioned MOE at the septal wall (asterisk). The inset magnification depicts the reduced thickness of axon bundles (arrows) and the MOE (double arrow, 35 μm) 2 weeks post-lesion. Few newly generated OMP-GFP positive OSNs are visible (arrowheads). (C) The MOE has largely recovered 8 weeks post-lesion (arrowheads). The inset magnification shows that the thickness of axon bundles (arrows) and the MOE (double arrow, 70 μm) is increased. Basal membrane (dotted line). (D) Immunoreactivity for Na v 1.3 and Na v 1.7 in the intact, unlesioned MOE shows strong labeling of axon bundles (asterisks). (E) Eight weeks post-lesion, tissue stretches with heavy immunolabeling for Na v 1.3 and Na v 1.7 in OSN somata (arrowheads) reside side-by-side with areas devoid of any somatic immunoreactivity (arrows). This pattern likely coincides with the different levels of initial damage yielding various levels of MOE regeneration. (F,G) Magnifications of the MOE at 6, 8, and 10 weeks post-lesion showing somatic staining for (F) Na v 1.3 (red) and (G) Na v 1.7 (red) colocalizing with OMP-GFP (green). Images are representatives of ( n = 2) mice at each recovery time point with n ≥ 20 sections per mouse. Scale bars (A–C) 200 μm, (D,E) 50 μm (F,G) 20 μm.

    Techniques Used: Expressing, Labeling, Generated, Immunolabeling, Staining

    anti na v 1 3  (Alomone Labs)


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    Alomone Labs anti na v 1 3
    Anti Na V 1 3, 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
    https://www.bioz.com/result/anti na v 1 3/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti na v 1 3 - by Bioz Stars, 2023-09
    86/100 stars

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    anti na v 1 3  (Alomone Labs)


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    Alomone Labs anti na v 1 3
    Anti Na V 1 3, 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
    https://www.bioz.com/result/anti na v 1 3/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti na v 1 3 - by Bioz Stars, 2023-09
    86/100 stars

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    na v 1 3  (Alomone Labs)


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    Alomone Labs na v 1 3
    Na V 1 3, 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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    Average 86 stars, based on 1 article reviews
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    na v 1 3  (Alomone Labs)


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    Structured Review

    Alomone Labs na v 1 3
    Na V 1 3, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/na v 1 3/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
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    • anti na v 1 3  (Alomone Labs)
    93
    Alomone Labs anti na v 1 3
    Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.
    Anti Na V 1 3, 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/anti na v 1 3/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    anti na v 1 3 rabbit polyclonal  (Alomone Labs)
    86
    Alomone Labs anti na v 1 3 rabbit polyclonal
    The Na v 1.3/1.1 selective blocker ICA-121431, but not the Na v 1.2/1.6 Na + channel blocker S-Lic reverses enhanced dendritic excitability. ( A and E ) Representative examples of the effects of the Na v 1.2/1.6 Na + channel blocker S-Lic (300 µM) on dendritic spikes ( insets show magnification of the fast phase of the dendritic spike), and on the first derivation of the voltage trace (d V /d t ) in sham-control ( A ) and epileptic ( E ) animals. ( B and F ) Effects of S-Lic on the maximal rate of rise of the dendritic spike in sham-control ( B ) and epileptic mice ( F ). ( C and G ) Representative examples of effects on the dendritic spike threshold in sham-control and epileptic mice (arrows indicate occurrence of dendritic spikes and dashed lines indicate thresholds). ( D and H ) Quantification showing the lack of significant effects on the dendritic spike threshold in sham-control ( D ) and epileptic mice ( H ) with S-Lic application. Two-way ANOVA revealed no significant effects of S-Lic on the rate of rise or threshold of dendritic spikes in control ( B and D ) and epileptic ( F and H ) animals. ( I – K ) Effects of S-Lic on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of S-Lic (violet, I ). Effects of S-Lic on firing induced by current injection at which firing frequency was maximal under ACSF conditions, control and epileptic animals ( I and K, respectively). Asterisks indicate Bonferroni’s post-test P = 0.0034. ( L – S ) Effects of the Na v 1.3/1.1 Na + channel blocker ICA-121431 (100 nM) in sham-control ( L – O ) and epileptic animals ( P – S ), depicted in the same manner as in panels ( A – H ). Asterisks indicate Bonferroni’s post-test, P = 0.023 ( Q ) and P = 0.0050 ( S ). ( T – V ) Lack of effects of ICA-121431 on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of ICA-121431 (blue, T ). Lack of effects of ICA-121431 on the maximal firing frequency of CA1 neurons ( U and V ).
    Anti Na V 1 3 Rabbit Polyclonal, 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
    https://www.bioz.com/result/anti na v 1 3 rabbit polyclonal/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti na v 1 3 rabbit polyclonal - by Bioz Stars, 2023-09
    86/100 stars
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    na v 1 3  (Alomone Labs)
    86
    Alomone Labs na v 1 3
    The Na v 1.3/1.1 selective blocker ICA-121431, but not the Na v 1.2/1.6 Na + channel blocker S-Lic reverses enhanced dendritic excitability. ( A and E ) Representative examples of the effects of the Na v 1.2/1.6 Na + channel blocker S-Lic (300 µM) on dendritic spikes ( insets show magnification of the fast phase of the dendritic spike), and on the first derivation of the voltage trace (d V /d t ) in sham-control ( A ) and epileptic ( E ) animals. ( B and F ) Effects of S-Lic on the maximal rate of rise of the dendritic spike in sham-control ( B ) and epileptic mice ( F ). ( C and G ) Representative examples of effects on the dendritic spike threshold in sham-control and epileptic mice (arrows indicate occurrence of dendritic spikes and dashed lines indicate thresholds). ( D and H ) Quantification showing the lack of significant effects on the dendritic spike threshold in sham-control ( D ) and epileptic mice ( H ) with S-Lic application. Two-way ANOVA revealed no significant effects of S-Lic on the rate of rise or threshold of dendritic spikes in control ( B and D ) and epileptic ( F and H ) animals. ( I – K ) Effects of S-Lic on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of S-Lic (violet, I ). Effects of S-Lic on firing induced by current injection at which firing frequency was maximal under ACSF conditions, control and epileptic animals ( I and K, respectively). Asterisks indicate Bonferroni’s post-test P = 0.0034. ( L – S ) Effects of the Na v 1.3/1.1 Na + channel blocker ICA-121431 (100 nM) in sham-control ( L – O ) and epileptic animals ( P – S ), depicted in the same manner as in panels ( A – H ). Asterisks indicate Bonferroni’s post-test, P = 0.023 ( Q ) and P = 0.0050 ( S ). ( T – V ) Lack of effects of ICA-121431 on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of ICA-121431 (blue, T ). Lack of effects of ICA-121431 on the maximal firing frequency of CA1 neurons ( U and V ).
    Na V 1 3, 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
    https://www.bioz.com/result/na v 1 3/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    na v 1 3 - by Bioz Stars, 2023-09
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    Image Search Results


    Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.

    Journal: International Journal of Molecular Sciences

    Article Title: Pharmacological Dissection of the Crosstalk between Na V and Ca V Channels in GH3b6 Cells

    doi: 10.3390/ijms23020827

    Figure Lengend Snippet: Na V channel expression in GH3b6 cells. ( A ) The mRNA expression levels of all α and β subunits were first determined by relative RT-qPCR. ( B ) RT-qPCR with absolute quantification for the genes, which were detected by relative RT-qPCR. One-way ANOVA (**** p < 0.0001) followed by Tukey post-hoc multiple comparison test was performed. The data are mean ± SEM. D: Disregarded (Ct > 32); ND: Not Detected. ( C ) Western blot analysis of Na V channel expression. Immunoblotting was performed using pan-Na V and Nav1.3 channels antibodies with 20 and 50 µg of protein extracts from GH3b6 cells and rat brain, after separation on 8% SDS-PAGE. Actin was the loading control. ( D ) Immunocytolocalization of Na V 1.3 channels in GH3b6 cells. Fluorescence labeling (green) using Alexa Fluor 488 anti-mouse secondary antibody allowed the detection of Na V 1.3 channels at the plasma membrane. Nuclei (blue) were stained with DAPI. Original magnification ×60.

    Article Snippet: The primary antibodies used were anti-pan Na V (rabbit, SP19, ASC-003, Alomone labs, Jerusalem, Israel), anti-Na V 1.3 (rabbit, ASC-004, Alomone labs or mouse, WH0006328M1, Sigma-Aldrich Merck), and anti-actin used as loading control (mouse, clones AC-203 or AC-74, Sigma-Aldrich Merck).

    Techniques: Expressing, Quantitative RT-PCR, Western Blot, SDS Page, Fluorescence, Labeling, Staining

    Effects of ICA-121431, a selective inhibitor of Na V 1.3 channels, on I Na recorded in GH3b6 cells by manual patch-clamp. ( A , B ) To illustrate the effects of ICA-121431, examples of superimposed I Na elicited by 500 ms depolarizing pulses (at −20, 0, and +20 mV) and examples of superimposed I Na elicited by depolarizing pulse at 0 mV immediately after a 500 ms prepulse (−120, −60, and −50 mV) are shown. The control traces are in blue (CTRL) and red traces correspond to I Na after ICA-121431 application (1 µM). ( B ) Current–voltage relationships and ( C ) activation/inactivation curves of I Na recorded before (blue circles) and after 1 µM ICA-121431 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.

    Journal: International Journal of Molecular Sciences

    Article Title: Pharmacological Dissection of the Crosstalk between Na V and Ca V Channels in GH3b6 Cells

    doi: 10.3390/ijms23020827

    Figure Lengend Snippet: Effects of ICA-121431, a selective inhibitor of Na V 1.3 channels, on I Na recorded in GH3b6 cells by manual patch-clamp. ( A , B ) To illustrate the effects of ICA-121431, examples of superimposed I Na elicited by 500 ms depolarizing pulses (at −20, 0, and +20 mV) and examples of superimposed I Na elicited by depolarizing pulse at 0 mV immediately after a 500 ms prepulse (−120, −60, and −50 mV) are shown. The control traces are in blue (CTRL) and red traces correspond to I Na after ICA-121431 application (1 µM). ( B ) Current–voltage relationships and ( C ) activation/inactivation curves of I Na recorded before (blue circles) and after 1 µM ICA-121431 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.

    Article Snippet: The primary antibodies used were anti-pan Na V (rabbit, SP19, ASC-003, Alomone labs, Jerusalem, Israel), anti-Na V 1.3 (rabbit, ASC-004, Alomone labs or mouse, WH0006328M1, Sigma-Aldrich Merck), and anti-actin used as loading control (mouse, clones AC-203 or AC-74, Sigma-Aldrich Merck).

    Techniques: Patch Clamp, Activation Assay, Two Tailed Test

    Effects of Tf2, a selective β-scorpion toxin of Na V 1.3 channels, on I Na recorded in GH3b6 cells by automated patch-clamp. ( A ) Representative examples of I Na elicited by 50 ms depolarization steps (protocol inset), in the absence and presence of 1 nM Tf2. To illustrate the strong effect of 1 nM Tf2, superimposed I Na traces at −45 mV are shown. ( B ) Current–voltage relationships ( C ) and activation/inactivation curves of I Na recorded before (blue circles) and after 1 nM Tf2 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.

    Journal: International Journal of Molecular Sciences

    Article Title: Pharmacological Dissection of the Crosstalk between Na V and Ca V Channels in GH3b6 Cells

    doi: 10.3390/ijms23020827

    Figure Lengend Snippet: Effects of Tf2, a selective β-scorpion toxin of Na V 1.3 channels, on I Na recorded in GH3b6 cells by automated patch-clamp. ( A ) Representative examples of I Na elicited by 50 ms depolarization steps (protocol inset), in the absence and presence of 1 nM Tf2. To illustrate the strong effect of 1 nM Tf2, superimposed I Na traces at −45 mV are shown. ( B ) Current–voltage relationships ( C ) and activation/inactivation curves of I Na recorded before (blue circles) and after 1 nM Tf2 (red circles). Comparison of V 1/2 activation ( D ) and inactivation ( E ) in the absence (CTRL) and in the presence of 1 nM Tf2. Statistical analysis was performed using the two-tailed unpaired t -test, **** p < 0.0001. Data represent the mean ± SEM.

    Article Snippet: The primary antibodies used were anti-pan Na V (rabbit, SP19, ASC-003, Alomone labs, Jerusalem, Israel), anti-Na V 1.3 (rabbit, ASC-004, Alomone labs or mouse, WH0006328M1, Sigma-Aldrich Merck), and anti-actin used as loading control (mouse, clones AC-203 or AC-74, Sigma-Aldrich Merck).

    Techniques: Patch Clamp, Activation Assay, Two Tailed Test

    Effect of Tf2, a selective β-scorpion toxin of Na V 1.3, on the intracellular Ca 2+ level in GH3b6 cells. ( A ) Representative kinetics of Fura-2 fluorescence emission in GH3b6 cells treated with increasing concentrations of Tf2. ( B ) The Ca 2+ responses induced by Tf2 are concentration dependent. The concentration–response relationships were analyzed using the Hill–Langmuir equation with variable slope. The values of EC 50 and the Hill coefficient were 17.51 ± 1.4 nM and 1.378 (R 2 = 0.99). ( C ) TTX inhibits in a concentration-dependent manner the Ca 2+ responses elicited by 0.5 µM of Tf2 with an IC 50 value of 7.9 ± 2.1 nM and a Hill coefficient of 1.31 ± 0.135, R 2 = 0.94. The data represent the mean ± SEM ( n = 3 wells) and are representative of at least two independent experiments.

    Journal: International Journal of Molecular Sciences

    Article Title: Pharmacological Dissection of the Crosstalk between Na V and Ca V Channels in GH3b6 Cells

    doi: 10.3390/ijms23020827

    Figure Lengend Snippet: Effect of Tf2, a selective β-scorpion toxin of Na V 1.3, on the intracellular Ca 2+ level in GH3b6 cells. ( A ) Representative kinetics of Fura-2 fluorescence emission in GH3b6 cells treated with increasing concentrations of Tf2. ( B ) The Ca 2+ responses induced by Tf2 are concentration dependent. The concentration–response relationships were analyzed using the Hill–Langmuir equation with variable slope. The values of EC 50 and the Hill coefficient were 17.51 ± 1.4 nM and 1.378 (R 2 = 0.99). ( C ) TTX inhibits in a concentration-dependent manner the Ca 2+ responses elicited by 0.5 µM of Tf2 with an IC 50 value of 7.9 ± 2.1 nM and a Hill coefficient of 1.31 ± 0.135, R 2 = 0.94. The data represent the mean ± SEM ( n = 3 wells) and are representative of at least two independent experiments.

    Article Snippet: The primary antibodies used were anti-pan Na V (rabbit, SP19, ASC-003, Alomone labs, Jerusalem, Israel), anti-Na V 1.3 (rabbit, ASC-004, Alomone labs or mouse, WH0006328M1, Sigma-Aldrich Merck), and anti-actin used as loading control (mouse, clones AC-203 or AC-74, Sigma-Aldrich Merck).

    Techniques: Fluorescence, Concentration Assay

    The Na v 1.3/1.1 selective blocker ICA-121431, but not the Na v 1.2/1.6 Na + channel blocker S-Lic reverses enhanced dendritic excitability. ( A and E ) Representative examples of the effects of the Na v 1.2/1.6 Na + channel blocker S-Lic (300 µM) on dendritic spikes ( insets show magnification of the fast phase of the dendritic spike), and on the first derivation of the voltage trace (d V /d t ) in sham-control ( A ) and epileptic ( E ) animals. ( B and F ) Effects of S-Lic on the maximal rate of rise of the dendritic spike in sham-control ( B ) and epileptic mice ( F ). ( C and G ) Representative examples of effects on the dendritic spike threshold in sham-control and epileptic mice (arrows indicate occurrence of dendritic spikes and dashed lines indicate thresholds). ( D and H ) Quantification showing the lack of significant effects on the dendritic spike threshold in sham-control ( D ) and epileptic mice ( H ) with S-Lic application. Two-way ANOVA revealed no significant effects of S-Lic on the rate of rise or threshold of dendritic spikes in control ( B and D ) and epileptic ( F and H ) animals. ( I – K ) Effects of S-Lic on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of S-Lic (violet, I ). Effects of S-Lic on firing induced by current injection at which firing frequency was maximal under ACSF conditions, control and epileptic animals ( I and K, respectively). Asterisks indicate Bonferroni’s post-test P = 0.0034. ( L – S ) Effects of the Na v 1.3/1.1 Na + channel blocker ICA-121431 (100 nM) in sham-control ( L – O ) and epileptic animals ( P – S ), depicted in the same manner as in panels ( A – H ). Asterisks indicate Bonferroni’s post-test, P = 0.023 ( Q ) and P = 0.0050 ( S ). ( T – V ) Lack of effects of ICA-121431 on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of ICA-121431 (blue, T ). Lack of effects of ICA-121431 on the maximal firing frequency of CA1 neurons ( U and V ).

    Journal: Brain

    Article Title: Targeting aberrant dendritic integration to treat cognitive comorbidities of epilepsy

    doi: 10.1093/brain/awac455

    Figure Lengend Snippet: The Na v 1.3/1.1 selective blocker ICA-121431, but not the Na v 1.2/1.6 Na + channel blocker S-Lic reverses enhanced dendritic excitability. ( A and E ) Representative examples of the effects of the Na v 1.2/1.6 Na + channel blocker S-Lic (300 µM) on dendritic spikes ( insets show magnification of the fast phase of the dendritic spike), and on the first derivation of the voltage trace (d V /d t ) in sham-control ( A ) and epileptic ( E ) animals. ( B and F ) Effects of S-Lic on the maximal rate of rise of the dendritic spike in sham-control ( B ) and epileptic mice ( F ). ( C and G ) Representative examples of effects on the dendritic spike threshold in sham-control and epileptic mice (arrows indicate occurrence of dendritic spikes and dashed lines indicate thresholds). ( D and H ) Quantification showing the lack of significant effects on the dendritic spike threshold in sham-control ( D ) and epileptic mice ( H ) with S-Lic application. Two-way ANOVA revealed no significant effects of S-Lic on the rate of rise or threshold of dendritic spikes in control ( B and D ) and epileptic ( F and H ) animals. ( I – K ) Effects of S-Lic on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of S-Lic (violet, I ). Effects of S-Lic on firing induced by current injection at which firing frequency was maximal under ACSF conditions, control and epileptic animals ( I and K, respectively). Asterisks indicate Bonferroni’s post-test P = 0.0034. ( L – S ) Effects of the Na v 1.3/1.1 Na + channel blocker ICA-121431 (100 nM) in sham-control ( L – O ) and epileptic animals ( P – S ), depicted in the same manner as in panels ( A – H ). Asterisks indicate Bonferroni’s post-test, P = 0.023 ( Q ) and P = 0.0050 ( S ). ( T – V ) Lack of effects of ICA-121431 on somatic action potential generation. Representative examples of repetitive firing evoked by somatic current injection in sham-control and epileptic mice in ACSF and in the presence of ICA-121431 (blue, T ). Lack of effects of ICA-121431 on the maximal firing frequency of CA1 neurons ( U and V ).

    Article Snippet: The primary and secondary antibodies were the following: anti-Na v 1.2 rabbit polyclonal (1:200; ASC-002, Alomone Labs); anti-Na v 1.3 rabbit polyclonal (1:200; ASC-004, Alomone Labs); anti-GAPDH mouse monoclonal (1:1000, NB300-221, Novus); IRDye® 800CW goat anti-rabbit IgG secondary antibody (1:10000, 926-32211, LI-COR Biosciences); IRDye® 680LT donkey anti-mouse IgG secondary antibody (1:10000, 926-68022, LI-COR Biosciences).

    Techniques: Injection

    Scn3a expression is increased at the mRNA and protein level in the hippocampal CA1 region of epileptic mice . ( A – D ) Multiplex fluorescent mRNA in-situ hybridization for Scn3a in hippocampal CA1 region. ( A and B ) Representative fluorescent images showing labelling of nuclei with DAPI (blue), labelling of GABAergic neurons (GAD) with a probe for Gad1/2 mRNA (green) and of Scn3a mRNA (red) in hippocampal slices from sham-control and epileptic animals, scale bar 500 µm. Close up ( right ) of the boxed areas, scale bar = 100 µm. ( C ) Cumulative distribution of Scn3a punctae per nucleus colocalized excitatory pyramidal cells (excluding GAD-labelled putative interneurons). The amount of punctae was significantly higher in epileptic animals (2979 cells in six animals and 3669 cells in five animals, for sham-control and epileptic mice, respectively; asterisks indicate Kolmogorov–Smirnov two-tailed test P < 0.0001). ( D ) Cumulative distribution of Scn3a punctae per nucleus colocalized in GAD+ interneurons. The amount of punctae was significantly lower in epileptic animals (253 cells in five animals and 141 cells in five animals, for sham-control and epileptic mice, respectively; asterisks indicate Kolmogorov–Smirnov two-tailed test P < 0.001). ( E – H ) Western blots for Na v 1.3 and Na v 1.2 in hippocampal CA1 region. ( E ) Representative Western blots of Na v 1.3 (indicated with arrrowhead) and the housekeeping protein GAPDH, used as loading control in sham-control and epileptic mice. ( F ) Quantitative analysis of the Na v 1.2 protein obtained by band intensity analysis from E (normalized Na v 1.2/GAPDH ratio of 1.0 ± 0.36 in sham-control n = 4 and 3.64 ± 0.85 in epileptic mice n = 4; unpaired Student’s t -test P = 0.029; data represent mean ± SEM). ( G ) Representative Western blots of Na v 1.2 (indicated with arrrowhead) and the housekeeping protein GAPDH, used as loading control in sham-control and epileptic mice. ( H ) Quantitative analysis of the Na v 1.2 protein obtained by band intensity analysis from G (normalized Na v 1.2/GAPDH ratio of 1.0 ± 0.05 in sham-control n = 3 and 0.93 ± 0.052 in epileptic mice n = 3; unpaired Student’s t -test P = 0.38).

    Journal: Brain

    Article Title: Targeting aberrant dendritic integration to treat cognitive comorbidities of epilepsy

    doi: 10.1093/brain/awac455

    Figure Lengend Snippet: Scn3a expression is increased at the mRNA and protein level in the hippocampal CA1 region of epileptic mice . ( A – D ) Multiplex fluorescent mRNA in-situ hybridization for Scn3a in hippocampal CA1 region. ( A and B ) Representative fluorescent images showing labelling of nuclei with DAPI (blue), labelling of GABAergic neurons (GAD) with a probe for Gad1/2 mRNA (green) and of Scn3a mRNA (red) in hippocampal slices from sham-control and epileptic animals, scale bar 500 µm. Close up ( right ) of the boxed areas, scale bar = 100 µm. ( C ) Cumulative distribution of Scn3a punctae per nucleus colocalized excitatory pyramidal cells (excluding GAD-labelled putative interneurons). The amount of punctae was significantly higher in epileptic animals (2979 cells in six animals and 3669 cells in five animals, for sham-control and epileptic mice, respectively; asterisks indicate Kolmogorov–Smirnov two-tailed test P < 0.0001). ( D ) Cumulative distribution of Scn3a punctae per nucleus colocalized in GAD+ interneurons. The amount of punctae was significantly lower in epileptic animals (253 cells in five animals and 141 cells in five animals, for sham-control and epileptic mice, respectively; asterisks indicate Kolmogorov–Smirnov two-tailed test P < 0.001). ( E – H ) Western blots for Na v 1.3 and Na v 1.2 in hippocampal CA1 region. ( E ) Representative Western blots of Na v 1.3 (indicated with arrrowhead) and the housekeeping protein GAPDH, used as loading control in sham-control and epileptic mice. ( F ) Quantitative analysis of the Na v 1.2 protein obtained by band intensity analysis from E (normalized Na v 1.2/GAPDH ratio of 1.0 ± 0.36 in sham-control n = 4 and 3.64 ± 0.85 in epileptic mice n = 4; unpaired Student’s t -test P = 0.029; data represent mean ± SEM). ( G ) Representative Western blots of Na v 1.2 (indicated with arrrowhead) and the housekeeping protein GAPDH, used as loading control in sham-control and epileptic mice. ( H ) Quantitative analysis of the Na v 1.2 protein obtained by band intensity analysis from G (normalized Na v 1.2/GAPDH ratio of 1.0 ± 0.05 in sham-control n = 3 and 0.93 ± 0.052 in epileptic mice n = 3; unpaired Student’s t -test P = 0.38).

    Article Snippet: The primary and secondary antibodies were the following: anti-Na v 1.2 rabbit polyclonal (1:200; ASC-002, Alomone Labs); anti-Na v 1.3 rabbit polyclonal (1:200; ASC-004, Alomone Labs); anti-GAPDH mouse monoclonal (1:1000, NB300-221, Novus); IRDye® 800CW goat anti-rabbit IgG secondary antibody (1:10000, 926-32211, LI-COR Biosciences); IRDye® 680LT donkey anti-mouse IgG secondary antibody (1:10000, 926-68022, LI-COR Biosciences).

    Techniques: Expressing, Multiplex Assay, In Situ Hybridization, Two Tailed Test, Western Blot