anti na v 1 1 antibody  (Alomone Labs)


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    Alomone Labs anti na v 1 1 antibody
    A . Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R613X allele. B-C. qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R613X on the mixed background (B), as well as on the pure 129S1/SvImJ background (C). A marginal background expression was found in homozygous Scn1a R613X/R613X mice. Mixed background: WT, n=4; Scn1a WT/R613X T , n=4; Scn1a R613X/R613X , n=2. 129S1/SvImJ background: WT, n=4; Scn1a WT/R613X , n=4. D. Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. E . Quantification of Na V 1.1 protein level from D. Only two of the three Scn1a R613X/R613X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in C and E utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in C utilized t-test. *, p<0.05, **, p<0.01, ***, p<0.001.
    Anti Na V 1 1 Antibody, 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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    Images

    1) Product Images from "Heat-induced seizures, premature mortality, and hyperactivity in a novel Scn1a nonsense model for Dravet syndrome"

    Article Title: Heat-induced seizures, premature mortality, and hyperactivity in a novel Scn1a nonsense model for Dravet syndrome

    Journal: bioRxiv

    doi: 10.1101/2023.02.01.526678

    A . Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R613X allele. B-C. qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R613X on the mixed background (B), as well as on the pure 129S1/SvImJ background (C). A marginal background expression was found in homozygous Scn1a R613X/R613X mice. Mixed background: WT, n=4; Scn1a WT/R613X T , n=4; Scn1a R613X/R613X , n=2. 129S1/SvImJ background: WT, n=4; Scn1a WT/R613X , n=4. D. Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. E . Quantification of Na V 1.1 protein level from D. Only two of the three Scn1a R613X/R613X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in C and E utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in C utilized t-test. *, p<0.05, **, p<0.01, ***, p<0.001.
    Figure Legend Snippet: A . Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R613X allele. B-C. qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R613X on the mixed background (B), as well as on the pure 129S1/SvImJ background (C). A marginal background expression was found in homozygous Scn1a R613X/R613X mice. Mixed background: WT, n=4; Scn1a WT/R613X T , n=4; Scn1a R613X/R613X , n=2. 129S1/SvImJ background: WT, n=4; Scn1a WT/R613X , n=4. D. Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. E . Quantification of Na V 1.1 protein level from D. Only two of the three Scn1a R613X/R613X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in C and E utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in C utilized t-test. *, p<0.05, **, p<0.01, ***, p<0.001.

    Techniques Used: Sequencing, Expressing, Western Blot

    A-C. Allele-specific quantification of Scn1a transcripts via dPCR. The R613X and WT Scn1a alleles were quantified with Affinity Plus probes on dPCR and normalized to mouse Gapdh levels. A. Cortical tissue from WT mice showed no detectable levels of the R613X allele transcript, demonstrating the specificity of allelic discrimination using this assay. B. In cortical tissue from Scn1a WT/R613X mice, the WT Scn1a allele is at 48.8% compared to in WT cortical tissue. C. Shown as the ratio of R613X to WT alleles, the mean steady-state level of the Scn1a R613X allele is at 8.9±0.9% of the WT allele in Scn1a WT/R613X animals. WT, n=6; Scn1a WT/R613X , n=6. D-F. Cortical levels of Na V 1.1 proteins were quantified using the Meso Scale Discovery Electrochemiluminescence (MSD-ECL) assay. D. The standard curve was generated by mixing P60 WT cortical and liver proteins at different ratios. The resulting 2 nd order polynomial fit, depicted as a solid line (R 2 = 0.9924) was used to calculate protein levels relative to P60 WT cortex in E and F. E. Protein Na V 1.1 expression in the whole cortex. F. Na V 1.1 protein expression in the parietal, temporal, frontal, and occipital lobes of the neocortex of WT and WT/R613X mice. G. The same data from F, but normalized to Na V 1.1 expression in WT mice. WT, n=4; Scn1a WT/R613X , n=4. Statistical comparison by unpaired t-test. ***, p<0.001, ****, p<0.0001
    Figure Legend Snippet: A-C. Allele-specific quantification of Scn1a transcripts via dPCR. The R613X and WT Scn1a alleles were quantified with Affinity Plus probes on dPCR and normalized to mouse Gapdh levels. A. Cortical tissue from WT mice showed no detectable levels of the R613X allele transcript, demonstrating the specificity of allelic discrimination using this assay. B. In cortical tissue from Scn1a WT/R613X mice, the WT Scn1a allele is at 48.8% compared to in WT cortical tissue. C. Shown as the ratio of R613X to WT alleles, the mean steady-state level of the Scn1a R613X allele is at 8.9±0.9% of the WT allele in Scn1a WT/R613X animals. WT, n=6; Scn1a WT/R613X , n=6. D-F. Cortical levels of Na V 1.1 proteins were quantified using the Meso Scale Discovery Electrochemiluminescence (MSD-ECL) assay. D. The standard curve was generated by mixing P60 WT cortical and liver proteins at different ratios. The resulting 2 nd order polynomial fit, depicted as a solid line (R 2 = 0.9924) was used to calculate protein levels relative to P60 WT cortex in E and F. E. Protein Na V 1.1 expression in the whole cortex. F. Na V 1.1 protein expression in the parietal, temporal, frontal, and occipital lobes of the neocortex of WT and WT/R613X mice. G. The same data from F, but normalized to Na V 1.1 expression in WT mice. WT, n=4; Scn1a WT/R613X , n=4. Statistical comparison by unpaired t-test. ***, p<0.001, ****, p<0.0001

    Techniques Used: Electrochemiluminescence, Generated, Expressing

    anti na v 1 1  (Alomone Labs)


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    Alomone Labs anti na v 1 1
    Proband and control iPSCs were differentiated into neurons to perform long-read sequencing and protein analysis. (A) Sashimi plots illustrate alternative splicing events identified by long-read RNA sequencing. Vertical bars indicate exons, and the height of the bars is proportionate to the read depth supporting the inclusion of an exon. Horizontal arcs illustrate splicing junctions that are supported by the sequencing reads. For visualization purposes, we highlight the region of SCN1A between exons 19 and 22, although individual reads capture the entire transcript. Sashimi plots are representative plots from one biological replicate. (B) We quantified the relative abundance of transcripts that include 20N for each sample. Abundance was calculated as a percentage of inclusion transcripts, normalized for read depth and cell maturation. Cell maturation was determined by the relative normalized expression of SCN3A and SCN8A . Two WT cell lines with the same genotype were combined for statistical analysis. Data are presented as the mean ± SD. For comparisons, an ordinary one-way ANOVA with post-hoc test was performed on WT-variant pairs (*P-adjusted ≤ 0.05; **P ≤ 0.01; ***P<0.001). Biologic replicates n = 1-3. (C) Relative abundance of 20N inclusion transcripts grouped by genotype. For comparisons, student’s unpaired two-tailed t-test was performed (***P<0.001). (D) Proband iPSC-derived neurons show less Na v 1.1 protein as detected by Western blot. Samples were prepared by membrane protein isolation, so Na,K-ATPase is used as a loading control. The sample in lane 4 serves as a positive control for haploinsufficiency as this lysate was prepared from neurons derived from an individual with Dravet syndrome who carries a heterozygous upstream deletion of the SCN1A transcription start site. Lysate from WT iPSCs is included as a negative control as iPSCs do not express SCN1A . Biologic replicates n = 1. (E) ImageJ quantification of Western blot bands shows reduced abundance of Na v 1.1 in neurons from probands 1, 4, and 5 as well as the haploinsufficiency control cells compared to WT.
    Anti Na V 1 1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Long-read sequencing and profiling of RNA-binding proteins reveals the pathogenic mechanism of aberrant splicing of an SCN1A poison exon in epilepsy"

    Article Title: Long-read sequencing and profiling of RNA-binding proteins reveals the pathogenic mechanism of aberrant splicing of an SCN1A poison exon in epilepsy

    Journal: bioRxiv

    doi: 10.1101/2023.05.04.538282

    Proband and control iPSCs were differentiated into neurons to perform long-read sequencing and protein analysis. (A) Sashimi plots illustrate alternative splicing events identified by long-read RNA sequencing. Vertical bars indicate exons, and the height of the bars is proportionate to the read depth supporting the inclusion of an exon. Horizontal arcs illustrate splicing junctions that are supported by the sequencing reads. For visualization purposes, we highlight the region of SCN1A between exons 19 and 22, although individual reads capture the entire transcript. Sashimi plots are representative plots from one biological replicate. (B) We quantified the relative abundance of transcripts that include 20N for each sample. Abundance was calculated as a percentage of inclusion transcripts, normalized for read depth and cell maturation. Cell maturation was determined by the relative normalized expression of SCN3A and SCN8A . Two WT cell lines with the same genotype were combined for statistical analysis. Data are presented as the mean ± SD. For comparisons, an ordinary one-way ANOVA with post-hoc test was performed on WT-variant pairs (*P-adjusted ≤ 0.05; **P ≤ 0.01; ***P<0.001). Biologic replicates n = 1-3. (C) Relative abundance of 20N inclusion transcripts grouped by genotype. For comparisons, student’s unpaired two-tailed t-test was performed (***P<0.001). (D) Proband iPSC-derived neurons show less Na v 1.1 protein as detected by Western blot. Samples were prepared by membrane protein isolation, so Na,K-ATPase is used as a loading control. The sample in lane 4 serves as a positive control for haploinsufficiency as this lysate was prepared from neurons derived from an individual with Dravet syndrome who carries a heterozygous upstream deletion of the SCN1A transcription start site. Lysate from WT iPSCs is included as a negative control as iPSCs do not express SCN1A . Biologic replicates n = 1. (E) ImageJ quantification of Western blot bands shows reduced abundance of Na v 1.1 in neurons from probands 1, 4, and 5 as well as the haploinsufficiency control cells compared to WT.
    Figure Legend Snippet: Proband and control iPSCs were differentiated into neurons to perform long-read sequencing and protein analysis. (A) Sashimi plots illustrate alternative splicing events identified by long-read RNA sequencing. Vertical bars indicate exons, and the height of the bars is proportionate to the read depth supporting the inclusion of an exon. Horizontal arcs illustrate splicing junctions that are supported by the sequencing reads. For visualization purposes, we highlight the region of SCN1A between exons 19 and 22, although individual reads capture the entire transcript. Sashimi plots are representative plots from one biological replicate. (B) We quantified the relative abundance of transcripts that include 20N for each sample. Abundance was calculated as a percentage of inclusion transcripts, normalized for read depth and cell maturation. Cell maturation was determined by the relative normalized expression of SCN3A and SCN8A . Two WT cell lines with the same genotype were combined for statistical analysis. Data are presented as the mean ± SD. For comparisons, an ordinary one-way ANOVA with post-hoc test was performed on WT-variant pairs (*P-adjusted ≤ 0.05; **P ≤ 0.01; ***P<0.001). Biologic replicates n = 1-3. (C) Relative abundance of 20N inclusion transcripts grouped by genotype. For comparisons, student’s unpaired two-tailed t-test was performed (***P<0.001). (D) Proband iPSC-derived neurons show less Na v 1.1 protein as detected by Western blot. Samples were prepared by membrane protein isolation, so Na,K-ATPase is used as a loading control. The sample in lane 4 serves as a positive control for haploinsufficiency as this lysate was prepared from neurons derived from an individual with Dravet syndrome who carries a heterozygous upstream deletion of the SCN1A transcription start site. Lysate from WT iPSCs is included as a negative control as iPSCs do not express SCN1A . Biologic replicates n = 1. (E) ImageJ quantification of Western blot bands shows reduced abundance of Na v 1.1 in neurons from probands 1, 4, and 5 as well as the haploinsufficiency control cells compared to WT.

    Techniques Used: Sequencing, RNA Sequencing Assay, Expressing, Variant Assay, Two Tailed Test, Derivative Assay, Western Blot, Isolation, Positive Control, Negative Control

    anti na v 1 1 antibody  (Alomone Labs)


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    Alomone Labs anti na v 1 1 antibody
    Reduced Scn1a mRNA and Na V 1.1 protein expression in the hippocampus of Scn1a WT/R 613 X mice. (A) Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R 613 X allele. (B,C) qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R 613 X on the mixed background (B) , and on the pure 129S1/SvImJ background (C) . Marginal background expression was found in homozygous Scn1a R 613 X/R 613 X mice. Mixed background: WT, n = 4; Scn1a WT/R 613 X T , n = 4; Scn1a R 613 X/R 613 X , n = 2. 129S1/SvImJ background: WT, n = 4; Scn1a WT/R 613 X , n = 4. (D) Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. Kilodaltons = kDa. (E) Quantification of Na V 1.1 protein level was based on multiple bands as indicated by the black arrow in panel (D) . Only two of the three Scn1a R 613 X/R 613 X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in panels (C,E) utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in panel (C) utilized t -test. * p < 0.05, ** p < 0.01, *** p < 0.001.
    Anti Na V 1 1 Antibody, 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
    Price from $9.99 to $1999.99
    anti na v 1 1 antibody - by Bioz Stars, 2023-05
    86/100 stars

    Images

    1) Product Images from "Heat-induced seizures, premature mortality, and hyperactivity in a novel Scn1a nonsense model for Dravet syndrome"

    Article Title: Heat-induced seizures, premature mortality, and hyperactivity in a novel Scn1a nonsense model for Dravet syndrome

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2023.1149391

    Reduced Scn1a mRNA and Na V 1.1 protein expression in the hippocampus of Scn1a WT/R 613 X mice. (A) Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R 613 X allele. (B,C) qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R 613 X on the mixed background (B) , and on the pure 129S1/SvImJ background (C) . Marginal background expression was found in homozygous Scn1a R 613 X/R 613 X mice. Mixed background: WT, n = 4; Scn1a WT/R 613 X T , n = 4; Scn1a R 613 X/R 613 X , n = 2. 129S1/SvImJ background: WT, n = 4; Scn1a WT/R 613 X , n = 4. (D) Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. Kilodaltons = kDa. (E) Quantification of Na V 1.1 protein level was based on multiple bands as indicated by the black arrow in panel (D) . Only two of the three Scn1a R 613 X/R 613 X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in panels (C,E) utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in panel (C) utilized t -test. * p < 0.05, ** p < 0.01, *** p < 0.001.
    Figure Legend Snippet: Reduced Scn1a mRNA and Na V 1.1 protein expression in the hippocampus of Scn1a WT/R 613 X mice. (A) Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R 613 X allele. (B,C) qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R 613 X on the mixed background (B) , and on the pure 129S1/SvImJ background (C) . Marginal background expression was found in homozygous Scn1a R 613 X/R 613 X mice. Mixed background: WT, n = 4; Scn1a WT/R 613 X T , n = 4; Scn1a R 613 X/R 613 X , n = 2. 129S1/SvImJ background: WT, n = 4; Scn1a WT/R 613 X , n = 4. (D) Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. Kilodaltons = kDa. (E) Quantification of Na V 1.1 protein level was based on multiple bands as indicated by the black arrow in panel (D) . Only two of the three Scn1a R 613 X/R 613 X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in panels (C,E) utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in panel (C) utilized t -test. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Techniques Used: Expressing, Sequencing, Western Blot

    Reduced Scn1a mRNA and Na V 1.1 protein expression in the cortex of Scn1a WT/R 613 X mice. (A–C) Allele-specific quantification of Scn1a transcripts via dPCR. The R613X and WT Scn1a alleles were quantified with Affinity Plus probes on dPCR and normalized to mouse Gapdh levels. (A) Cortical tissue from WT mice showed no detectable levels of the R613X allele transcript, demonstrating the specificity of allelic discrimination using this assay. (B) In cortical tissue from Scn1a WT/R 613 X mice, the WT Scn1a allele is at 48.8% compared to WT cortical tissue. (C) Shown as the ratio of R613X to WT alleles, the mean steady-state level of the Scn1a R613X allele is at 8.9 ± 0.9% of the WT allele in Scn1a WT/R 613 X animals. WT, n = 6; Scn1a WT/R 613 X , n = 6. (D–F) Cortical levels of Na V 1.1 proteins were quantified using the Meso Scale Discovery Electrochemiluminescence (MSD-ECL) assay. (D) The standard curve was generated by mixing P60 WT cortical and liver proteins at different ratios. The resulting 2nd order polynomial fit, depicted as a solid line ( R 2 = 0.9924) was used to calculate protein levels relative to P60 WT cortex in panels (E,F) . (E) Na V 1.1 protein expression in the whole cortex. (F) Na V 1.1 protein expression in the parietal, temporal, frontal, and occipital lobes of the neocortex of WT and Scn1a WT / R 613 X mice. (G) The same data from panel (F) , but normalized to Na V 1.1 expression in WT mice. WT, n = 4; Scn1a WT/R613X , n = 4. Statistical comparison using mixed model ANOVA followed by Holm–Sidak, to account for analyses of different neocortical sections from each mouse. ** p < 0.01, *** p < 0.001, **** p < 0.0001.
    Figure Legend Snippet: Reduced Scn1a mRNA and Na V 1.1 protein expression in the cortex of Scn1a WT/R 613 X mice. (A–C) Allele-specific quantification of Scn1a transcripts via dPCR. The R613X and WT Scn1a alleles were quantified with Affinity Plus probes on dPCR and normalized to mouse Gapdh levels. (A) Cortical tissue from WT mice showed no detectable levels of the R613X allele transcript, demonstrating the specificity of allelic discrimination using this assay. (B) In cortical tissue from Scn1a WT/R 613 X mice, the WT Scn1a allele is at 48.8% compared to WT cortical tissue. (C) Shown as the ratio of R613X to WT alleles, the mean steady-state level of the Scn1a R613X allele is at 8.9 ± 0.9% of the WT allele in Scn1a WT/R 613 X animals. WT, n = 6; Scn1a WT/R 613 X , n = 6. (D–F) Cortical levels of Na V 1.1 proteins were quantified using the Meso Scale Discovery Electrochemiluminescence (MSD-ECL) assay. (D) The standard curve was generated by mixing P60 WT cortical and liver proteins at different ratios. The resulting 2nd order polynomial fit, depicted as a solid line ( R 2 = 0.9924) was used to calculate protein levels relative to P60 WT cortex in panels (E,F) . (E) Na V 1.1 protein expression in the whole cortex. (F) Na V 1.1 protein expression in the parietal, temporal, frontal, and occipital lobes of the neocortex of WT and Scn1a WT / R 613 X mice. (G) The same data from panel (F) , but normalized to Na V 1.1 expression in WT mice. WT, n = 4; Scn1a WT/R613X , n = 4. Statistical comparison using mixed model ANOVA followed by Holm–Sidak, to account for analyses of different neocortical sections from each mouse. ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Techniques Used: Expressing, Electrochemiluminescence, Generated

    na v 1 1  (Alomone Labs)


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    Alomone Labs na v 1 1
    Reduced Scn1a mRNA and Na V 1.1 protein expression in the hippocampus of Scn1a WT/R 613 X mice. (A) Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R 613 X allele. (B,C) qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R 613 X on the mixed background (B) , and on the pure 129S1/SvImJ background (C) . Marginal background expression was found in homozygous Scn1a R 613 X/R 613 X mice. Mixed background: WT, n = 4; Scn1a WT/R 613 X T , n = 4; Scn1a R 613 X/R 613 X , n = 2. 129S1/SvImJ background: WT, n = 4; Scn1a WT/R 613 X , n = 4. (D) Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. Kilodaltons = kDa. (E) Quantification of Na V 1.1 protein level was based on multiple bands as indicated by the black arrow in panel (D) . Only two of the three Scn1a R 613 X/R 613 X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in panels (C,E) utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in panel (C) utilized t -test. * p < 0.05, ** p < 0.01, *** p < 0.001.
    Na V 1 1, 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 1/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    na v 1 1 - by Bioz Stars, 2023-05
    86/100 stars

    Images

    1) Product Images from "Heat-induced seizures, premature mortality, and hyperactivity in a novel Scn1a nonsense model for Dravet syndrome"

    Article Title: Heat-induced seizures, premature mortality, and hyperactivity in a novel Scn1a nonsense model for Dravet syndrome

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2023.1149391

    Reduced Scn1a mRNA and Na V 1.1 protein expression in the hippocampus of Scn1a WT/R 613 X mice. (A) Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R 613 X allele. (B,C) qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R 613 X on the mixed background (B) , and on the pure 129S1/SvImJ background (C) . Marginal background expression was found in homozygous Scn1a R 613 X/R 613 X mice. Mixed background: WT, n = 4; Scn1a WT/R 613 X T , n = 4; Scn1a R 613 X/R 613 X , n = 2. 129S1/SvImJ background: WT, n = 4; Scn1a WT/R 613 X , n = 4. (D) Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. Kilodaltons = kDa. (E) Quantification of Na V 1.1 protein level was based on multiple bands as indicated by the black arrow in panel (D) . Only two of the three Scn1a R 613 X/R 613 X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in panels (C,E) utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in panel (C) utilized t -test. * p < 0.05, ** p < 0.01, *** p < 0.001.
    Figure Legend Snippet: Reduced Scn1a mRNA and Na V 1.1 protein expression in the hippocampus of Scn1a WT/R 613 X mice. (A) Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R 613 X allele. (B,C) qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R 613 X on the mixed background (B) , and on the pure 129S1/SvImJ background (C) . Marginal background expression was found in homozygous Scn1a R 613 X/R 613 X mice. Mixed background: WT, n = 4; Scn1a WT/R 613 X T , n = 4; Scn1a R 613 X/R 613 X , n = 2. 129S1/SvImJ background: WT, n = 4; Scn1a WT/R 613 X , n = 4. (D) Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. Kilodaltons = kDa. (E) Quantification of Na V 1.1 protein level was based on multiple bands as indicated by the black arrow in panel (D) . Only two of the three Scn1a R 613 X/R 613 X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in panels (C,E) utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in panel (C) utilized t -test. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Techniques Used: Expressing, Sequencing, Western Blot

    Reduced Scn1a mRNA and Na V 1.1 protein expression in the cortex of Scn1a WT/R 613 X mice. (A–C) Allele-specific quantification of Scn1a transcripts via dPCR. The R613X and WT Scn1a alleles were quantified with Affinity Plus probes on dPCR and normalized to mouse Gapdh levels. (A) Cortical tissue from WT mice showed no detectable levels of the R613X allele transcript, demonstrating the specificity of allelic discrimination using this assay. (B) In cortical tissue from Scn1a WT/R 613 X mice, the WT Scn1a allele is at 48.8% compared to WT cortical tissue. (C) Shown as the ratio of R613X to WT alleles, the mean steady-state level of the Scn1a R613X allele is at 8.9 ± 0.9% of the WT allele in Scn1a WT/R 613 X animals. WT, n = 6; Scn1a WT/R 613 X , n = 6. (D–F) Cortical levels of Na V 1.1 proteins were quantified using the Meso Scale Discovery Electrochemiluminescence (MSD-ECL) assay. (D) The standard curve was generated by mixing P60 WT cortical and liver proteins at different ratios. The resulting 2nd order polynomial fit, depicted as a solid line ( R 2 = 0.9924) was used to calculate protein levels relative to P60 WT cortex in panels (E,F) . (E) Na V 1.1 protein expression in the whole cortex. (F) Na V 1.1 protein expression in the parietal, temporal, frontal, and occipital lobes of the neocortex of WT and Scn1a WT / R 613 X mice. (G) The same data from panel (F) , but normalized to Na V 1.1 expression in WT mice. WT, n = 4; Scn1a WT/R613X , n = 4. Statistical comparison using mixed model ANOVA followed by Holm–Sidak, to account for analyses of different neocortical sections from each mouse. ** p < 0.01, *** p < 0.001, **** p < 0.0001.
    Figure Legend Snippet: Reduced Scn1a mRNA and Na V 1.1 protein expression in the cortex of Scn1a WT/R 613 X mice. (A–C) Allele-specific quantification of Scn1a transcripts via dPCR. The R613X and WT Scn1a alleles were quantified with Affinity Plus probes on dPCR and normalized to mouse Gapdh levels. (A) Cortical tissue from WT mice showed no detectable levels of the R613X allele transcript, demonstrating the specificity of allelic discrimination using this assay. (B) In cortical tissue from Scn1a WT/R 613 X mice, the WT Scn1a allele is at 48.8% compared to WT cortical tissue. (C) Shown as the ratio of R613X to WT alleles, the mean steady-state level of the Scn1a R613X allele is at 8.9 ± 0.9% of the WT allele in Scn1a WT/R 613 X animals. WT, n = 6; Scn1a WT/R 613 X , n = 6. (D–F) Cortical levels of Na V 1.1 proteins were quantified using the Meso Scale Discovery Electrochemiluminescence (MSD-ECL) assay. (D) The standard curve was generated by mixing P60 WT cortical and liver proteins at different ratios. The resulting 2nd order polynomial fit, depicted as a solid line ( R 2 = 0.9924) was used to calculate protein levels relative to P60 WT cortex in panels (E,F) . (E) Na V 1.1 protein expression in the whole cortex. (F) Na V 1.1 protein expression in the parietal, temporal, frontal, and occipital lobes of the neocortex of WT and Scn1a WT / R 613 X mice. (G) The same data from panel (F) , but normalized to Na V 1.1 expression in WT mice. WT, n = 4; Scn1a WT/R613X , n = 4. Statistical comparison using mixed model ANOVA followed by Holm–Sidak, to account for analyses of different neocortical sections from each mouse. ** p < 0.01, *** p < 0.001, **** p < 0.0001.

    Techniques Used: Expressing, Electrochemiluminescence, Generated

    antibody rabbit anti gaba a α1 receptor  (Alomone Labs)


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    Alomone Labs antibody rabbit anti gaba a α1 receptor
    Antibody Rabbit Anti Gaba A α1 Receptor, 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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    anti kcnj1  (Alomone Labs)


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    Alomone Labs anti kcnj1
    Assessment of mitoK ATP potassium pore expression. ( A ) Representative images of western blots. ( B ) Quantification of bands illustrates similar cardiac mitochondrial protein expression between WT and TG SUR2A−55 of <t>ROMK</t> and CCDC51. Data normalized to COXIV expression. Data presented as the means + SEMs. n = 4/group NS = not significant.
    Anti Kcnj1, 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 "Overexpression of a Short Sulfonylurea Splice Variant Increases Cardiac Glucose Uptake and Uncouples Mitochondria by Regulating ROMK Activity"

    Article Title: Overexpression of a Short Sulfonylurea Splice Variant Increases Cardiac Glucose Uptake and Uncouples Mitochondria by Regulating ROMK Activity

    Journal: Life

    doi: 10.3390/life13041015

    Assessment of mitoK ATP potassium pore expression. ( A ) Representative images of western blots. ( B ) Quantification of bands illustrates similar cardiac mitochondrial protein expression between WT and TG SUR2A−55 of ROMK and CCDC51. Data normalized to COXIV expression. Data presented as the means + SEMs. n = 4/group NS = not significant.
    Figure Legend Snippet: Assessment of mitoK ATP potassium pore expression. ( A ) Representative images of western blots. ( B ) Quantification of bands illustrates similar cardiac mitochondrial protein expression between WT and TG SUR2A−55 of ROMK and CCDC51. Data normalized to COXIV expression. Data presented as the means + SEMs. n = 4/group NS = not significant.

    Techniques Used: Expressing, Western Blot

    Δψm in isolated cardiomyocytes from WT and TGSUR2A-55 mice treated with or without a ROMK inhibitor ( A ) Δψm during ROMK inhibitor or vehicle perfusion. ( B ) Confocal images of vehicle or ROMK inhibitor treated isolated adult mouse cardiomyocytes stained with TMRE at baseline and after FCCP perfusion at 20× magnification. ( C ) Cumulative data of TMRE fluorescence relative to baseline (F/F o ) of vehicle or ROMK inhibitor treated cardiomyocytes during 10 μM FCCP perfusion. ( D ) Summary data from ( C ) at end FCCP perfusion. Only cells determined to be alive by morphology (not shrunken) were assessed at end FCCP perfusion. Data presented as the means ± SEMs. For panel ( A ), n = 8–10 cells/group; 3 mice/group; for panel ( C ), n = 11–33 cells/group; 4 mice/group. * p < 0.05; ** p < 0.01. Data were subjected to two-way ANOVA ( A , C ) or Student’s t -test ( D ).
    Figure Legend Snippet: Δψm in isolated cardiomyocytes from WT and TGSUR2A-55 mice treated with or without a ROMK inhibitor ( A ) Δψm during ROMK inhibitor or vehicle perfusion. ( B ) Confocal images of vehicle or ROMK inhibitor treated isolated adult mouse cardiomyocytes stained with TMRE at baseline and after FCCP perfusion at 20× magnification. ( C ) Cumulative data of TMRE fluorescence relative to baseline (F/F o ) of vehicle or ROMK inhibitor treated cardiomyocytes during 10 μM FCCP perfusion. ( D ) Summary data from ( C ) at end FCCP perfusion. Only cells determined to be alive by morphology (not shrunken) were assessed at end FCCP perfusion. Data presented as the means ± SEMs. For panel ( A ), n = 8–10 cells/group; 3 mice/group; for panel ( C ), n = 11–33 cells/group; 4 mice/group. * p < 0.05; ** p < 0.01. Data were subjected to two-way ANOVA ( A , C ) or Student’s t -test ( D ).

    Techniques Used: Isolation, Staining, Fluorescence

    The influence of ROMK inhibition on Δψm in isolated adult mouse cardiomyocytes from WT and TG SUR2A−55 mice treated with diazoxide. ( A ) Confocal images of vehicle or ROMK inhibitor treated cardiomyocytes stained with TMRE at baseline, after diazoxide (100 μM) perfusion, and FCCP (10 μM) perfusion at 20× magnification. ( B ) Cumulative data of TMRE fluorescence relative to baseline (F/Fe) of vehicle or ROMK inhibitor treated cardiomyocytes after diazoxide followed by FCCP perfusion. ( C ) Summary data of TMRE florescence after diazoxide (top) and FCCP perfusion (bottom). Data presented as the means ± SEMs. n = 16–30 cells/group; 4 mice/group. * p < 0.05; ** p < 0.01. Data were subjected to two-way ANOVA ( B ) or Student’s I-test ( C ).
    Figure Legend Snippet: The influence of ROMK inhibition on Δψm in isolated adult mouse cardiomyocytes from WT and TG SUR2A−55 mice treated with diazoxide. ( A ) Confocal images of vehicle or ROMK inhibitor treated cardiomyocytes stained with TMRE at baseline, after diazoxide (100 μM) perfusion, and FCCP (10 μM) perfusion at 20× magnification. ( B ) Cumulative data of TMRE fluorescence relative to baseline (F/Fe) of vehicle or ROMK inhibitor treated cardiomyocytes after diazoxide followed by FCCP perfusion. ( C ) Summary data of TMRE florescence after diazoxide (top) and FCCP perfusion (bottom). Data presented as the means ± SEMs. n = 16–30 cells/group; 4 mice/group. * p < 0.05; ** p < 0.01. Data were subjected to two-way ANOVA ( B ) or Student’s I-test ( C ).

    Techniques Used: Inhibition, Isolation, Staining, Fluorescence

    The effect of ROMK inhibition on Δψm in WT and TG SUR2A−55 mice isolated cardiac mitochondria. ( A , B ) show representative experiments of Δψm measured by rhodamine 123 fluorescence in isolated mitochondria from WT and TG SUR2A−55 mouse hearts treated with vehicle or ROMK inhibitor and then 3000 μM ATP. Graphs are normalized to florescence after the addition of FCCP. ( C ) Summary data of Δψm after ROMK inhibitor treatment vs. vehicle and response to ATP. In the scatter box plots, boxes cover the 25–75% range of data with the median as a line. n = 4 mice/group, * p < 0.05, ** p < 0.001.
    Figure Legend Snippet: The effect of ROMK inhibition on Δψm in WT and TG SUR2A−55 mice isolated cardiac mitochondria. ( A , B ) show representative experiments of Δψm measured by rhodamine 123 fluorescence in isolated mitochondria from WT and TG SUR2A−55 mouse hearts treated with vehicle or ROMK inhibitor and then 3000 μM ATP. Graphs are normalized to florescence after the addition of FCCP. ( C ) Summary data of Δψm after ROMK inhibitor treatment vs. vehicle and response to ATP. In the scatter box plots, boxes cover the 25–75% range of data with the median as a line. n = 4 mice/group, * p < 0.05, ** p < 0.001.

    Techniques Used: Inhibition, Isolation, Fluorescence

    rabbit antibestrophin 1  (Alomone Labs)


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    Alomone Labs rabbit antibestrophin 1
    Rabbit Antibestrophin 1, 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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    rabbit lrrc8a  (Alomone Labs)


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    Alomone Labs rabbit lrrc8a
    Rabbit Lrrc8a, 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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    sodium channel alpha subunit 1  (Alomone Labs)


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    Alomone Labs sodium channel alpha subunit 1
    Targeting construct and generation of global Scn1a knockout rats. (A) The arrows show the position of the genotyping primer set (forward 5′-TAATAACTTTTAATGCTATC-3′, reverse 5′-CTTCCCAGCTTCCAAGTCAC-3′). Genotype analysis shows a 272 bp band in the wild-type allele and a 178 bp band in the Scn 1 a em1kyo mutant. The upper band of the Scn 1 a em1kyo mutant is nonspecific. Genotypes are indicated by +/+ for wild-type, +/– for heterozygous, and –/– for homozygous animals. (B) Western blotting of brain membrane proteins from wild-type (+/+), heterozygous (+/–), and homozygous (–/–) Scn1a rats at P13 using an anti- voltage-gated sodium channel alpha <t>subunit</t> <t>1</t> (Na V 1.1) antibody. β-actin was used as the internal control. Original blots/gels are presented in . (C) Relative Na V 1.1 protein levels normalized to β-actin. (D) Survival curves of wild-type ( n = 15), Scn 1 a + /− ( n =15), and Scn 1 a −/− ( n = 20) rats. Scn 1 a −/− rats exhibited ataxia and seizures from postnatal day (P) 10, gradually progressing to weight loss and complete loss of postural control. They became inactive and did not survive beyond P18. In wild-type and Scn 1 a + /− rats, there were no spontaneous deaths. (E) Body weight curves of wild-type (blue circle), Scn 1 a + /− (red square), and Scn 1 a −/− (black triangle) rats. The sample size is shown below the graph. Scn 1 a + /− rats showed no difference in body weight compared to wild-type rats. Data are presented as mean ± standard deviation. (F) Ictal electroencephalography (EEG) recording of heat-induced seizures from Scn 1 a + /− rats at P21. Spiking activity was recorded, and generalized tonic-clonic seizures were observed. Open triangle indicates seizure onset. Asterisk indicates the expanded EEG trace of spiking activity. (G) Representative interictal EEG recordings from wild-type and Scn 1 a + /− rats at P21. No interictal epileptic discharge was found.
    Sodium Channel Alpha Subunit 1, 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 "Developmental changes in brain activity of heterozygous Scn1a knockout rats"

    Article Title: Developmental changes in brain activity of heterozygous Scn1a knockout rats

    Journal: Frontiers in Neurology

    doi: 10.3389/fneur.2023.1125089

    Targeting construct and generation of global Scn1a knockout rats. (A) The arrows show the position of the genotyping primer set (forward 5′-TAATAACTTTTAATGCTATC-3′, reverse 5′-CTTCCCAGCTTCCAAGTCAC-3′). Genotype analysis shows a 272 bp band in the wild-type allele and a 178 bp band in the Scn 1 a em1kyo mutant. The upper band of the Scn 1 a em1kyo mutant is nonspecific. Genotypes are indicated by +/+ for wild-type, +/– for heterozygous, and –/– for homozygous animals. (B) Western blotting of brain membrane proteins from wild-type (+/+), heterozygous (+/–), and homozygous (–/–) Scn1a rats at P13 using an anti- voltage-gated sodium channel alpha subunit 1 (Na V 1.1) antibody. β-actin was used as the internal control. Original blots/gels are presented in . (C) Relative Na V 1.1 protein levels normalized to β-actin. (D) Survival curves of wild-type ( n = 15), Scn 1 a + /− ( n =15), and Scn 1 a −/− ( n = 20) rats. Scn 1 a −/− rats exhibited ataxia and seizures from postnatal day (P) 10, gradually progressing to weight loss and complete loss of postural control. They became inactive and did not survive beyond P18. In wild-type and Scn 1 a + /− rats, there were no spontaneous deaths. (E) Body weight curves of wild-type (blue circle), Scn 1 a + /− (red square), and Scn 1 a −/− (black triangle) rats. The sample size is shown below the graph. Scn 1 a + /− rats showed no difference in body weight compared to wild-type rats. Data are presented as mean ± standard deviation. (F) Ictal electroencephalography (EEG) recording of heat-induced seizures from Scn 1 a + /− rats at P21. Spiking activity was recorded, and generalized tonic-clonic seizures were observed. Open triangle indicates seizure onset. Asterisk indicates the expanded EEG trace of spiking activity. (G) Representative interictal EEG recordings from wild-type and Scn 1 a + /− rats at P21. No interictal epileptic discharge was found.
    Figure Legend Snippet: Targeting construct and generation of global Scn1a knockout rats. (A) The arrows show the position of the genotyping primer set (forward 5′-TAATAACTTTTAATGCTATC-3′, reverse 5′-CTTCCCAGCTTCCAAGTCAC-3′). Genotype analysis shows a 272 bp band in the wild-type allele and a 178 bp band in the Scn 1 a em1kyo mutant. The upper band of the Scn 1 a em1kyo mutant is nonspecific. Genotypes are indicated by +/+ for wild-type, +/– for heterozygous, and –/– for homozygous animals. (B) Western blotting of brain membrane proteins from wild-type (+/+), heterozygous (+/–), and homozygous (–/–) Scn1a rats at P13 using an anti- voltage-gated sodium channel alpha subunit 1 (Na V 1.1) antibody. β-actin was used as the internal control. Original blots/gels are presented in . (C) Relative Na V 1.1 protein levels normalized to β-actin. (D) Survival curves of wild-type ( n = 15), Scn 1 a + /− ( n =15), and Scn 1 a −/− ( n = 20) rats. Scn 1 a −/− rats exhibited ataxia and seizures from postnatal day (P) 10, gradually progressing to weight loss and complete loss of postural control. They became inactive and did not survive beyond P18. In wild-type and Scn 1 a + /− rats, there were no spontaneous deaths. (E) Body weight curves of wild-type (blue circle), Scn 1 a + /− (red square), and Scn 1 a −/− (black triangle) rats. The sample size is shown below the graph. Scn 1 a + /− rats showed no difference in body weight compared to wild-type rats. Data are presented as mean ± standard deviation. (F) Ictal electroencephalography (EEG) recording of heat-induced seizures from Scn 1 a + /− rats at P21. Spiking activity was recorded, and generalized tonic-clonic seizures were observed. Open triangle indicates seizure onset. Asterisk indicates the expanded EEG trace of spiking activity. (G) Representative interictal EEG recordings from wild-type and Scn 1 a + /− rats at P21. No interictal epileptic discharge was found.

    Techniques Used: Construct, Knock-Out, Mutagenesis, Western Blot, Standard Deviation, Activity Assay

    anti nav1 1 antibody  (Alomone Labs)


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    Alomone Labs anti nav1 1 antibody
    Histological and biochemical assessment of neurodegeneration, localization of human or phosphorylated tau within inhibitory interneurons, and expression of <t>Nav1.1</t> protein (A and B) Immunohistochemistry for GABA (red) and human tau (HT7, green in A) or phosphorylated tau (AT8, green in B) in the somatosensory cortex. Asterisks indicate GABA + cells. Scale bars: 10 μm. See also <xref ref-type=Figure S4 . (C) Immunohistochemistry for NeuN, GABA, and PV in the somatosensory cortex. Scale bars: 50 μm. (D–F) The number of NeuN (D), GABA (E), or PV (F) –positive cells in the field of view (FOV) (N = six male mice for each genotype). (G and H) Western blot for Nav1.1 and β-actin. The intensity of the Nav1.1-ir bands is normalized to that of the β-actin-ir bands and shown as relative values to the mean value in non-Tg mice (N = four mice for each genotype) in (H). (I) Immunohistochemistry for Kv3.1b (green), PV (red), and NeuN (blue) in the somatosensory cortex. Scale bars: 30 μm. (J) Mean intensity of perisomatic Kv3.1b in PV + cells at age 6 months (N = six mice for each genotype). Data are shown as mean ± S.E.M. p value ( ∗∗ p< 0.01) by the Student’s t test. " width="250" height="auto" />
    Anti Nav1 1 Antibody, 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 "Selective dysfunction of fast-spiking inhibitory interneurons and disruption of perineuronal nets in a tauopathy mouse model"

    Article Title: Selective dysfunction of fast-spiking inhibitory interneurons and disruption of perineuronal nets in a tauopathy mouse model

    Journal: iScience

    doi: 10.1016/j.isci.2023.106342

    Histological and biochemical assessment of neurodegeneration, localization of human or phosphorylated tau within inhibitory interneurons, and expression of Nav1.1 protein (A and B) Immunohistochemistry for GABA (red) and human tau (HT7, green in A) or phosphorylated tau (AT8, green in B) in the somatosensory cortex. Asterisks indicate GABA + cells. Scale bars: 10 μm. See also <xref ref-type=Figure S4 . (C) Immunohistochemistry for NeuN, GABA, and PV in the somatosensory cortex. Scale bars: 50 μm. (D–F) The number of NeuN (D), GABA (E), or PV (F) –positive cells in the field of view (FOV) (N = six male mice for each genotype). (G and H) Western blot for Nav1.1 and β-actin. The intensity of the Nav1.1-ir bands is normalized to that of the β-actin-ir bands and shown as relative values to the mean value in non-Tg mice (N = four mice for each genotype) in (H). (I) Immunohistochemistry for Kv3.1b (green), PV (red), and NeuN (blue) in the somatosensory cortex. Scale bars: 30 μm. (J) Mean intensity of perisomatic Kv3.1b in PV + cells at age 6 months (N = six mice for each genotype). Data are shown as mean ± S.E.M. p value ( ∗∗ p< 0.01) by the Student’s t test. " title="... phosphorylated tau within inhibitory interneurons, and expression of Nav1.1 protein (A and B) Immunohistochemistry for GABA (red) ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Histological and biochemical assessment of neurodegeneration, localization of human or phosphorylated tau within inhibitory interneurons, and expression of Nav1.1 protein (A and B) Immunohistochemistry for GABA (red) and human tau (HT7, green in A) or phosphorylated tau (AT8, green in B) in the somatosensory cortex. Asterisks indicate GABA + cells. Scale bars: 10 μm. See also Figure S4 . (C) Immunohistochemistry for NeuN, GABA, and PV in the somatosensory cortex. Scale bars: 50 μm. (D–F) The number of NeuN (D), GABA (E), or PV (F) –positive cells in the field of view (FOV) (N = six male mice for each genotype). (G and H) Western blot for Nav1.1 and β-actin. The intensity of the Nav1.1-ir bands is normalized to that of the β-actin-ir bands and shown as relative values to the mean value in non-Tg mice (N = four mice for each genotype) in (H). (I) Immunohistochemistry for Kv3.1b (green), PV (red), and NeuN (blue) in the somatosensory cortex. Scale bars: 30 μm. (J) Mean intensity of perisomatic Kv3.1b in PV + cells at age 6 months (N = six mice for each genotype). Data are shown as mean ± S.E.M. p value ( ∗∗ p< 0.01) by the Student’s t test.

    Techniques Used: Expressing, Immunohistochemistry, Western Blot


    Figure Legend Snippet:

    Techniques Used: Purification, Recombinant, Plasmid Preparation, Software

    anti na v 1 1 antibody  (Alomone Labs)


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    Alomone Labs anti na v 1 1 antibody
    A . Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R613X allele. B-C. qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R613X on the mixed background (B), as well as on the pure 129S1/SvImJ background (C). A marginal background expression was found in homozygous Scn1a R613X/R613X mice. Mixed background: WT, n=4; Scn1a WT/R613X T , n=4; Scn1a R613X/R613X , n=2. 129S1/SvImJ background: WT, n=4; Scn1a WT/R613X , n=4. D. Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. E . Quantification of Na V 1.1 protein level from D. Only two of the three Scn1a R613X/R613X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in C and E utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in C utilized t-test. *, p<0.05, **, p<0.01, ***, p<0.001.
    Anti Na V 1 1 Antibody, 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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    Images

    1) Product Images from "Heat-induced seizures, premature mortality, and hyperactivity in a novel Scn1a nonsense model for Dravet syndrome"

    Article Title: Heat-induced seizures, premature mortality, and hyperactivity in a novel Scn1a nonsense model for Dravet syndrome

    Journal: bioRxiv

    doi: 10.1101/2023.02.01.526678

    A . Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R613X allele. B-C. qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R613X on the mixed background (B), as well as on the pure 129S1/SvImJ background (C). A marginal background expression was found in homozygous Scn1a R613X/R613X mice. Mixed background: WT, n=4; Scn1a WT/R613X T , n=4; Scn1a R613X/R613X , n=2. 129S1/SvImJ background: WT, n=4; Scn1a WT/R613X , n=4. D. Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. E . Quantification of Na V 1.1 protein level from D. Only two of the three Scn1a R613X/R613X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in C and E utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in C utilized t-test. *, p<0.05, **, p<0.01, ***, p<0.001.
    Figure Legend Snippet: A . Sequencing of hippocampal mRNA confirmed the expression of the Scn1a R613X allele. B-C. qPCR analysis of Scn1a mRNA expression levels showed a significant reduction to approximately 50% in heterozygous Scn1a WT/R613X on the mixed background (B), as well as on the pure 129S1/SvImJ background (C). A marginal background expression was found in homozygous Scn1a R613X/R613X mice. Mixed background: WT, n=4; Scn1a WT/R613X T , n=4; Scn1a R613X/R613X , n=2. 129S1/SvImJ background: WT, n=4; Scn1a WT/R613X , n=4. D. Western blot analysis of Na V 1.1 protein extracted from the hippocampi of three different mice from each genotype. E . Quantification of Na V 1.1 protein level from D. Only two of the three Scn1a R613X/R613X were included in the quantification due to the dark spot in the middle lane that precluded the inclusion of this sample. Statistical comparison in C and E utilized One-Way ANOVA followed by Tukey’s multiple comparisons test. Statistical comparison in C utilized t-test. *, p<0.05, **, p<0.01, ***, p<0.001.

    Techniques Used: Sequencing, Expressing, Western Blot

    A-C. Allele-specific quantification of Scn1a transcripts via dPCR. The R613X and WT Scn1a alleles were quantified with Affinity Plus probes on dPCR and normalized to mouse Gapdh levels. A. Cortical tissue from WT mice showed no detectable levels of the R613X allele transcript, demonstrating the specificity of allelic discrimination using this assay. B. In cortical tissue from Scn1a WT/R613X mice, the WT Scn1a allele is at 48.8% compared to in WT cortical tissue. C. Shown as the ratio of R613X to WT alleles, the mean steady-state level of the Scn1a R613X allele is at 8.9±0.9% of the WT allele in Scn1a WT/R613X animals. WT, n=6; Scn1a WT/R613X , n=6. D-F. Cortical levels of Na V 1.1 proteins were quantified using the Meso Scale Discovery Electrochemiluminescence (MSD-ECL) assay. D. The standard curve was generated by mixing P60 WT cortical and liver proteins at different ratios. The resulting 2 nd order polynomial fit, depicted as a solid line (R 2 = 0.9924) was used to calculate protein levels relative to P60 WT cortex in E and F. E. Protein Na V 1.1 expression in the whole cortex. F. Na V 1.1 protein expression in the parietal, temporal, frontal, and occipital lobes of the neocortex of WT and WT/R613X mice. G. The same data from F, but normalized to Na V 1.1 expression in WT mice. WT, n=4; Scn1a WT/R613X , n=4. Statistical comparison by unpaired t-test. ***, p<0.001, ****, p<0.0001
    Figure Legend Snippet: A-C. Allele-specific quantification of Scn1a transcripts via dPCR. The R613X and WT Scn1a alleles were quantified with Affinity Plus probes on dPCR and normalized to mouse Gapdh levels. A. Cortical tissue from WT mice showed no detectable levels of the R613X allele transcript, demonstrating the specificity of allelic discrimination using this assay. B. In cortical tissue from Scn1a WT/R613X mice, the WT Scn1a allele is at 48.8% compared to in WT cortical tissue. C. Shown as the ratio of R613X to WT alleles, the mean steady-state level of the Scn1a R613X allele is at 8.9±0.9% of the WT allele in Scn1a WT/R613X animals. WT, n=6; Scn1a WT/R613X , n=6. D-F. Cortical levels of Na V 1.1 proteins were quantified using the Meso Scale Discovery Electrochemiluminescence (MSD-ECL) assay. D. The standard curve was generated by mixing P60 WT cortical and liver proteins at different ratios. The resulting 2 nd order polynomial fit, depicted as a solid line (R 2 = 0.9924) was used to calculate protein levels relative to P60 WT cortex in E and F. E. Protein Na V 1.1 expression in the whole cortex. F. Na V 1.1 protein expression in the parietal, temporal, frontal, and occipital lobes of the neocortex of WT and WT/R613X mice. G. The same data from F, but normalized to Na V 1.1 expression in WT mice. WT, n=4; Scn1a WT/R613X , n=4. Statistical comparison by unpaired t-test. ***, p<0.001, ****, p<0.0001

    Techniques Used: Electrochemiluminescence, Generated, Expressing

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