rabbit polyclonal anti ca v 1 2  (Alomone Labs)


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    Alomone Labs rabbit polyclonal anti ca v 1 2
    (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.
    Rabbit Polyclonal Anti Ca V 1 2, 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/rabbit polyclonal anti ca v 1 2/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Images

    1) Product Images from "Aging impairs the clustering and reduces the activity of L-type calcium channels in cardiac pacemaker cells"

    Article Title: Aging impairs the clustering and reduces the activity of L-type calcium channels in cardiac pacemaker cells

    Journal: bioRxiv

    doi: 10.1101/2022.06.22.497267

    (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.
    Figure Legend Snippet: (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.

    Techniques Used: Western Blot, Expressing, MANN-WHITNEY, Labeling

    (A, B) Representative super-resolution (GSD) images of Ca V 1.2 and Ca V 1.3 channels in young and old pacemaker cells. Panels to the right of each image are zoom in. (C) Average cluster area for Ca V 1.2 and Ca V 1.3 channel clusters in young and old pacemaker cells. (D) Comparison of Ca V 1.2 and Ca V 1.3 cluster density between young and old cells. (E , F) Comparison of the frequency distributions of the area of Ca V 1.2 and Ca V 1.3 channel clusters between young and old cells. In all the scattered plots bars represent the mean and error bars the SEM. Statistical comparisons used a two-tail t-test comparing a population of n = 8 cells, N = 3 mice for Ca V 1.2 young; n = 12 cells, N = 4 mice for Ca V 1.3 young; n = 6 cells, N = 3 mice for Ca V 1.2 old; and n = 8 cells, N = 3 mice for Ca V 1.3 old.
    Figure Legend Snippet: (A, B) Representative super-resolution (GSD) images of Ca V 1.2 and Ca V 1.3 channels in young and old pacemaker cells. Panels to the right of each image are zoom in. (C) Average cluster area for Ca V 1.2 and Ca V 1.3 channel clusters in young and old pacemaker cells. (D) Comparison of Ca V 1.2 and Ca V 1.3 cluster density between young and old cells. (E , F) Comparison of the frequency distributions of the area of Ca V 1.2 and Ca V 1.3 channel clusters between young and old cells. In all the scattered plots bars represent the mean and error bars the SEM. Statistical comparisons used a two-tail t-test comparing a population of n = 8 cells, N = 3 mice for Ca V 1.2 young; n = 12 cells, N = 4 mice for Ca V 1.3 young; n = 6 cells, N = 3 mice for Ca V 1.2 old; and n = 8 cells, N = 3 mice for Ca V 1.3 old.

    Techniques Used:

    rabbit polyclonal anti ca v 1 2  (Alomone Labs)


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    Alomone Labs rabbit polyclonal anti ca v 1 2
    (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.
    Rabbit Polyclonal Anti Ca V 1 2, 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/rabbit polyclonal anti ca v 1 2/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti ca v 1 2 - by Bioz Stars, 2023-01
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    Images

    1) Product Images from "Aging impairs the clustering and reduces the activity of L-type calcium channels in cardiac pacemaker cells"

    Article Title: Aging impairs the clustering and reduces the activity of L-type calcium channels in cardiac pacemaker cells

    Journal: bioRxiv

    doi: 10.1101/2022.06.22.497267

    (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.
    Figure Legend Snippet: (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.

    Techniques Used: Western Blot, Expressing, MANN-WHITNEY, Labeling

    (A, B) Representative super-resolution (GSD) images of Ca V 1.2 and Ca V 1.3 channels in young and old pacemaker cells. Panels to the right of each image are zoom in. (C) Average cluster area for Ca V 1.2 and Ca V 1.3 channel clusters in young and old pacemaker cells. (D) Comparison of Ca V 1.2 and Ca V 1.3 cluster density between young and old cells. (E , F) Comparison of the frequency distributions of the area of Ca V 1.2 and Ca V 1.3 channel clusters between young and old cells. In all the scattered plots bars represent the mean and error bars the SEM. Statistical comparisons used a two-tail t-test comparing a population of n = 8 cells, N = 3 mice for Ca V 1.2 young; n = 12 cells, N = 4 mice for Ca V 1.3 young; n = 6 cells, N = 3 mice for Ca V 1.2 old; and n = 8 cells, N = 3 mice for Ca V 1.3 old.
    Figure Legend Snippet: (A, B) Representative super-resolution (GSD) images of Ca V 1.2 and Ca V 1.3 channels in young and old pacemaker cells. Panels to the right of each image are zoom in. (C) Average cluster area for Ca V 1.2 and Ca V 1.3 channel clusters in young and old pacemaker cells. (D) Comparison of Ca V 1.2 and Ca V 1.3 cluster density between young and old cells. (E , F) Comparison of the frequency distributions of the area of Ca V 1.2 and Ca V 1.3 channel clusters between young and old cells. In all the scattered plots bars represent the mean and error bars the SEM. Statistical comparisons used a two-tail t-test comparing a population of n = 8 cells, N = 3 mice for Ca V 1.2 young; n = 12 cells, N = 4 mice for Ca V 1.3 young; n = 6 cells, N = 3 mice for Ca V 1.2 old; and n = 8 cells, N = 3 mice for Ca V 1.3 old.

    Techniques Used:

    rabbit polyclonal antibodies against gat 1  (Alomone Labs)


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    Alomone Labs rabbit polyclonal antibodies against gat 1
    Rabbit Polyclonal Antibodies Against Gat 1, 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/rabbit polyclonal antibodies against gat 1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    rabbit polyclonal antibodies against gat 1  (Alomone Labs)


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    Alomone Labs rabbit polyclonal antibodies against gat 1
    (A). Schematic representation of <t>GAT-1</t> protein topology and locations of GAT-1 variants previously identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. Val125Met (V125M) is located at the 3rd transmembrane helix of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. (B) Pedigree and the genotype. A missense mutation was found in the proband and the half-sister but not in the rest of the family members. (C). Amino acid sequence homology shows that valine (V) at residue 125 is highly conserved in SCL6A1 in humans (Accession NO.NP_003033.3) and across species as shown in boxed region.
    Rabbit Polyclonal Antibodies Against Gat 1, 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/rabbit polyclonal antibodies against gat 1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal antibodies against gat 1 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Genetic mosaicism, intrafamilial phenotypic heterogeneity, and molecular defects of a novel missense SLC6A1 mutation associated with epilepsy and ADHD"

    Article Title: Genetic mosaicism, intrafamilial phenotypic heterogeneity, and molecular defects of a novel missense SLC6A1 mutation associated with epilepsy and ADHD

    Journal: Experimental neurology

    doi: 10.1016/j.expneurol.2021.113723

    (A). Schematic representation of GAT-1 protein topology and locations of GAT-1 variants previously identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. Val125Met (V125M) is located at the 3rd transmembrane helix of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. (B) Pedigree and the genotype. A missense mutation was found in the proband and the half-sister but not in the rest of the family members. (C). Amino acid sequence homology shows that valine (V) at residue 125 is highly conserved in SCL6A1 in humans (Accession NO.NP_003033.3) and across species as shown in boxed region.
    Figure Legend Snippet: (A). Schematic representation of GAT-1 protein topology and locations of GAT-1 variants previously identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. Val125Met (V125M) is located at the 3rd transmembrane helix of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. (B) Pedigree and the genotype. A missense mutation was found in the proband and the half-sister but not in the rest of the family members. (C). Amino acid sequence homology shows that valine (V) at residue 125 is highly conserved in SCL6A1 in humans (Accession NO.NP_003033.3) and across species as shown in boxed region.

    Techniques Used: Mutagenesis, Sequencing

    (A-B). Tertiary structures of both the wildtype (A) and Val125Met mutant (B) GAT-1 protein are predicted by I-TASSER and DynaMut. The valine at residue 125 is mutated to methionine, both highlighted in light green, alongside with the surrounding residues. The interatomic interactions were predicted by DynaMut, where halogen bonds are depicted in blue and hydrogen bonds are colored in red. The Val125Met mutation results in the addition of sulfur into the sidechain, not causing drastic changes in polarity and charge, but making the protein less hydrophobic. (C). Machine learning tools predicted ΔΔG (Kcal/mol) of the mutant GAT-1(Val125Met) protein. Bars in the positive direction are predicted as stabilizing while bars in the negative direction are predicted as destabilizing.
    Figure Legend Snippet: (A-B). Tertiary structures of both the wildtype (A) and Val125Met mutant (B) GAT-1 protein are predicted by I-TASSER and DynaMut. The valine at residue 125 is mutated to methionine, both highlighted in light green, alongside with the surrounding residues. The interatomic interactions were predicted by DynaMut, where halogen bonds are depicted in blue and hydrogen bonds are colored in red. The Val125Met mutation results in the addition of sulfur into the sidechain, not causing drastic changes in polarity and charge, but making the protein less hydrophobic. (C). Machine learning tools predicted ΔΔG (Kcal/mol) of the mutant GAT-1(Val125Met) protein. Bars in the positive direction are predicted as stabilizing while bars in the negative direction are predicted as destabilizing.

    Techniques Used: Mutagenesis

    A-B. HEK293T cells or mouse cortical astrocytes were transfected with wildtype GAT-1YFP (wt), or the mutant GAT-1(Val125Met, V125M)YFP cDNAs (1μg per a 35mm2 dish) for 48 hrs before 3H radioactive GABA uptake assay. C. Mouse cortical neurons were transfected with the wildtype or the mutant GAT-1(Val125Met) cDNAs at day 7 in culture. 3H radioactive GABA uptake assay was performed after 8 days of transfection. GABA flux was measured after 30 min transport at room temperature. The influx of GABA, expressed in pmol/μg protein/min, was averaged from duplicates for each condition and for each transfection. The average counting was taken as n = 1. The untransfected condition was taken as baseline flux, which was subtracted from both the wildtype and the mutant conditions in HEK293T cells (A). The pmol/μg protein/min in the mutant was then normalized to the wildtype from each experiment, which was arbitrarily set as 100%. (***p < 0.01 vs. wt, n=4-7 different transfections). Cl-966 (100μm) was applied 30 min before preincubation and removed during preincubation. (One-sample t test. Values were expressed as mean ± S.E.M).
    Figure Legend Snippet: A-B. HEK293T cells or mouse cortical astrocytes were transfected with wildtype GAT-1YFP (wt), or the mutant GAT-1(Val125Met, V125M)YFP cDNAs (1μg per a 35mm2 dish) for 48 hrs before 3H radioactive GABA uptake assay. C. Mouse cortical neurons were transfected with the wildtype or the mutant GAT-1(Val125Met) cDNAs at day 7 in culture. 3H radioactive GABA uptake assay was performed after 8 days of transfection. GABA flux was measured after 30 min transport at room temperature. The influx of GABA, expressed in pmol/μg protein/min, was averaged from duplicates for each condition and for each transfection. The average counting was taken as n = 1. The untransfected condition was taken as baseline flux, which was subtracted from both the wildtype and the mutant conditions in HEK293T cells (A). The pmol/μg protein/min in the mutant was then normalized to the wildtype from each experiment, which was arbitrarily set as 100%. (***p < 0.01 vs. wt, n=4-7 different transfections). Cl-966 (100μm) was applied 30 min before preincubation and removed during preincubation. (One-sample t test. Values were expressed as mean ± S.E.M).

    Techniques Used: Transfection, Mutagenesis

    A, B. HEK293T cells were transfected with wildtype GAT-1YFP (wt), or the mutant GAT-1(Val125Met, V125M)YFP cDNAs (3μg/60 mm2) for 48 hrs. The cells (A) were either harvested directly after wash with PBS for total lysates or followed by cell surface biotinylation to isolate the cell surface bound proteins (B). The total lysates (A) or isolated surface protein (B) were then analyzed by SDS-PAGE. Membranes were immunoblotted with rabbit anti-GAT-1 (1:300). (C). The total protein integrated density values (IDVs) from the total lysates (C) or isolated cell surface protein (D) were measured. The abundance of the mutant GAT-1(Val125Met) transporter was normalized to the wildtype cells expressing GAT-1YFP. In C, the total protein abundance was measured by adding up all the bands between 90-110 KDa. The total protein IDVs of either the wildtype or the mutant was normalized to its loading control. The abundance of the mutant transporter was then normalized to the wildtype. (**p < 0.01; ***p < 0.001 vs. wt, n=4 different transfections, One-sample t test, Values were expressed as mean ± S.E.M).
    Figure Legend Snippet: A, B. HEK293T cells were transfected with wildtype GAT-1YFP (wt), or the mutant GAT-1(Val125Met, V125M)YFP cDNAs (3μg/60 mm2) for 48 hrs. The cells (A) were either harvested directly after wash with PBS for total lysates or followed by cell surface biotinylation to isolate the cell surface bound proteins (B). The total lysates (A) or isolated surface protein (B) were then analyzed by SDS-PAGE. Membranes were immunoblotted with rabbit anti-GAT-1 (1:300). (C). The total protein integrated density values (IDVs) from the total lysates (C) or isolated cell surface protein (D) were measured. The abundance of the mutant GAT-1(Val125Met) transporter was normalized to the wildtype cells expressing GAT-1YFP. In C, the total protein abundance was measured by adding up all the bands between 90-110 KDa. The total protein IDVs of either the wildtype or the mutant was normalized to its loading control. The abundance of the mutant transporter was then normalized to the wildtype. (**p < 0.01; ***p < 0.001 vs. wt, n=4 different transfections, One-sample t test, Values were expressed as mean ± S.E.M).

    Techniques Used: Transfection, Mutagenesis, Isolation, SDS Page, Expressing

    (A) HEK293T cells were transfected with wildtype GAT-1YFP or the mutant GAT-1(Val125Met, V125M)YFP with the pECFP-ER marker (ERCFP) at 2:1 ratio (2 μg:1μg cDNAs) for 48 hrs. Live cells were examined under a confocal microscopy with excitation at 458 nm for CFP, 514 nm for YFP. All images were single confocal sections averaged from 8 times to reduce noise, except when otherwise specified. (B) The GAT-1YFP fluorescence overlapping with ERCFP fluorescence was quantified by Metamorph with colocalization percentage. Tu stands for Tunicamycin (10 μg/ml) treated for 16 hrs. (***p < 0.001 V125M vs. wt, V125M §§ vs wt+Tun. N=7-8 representative fields from 4 different transfections. One-way analysis of variance (ANOVA) and Newman-Keuls test was used to determine significance compared to the wt condition and between mutation and wt+Tu. Values were expressed as mean ± S.E.M).
    Figure Legend Snippet: (A) HEK293T cells were transfected with wildtype GAT-1YFP or the mutant GAT-1(Val125Met, V125M)YFP with the pECFP-ER marker (ERCFP) at 2:1 ratio (2 μg:1μg cDNAs) for 48 hrs. Live cells were examined under a confocal microscopy with excitation at 458 nm for CFP, 514 nm for YFP. All images were single confocal sections averaged from 8 times to reduce noise, except when otherwise specified. (B) The GAT-1YFP fluorescence overlapping with ERCFP fluorescence was quantified by Metamorph with colocalization percentage. Tu stands for Tunicamycin (10 μg/ml) treated for 16 hrs. (***p < 0.001 V125M vs. wt, V125M §§ vs wt+Tun. N=7-8 representative fields from 4 different transfections. One-way analysis of variance (ANOVA) and Newman-Keuls test was used to determine significance compared to the wt condition and between mutation and wt+Tu. Values were expressed as mean ± S.E.M).

    Techniques Used: Transfection, Mutagenesis, Marker, Confocal Microscopy, Fluorescence

    anti aeg 1  (Alomone Labs)


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    Alomone Labs anti aeg 1
    Anti Aeg 1, 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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    Average 94 stars, based on 1 article reviews
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    anti aeg 1 - by Bioz Stars, 2023-01
    94/100 stars

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    rabbit polyclonal antibodies against gat 1  (Alomone Labs)


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    Alomone Labs rabbit polyclonal antibodies against gat 1
    <t>GABA</t> <t>transporter</t> <t>1</t> <t>(GAT-1)</t> protein topology, mutations and identification of a novel SLC6A1 missense mutation GAT1(P361T). a. Schematic representation of GAT-1 protein topology and locations of GAT-1 variants previously identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. P361 is located at the extracellular loop between the 7th and 8th transmembrane helices of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. b Pedigree and the genotype. A missense mutation was only found in the proband but not in the rest of the family members. c Chromatogram of PCR-Sanger sequencing. DNA sequences of the proband and the immediate family members were shown. Arrow indicated a C-to-A transversion. d Amino acid sequence homology shows that proline (P) at residue 361 is highly conserved in SCL6A1 in humans (Accession NO.NP_003033.3) and across species as shown in boxed region
    Rabbit Polyclonal Antibodies Against Gat 1, 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/rabbit polyclonal antibodies against gat 1/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal antibodies against gat 1 - by Bioz Stars, 2023-01
    94/100 stars

    Images

    1) Product Images from "Endoplasmic reticulum retention and degradation of a mutation in SLC6A1 associated with epilepsy and autism"

    Article Title: Endoplasmic reticulum retention and degradation of a mutation in SLC6A1 associated with epilepsy and autism

    Journal: Molecular Brain

    doi: 10.1186/s13041-020-00612-6

    GABA transporter 1 (GAT-1) protein topology, mutations and identification of a novel SLC6A1 missense mutation GAT1(P361T). a. Schematic representation of GAT-1 protein topology and locations of GAT-1 variants previously identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. P361 is located at the extracellular loop between the 7th and 8th transmembrane helices of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. b Pedigree and the genotype. A missense mutation was only found in the proband but not in the rest of the family members. c Chromatogram of PCR-Sanger sequencing. DNA sequences of the proband and the immediate family members were shown. Arrow indicated a C-to-A transversion. d Amino acid sequence homology shows that proline (P) at residue 361 is highly conserved in SCL6A1 in humans (Accession NO.NP_003033.3) and across species as shown in boxed region
    Figure Legend Snippet: GABA transporter 1 (GAT-1) protein topology, mutations and identification of a novel SLC6A1 missense mutation GAT1(P361T). a. Schematic representation of GAT-1 protein topology and locations of GAT-1 variants previously identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. P361 is located at the extracellular loop between the 7th and 8th transmembrane helices of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. b Pedigree and the genotype. A missense mutation was only found in the proband but not in the rest of the family members. c Chromatogram of PCR-Sanger sequencing. DNA sequences of the proband and the immediate family members were shown. Arrow indicated a C-to-A transversion. d Amino acid sequence homology shows that proline (P) at residue 361 is highly conserved in SCL6A1 in humans (Accession NO.NP_003033.3) and across species as shown in boxed region

    Techniques Used: Mutagenesis, Sequencing

    Modeling of the mutant GAT-1 protein with machine learning tools. a-b . Tertiary structures of both the wildtype ( a ) and P361T mutant ( b ) GAT-1 protein are predicted by I-TASSER and DynaMut. The proline at residue 361 is mutated to threonine, both highlighted in light green, alongside with the surrounding residues. The interatomic interactions were predicted by DynaMut, where halogen bonds are depicted in blue and hydrogen bonds are colored in red. The P361T mutation results in the loss of two hydrogen bonds, those between residues 361 and 365 (yellow arrow with red border) and between 361 and 364 (yellow arrow with blue border). This supports the result in Table that this mutation destabilized the global conformation of the GAT-1 protein. c . Machine learning tools predicted ΔΔG (Kcal/mol) of the mutant GAT-1 protein. Bars in the positive direction are predicted as stabilizing while bars in the negative direction are predicted as destabilizing
    Figure Legend Snippet: Modeling of the mutant GAT-1 protein with machine learning tools. a-b . Tertiary structures of both the wildtype ( a ) and P361T mutant ( b ) GAT-1 protein are predicted by I-TASSER and DynaMut. The proline at residue 361 is mutated to threonine, both highlighted in light green, alongside with the surrounding residues. The interatomic interactions were predicted by DynaMut, where halogen bonds are depicted in blue and hydrogen bonds are colored in red. The P361T mutation results in the loss of two hydrogen bonds, those between residues 361 and 365 (yellow arrow with red border) and between 361 and 364 (yellow arrow with blue border). This supports the result in Table that this mutation destabilized the global conformation of the GAT-1 protein. c . Machine learning tools predicted ΔΔG (Kcal/mol) of the mutant GAT-1 protein. Bars in the positive direction are predicted as stabilizing while bars in the negative direction are predicted as destabilizing

    Techniques Used: Mutagenesis

    Electroencephalogram (EEG) of a 6-year-old girl carrying GAT-1(P361T) mutation. Interictal video EEG recordings showed 2.5–3.0 Hz generalized spike and slow waves ( a ), 2.0–3.0 Hz spike and slow waves in the bilateral prefrontal lobes ( b ) and 2.0–3.0 Hz slow waves predominantly in the bilateral occipital area ( c ) during both wakefulness and sleep when the patient was 3.5 years old. Interictal video EEG recordings demonstrated 2.0–3.0 Hz spike and slow waves in the bilateral prefrontal lobes ( d ), and 2.0–3.0 Hz spike and slow waves predominantly in the bilateral occipital and posterior-temporal area ( e ) during both wakefulness and sleep when the patient was 6 years old
    Figure Legend Snippet: Electroencephalogram (EEG) of a 6-year-old girl carrying GAT-1(P361T) mutation. Interictal video EEG recordings showed 2.5–3.0 Hz generalized spike and slow waves ( a ), 2.0–3.0 Hz spike and slow waves in the bilateral prefrontal lobes ( b ) and 2.0–3.0 Hz slow waves predominantly in the bilateral occipital area ( c ) during both wakefulness and sleep when the patient was 3.5 years old. Interictal video EEG recordings demonstrated 2.0–3.0 Hz spike and slow waves in the bilateral prefrontal lobes ( d ), and 2.0–3.0 Hz spike and slow waves predominantly in the bilateral occipital and posterior-temporal area ( e ) during both wakefulness and sleep when the patient was 6 years old

    Techniques Used: Mutagenesis

    The expression of the mutant of GAT-1(P361T) protein was reduced in non-neuronal cells and neurons. a-b. Mouse cortical neurons were transfected with the wildtype or the mutant GAT-1(P361T) cDNAs at day 7 in culture. The total lysates were harvested from mouse cortical neurons expressing the wildtype GAT-1 YFP (wt) or mutant GAT-1(P361T) YFP transporters after 8 days of transfection ( a ). HeLa cells were transfected with the wildtype GAT-1 YFP (wt) or mutant GAT-1(P361T) YFP transporters for 48 h ( b ). The total lysates were then analyzed by SDS-PAGE. Membranes were immunoblotted with rabbit anti-GAT-1 for both neuronal and HeLa cell lysates (1:200). In neurons, the protein band of endogenous GAT-1, at 67 KDa, was intense. The main protein bands run at 108 KDa in both the wildtype and the mutant conditions, representing the YFP-tagged GAT-1. c . The total protein integrated density values (IDVs) were measured. The abundance of the mutant GAT-1(P361T) transporter was normalized to the wildtype condition. In c , the total protein abundance was measured by adding up all the bands between 90 and 110 KDa. The total protein IDVs of either the wildtype or the mutant was normalized to its loading control. The abundance of the mutant transporter was then normalized to the wildtype. (* p < 0.05 vs wt in HeLa; ** p < 0.01 vs. wt in Neuron, n = 4–5 different transfections)
    Figure Legend Snippet: The expression of the mutant of GAT-1(P361T) protein was reduced in non-neuronal cells and neurons. a-b. Mouse cortical neurons were transfected with the wildtype or the mutant GAT-1(P361T) cDNAs at day 7 in culture. The total lysates were harvested from mouse cortical neurons expressing the wildtype GAT-1 YFP (wt) or mutant GAT-1(P361T) YFP transporters after 8 days of transfection ( a ). HeLa cells were transfected with the wildtype GAT-1 YFP (wt) or mutant GAT-1(P361T) YFP transporters for 48 h ( b ). The total lysates were then analyzed by SDS-PAGE. Membranes were immunoblotted with rabbit anti-GAT-1 for both neuronal and HeLa cell lysates (1:200). In neurons, the protein band of endogenous GAT-1, at 67 KDa, was intense. The main protein bands run at 108 KDa in both the wildtype and the mutant conditions, representing the YFP-tagged GAT-1. c . The total protein integrated density values (IDVs) were measured. The abundance of the mutant GAT-1(P361T) transporter was normalized to the wildtype condition. In c , the total protein abundance was measured by adding up all the bands between 90 and 110 KDa. The total protein IDVs of either the wildtype or the mutant was normalized to its loading control. The abundance of the mutant transporter was then normalized to the wildtype. (* p < 0.05 vs wt in HeLa; ** p < 0.01 vs. wt in Neuron, n = 4–5 different transfections)

    Techniques Used: Expressing, Mutagenesis, Transfection, SDS Page

    There was reduced YFP fluorescence in cells expressing the mutant GAT-1(P361T) transporters, which were retained inside the endoplasmic reticulum. a HEK293T cells were transfected with wildtype GAT-1 YFP or the mutant GAT-1(P361T) YFP with the pECFP-ER marker (ER CFP ) at 2:1 ratio (2 μg:1 μg cDNAs) for 48 h. Live cells were examined under a confocal microscopy with excitation at 458 nm for CFP, 514 nm for YFP. All images were single confocal sections averaged from 8 times to reduce noise, except when otherwise specified. b The GAT-1 YFP fluorescence overlapping with ER CFP fluorescence was quantified by Metamorph with colocalization percentage. (*** p < 0.001 P361T vs. wt, §§ p < 0.01 wt + Tunicamycin vs wt untreated, n = 5–9 representative fields from different transfections)
    Figure Legend Snippet: There was reduced YFP fluorescence in cells expressing the mutant GAT-1(P361T) transporters, which were retained inside the endoplasmic reticulum. a HEK293T cells were transfected with wildtype GAT-1 YFP or the mutant GAT-1(P361T) YFP with the pECFP-ER marker (ER CFP ) at 2:1 ratio (2 μg:1 μg cDNAs) for 48 h. Live cells were examined under a confocal microscopy with excitation at 458 nm for CFP, 514 nm for YFP. All images were single confocal sections averaged from 8 times to reduce noise, except when otherwise specified. b The GAT-1 YFP fluorescence overlapping with ER CFP fluorescence was quantified by Metamorph with colocalization percentage. (*** p < 0.001 P361T vs. wt, §§ p < 0.01 wt + Tunicamycin vs wt untreated, n = 5–9 representative fields from different transfections)

    Techniques Used: Fluorescence, Expressing, Mutagenesis, Transfection, Marker, Confocal Microscopy

    Impaired GABA uptake of the mutant GAT-1(P361T) transporters. ( A ) HEK293T cells were transfected with wildtype GAT-1 YFP (wt), or the mutant GAT-1(P361T) YFP cDNAs (1 μg/35mm 2 ) for 48 h. The GABA uptake assay was carried out with 3 H radioactive labeling in HEK 293 T cells. GABA flux was measured after 30 min transport at room temperature. The influx of GABA, expressed in pmol/μg protein/min, was averaged from duplicates for each condition and for each transfection. The average counting was taken as n = 1. The untransfected condition was taken as baseline flux, which was subtracted from both the wild-type and the mutant conditions. The pmol/μg protein/min in the mutant was then normalized to the wildtype from each experiment, which was arbitrarily set as 100%. (** p < 0.01 vs. wt, n = 4–5 different transfections)
    Figure Legend Snippet: Impaired GABA uptake of the mutant GAT-1(P361T) transporters. ( A ) HEK293T cells were transfected with wildtype GAT-1 YFP (wt), or the mutant GAT-1(P361T) YFP cDNAs (1 μg/35mm 2 ) for 48 h. The GABA uptake assay was carried out with 3 H radioactive labeling in HEK 293 T cells. GABA flux was measured after 30 min transport at room temperature. The influx of GABA, expressed in pmol/μg protein/min, was averaged from duplicates for each condition and for each transfection. The average counting was taken as n = 1. The untransfected condition was taken as baseline flux, which was subtracted from both the wild-type and the mutant conditions. The pmol/μg protein/min in the mutant was then normalized to the wildtype from each experiment, which was arbitrarily set as 100%. (** p < 0.01 vs. wt, n = 4–5 different transfections)

    Techniques Used: Mutagenesis, Transfection, Labeling

    polyclonal rabbit anti na v 1 9  (Alomone Labs)


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    Alomone Labs polyclonal rabbit anti na v 1 9
    a – c Current-clamp recordings show that HpTx1 decreases the membrane excitability of small DRG neurons from Na v 1.9-KO mice. a Bars show no significant changes in RMP (left, n = 29) or AP amplitude (right, n = 25), but a significant increase in rheobase (middle, n = 25, nonparametric Wilcoxon matched-pair signed-rank two-tailed test: P = 0.008) in the presence of 0.75 μM HpTx1. b AP traces recorded from a representative small Na v 1.9-KO DRG neuron before (black) and after (red) application of 0.75 μM HpTx1. The dashed lines indicate 0 mV. c Statistics plots show significant decreases in AP spike number in the presence of 0.75 μM HpTx1 ( n = 25, two-way repeated measures ANOVA followed by Bonferroni’s multiple comparisons test, treatment × inject current: F (7,168) = 8.834, P < 0.0001; treatment: F (1,24) = 25.49, #### P < 0.0001; inject current: F (7,168) = 25.28, P < 0.0001). d Comparison of nocifensive behaviors (licking or biting) following intraplantar injection of vehicle (10 μl 0.9% saline, n = 6) versus HpTx1 (1 μM or 10 μM in 10 μl saline, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 8.551, P = 0.0012; treatment: F (2,30) = 11.04, P = 0.0003; genotype: F (1,30) = 24.37, P < 0.0001). e Mechanical response thresholds measured in paws in response to vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) injections (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 18.68, P < 0.0001; treatment: F (2,30) = 0.0356, P = 0.9651; genotype: F (1,30) = 67.3, P < 0.0001). f Latency of WD to noxious heat stimuli measured after intraplantar injection of vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 44.54, P < 0.0001; treatment: F (2,30) = 9.701, P = 0.0006; genotype: F (1,30) = 113.5, P < 0.0001). All DRG neurons recorded were held at −53 ± 2 mV. Data are presented as the mean ± S.E.M. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Exact P ( c – f ) are presented in Supplementary Data  . Source data are provided as a  .   .
    Polyclonal Rabbit Anti Na V 1 9, 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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    Images

    1) Product Images from "Spider venom-derived peptide induces hyperalgesia in Na v 1.7 knockout mice by activating Na v 1.9 channels"

    Article Title: Spider venom-derived peptide induces hyperalgesia in Na v 1.7 knockout mice by activating Na v 1.9 channels

    Journal: Nature Communications

    doi: 10.1038/s41467-020-16210-y

    a – c Current-clamp recordings show that HpTx1 decreases the membrane excitability of small DRG neurons from Na v 1.9-KO mice. a Bars show no significant changes in RMP (left, n = 29) or AP amplitude (right, n = 25), but a significant increase in rheobase (middle, n = 25, nonparametric Wilcoxon matched-pair signed-rank two-tailed test: P = 0.008) in the presence of 0.75 μM HpTx1. b AP traces recorded from a representative small Na v 1.9-KO DRG neuron before (black) and after (red) application of 0.75 μM HpTx1. The dashed lines indicate 0 mV. c Statistics plots show significant decreases in AP spike number in the presence of 0.75 μM HpTx1 ( n = 25, two-way repeated measures ANOVA followed by Bonferroni’s multiple comparisons test, treatment × inject current: F (7,168) = 8.834, P < 0.0001; treatment: F (1,24) = 25.49, #### P < 0.0001; inject current: F (7,168) = 25.28, P < 0.0001). d Comparison of nocifensive behaviors (licking or biting) following intraplantar injection of vehicle (10 μl 0.9% saline, n = 6) versus HpTx1 (1 μM or 10 μM in 10 μl saline, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 8.551, P = 0.0012; treatment: F (2,30) = 11.04, P = 0.0003; genotype: F (1,30) = 24.37, P < 0.0001). e Mechanical response thresholds measured in paws in response to vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) injections (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 18.68, P < 0.0001; treatment: F (2,30) = 0.0356, P = 0.9651; genotype: F (1,30) = 67.3, P < 0.0001). f Latency of WD to noxious heat stimuli measured after intraplantar injection of vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 44.54, P < 0.0001; treatment: F (2,30) = 9.701, P = 0.0006; genotype: F (1,30) = 113.5, P < 0.0001). All DRG neurons recorded were held at −53 ± 2 mV. Data are presented as the mean ± S.E.M. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Exact P ( c – f ) are presented in Supplementary Data  . Source data are provided as a  .   .
    Figure Legend Snippet: a – c Current-clamp recordings show that HpTx1 decreases the membrane excitability of small DRG neurons from Na v 1.9-KO mice. a Bars show no significant changes in RMP (left, n = 29) or AP amplitude (right, n = 25), but a significant increase in rheobase (middle, n = 25, nonparametric Wilcoxon matched-pair signed-rank two-tailed test: P = 0.008) in the presence of 0.75 μM HpTx1. b AP traces recorded from a representative small Na v 1.9-KO DRG neuron before (black) and after (red) application of 0.75 μM HpTx1. The dashed lines indicate 0 mV. c Statistics plots show significant decreases in AP spike number in the presence of 0.75 μM HpTx1 ( n = 25, two-way repeated measures ANOVA followed by Bonferroni’s multiple comparisons test, treatment × inject current: F (7,168) = 8.834, P < 0.0001; treatment: F (1,24) = 25.49, #### P < 0.0001; inject current: F (7,168) = 25.28, P < 0.0001). d Comparison of nocifensive behaviors (licking or biting) following intraplantar injection of vehicle (10 μl 0.9% saline, n = 6) versus HpTx1 (1 μM or 10 μM in 10 μl saline, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 8.551, P = 0.0012; treatment: F (2,30) = 11.04, P = 0.0003; genotype: F (1,30) = 24.37, P < 0.0001). e Mechanical response thresholds measured in paws in response to vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) injections (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 18.68, P < 0.0001; treatment: F (2,30) = 0.0356, P = 0.9651; genotype: F (1,30) = 67.3, P < 0.0001). f Latency of WD to noxious heat stimuli measured after intraplantar injection of vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 44.54, P < 0.0001; treatment: F (2,30) = 9.701, P = 0.0006; genotype: F (1,30) = 113.5, P < 0.0001). All DRG neurons recorded were held at −53 ± 2 mV. Data are presented as the mean ± S.E.M. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Exact P ( c – f ) are presented in Supplementary Data . Source data are provided as a . .

    Techniques Used: Two Tailed Test, Injection

    a Sequence alignments corresponding to the DIV s3b-s4 region of Na v subtypes. The highlighted sequences show the regions swapped between Na v 1.8 and Na v 1.9. b Representative current traces from Na v 1.9/1.8 DIV s3b-s4 P1 (top) and Na v 1.8/1.9 DIV s3b-s4 P1 (bottom) chimaera channels in the absence (black) and presence (red) of HpTx1. c Effects of HpTx1 on WT and mutant hNa v 1.9 channels. Dot plots display the effect of 0.75 μM HpTx1 on the peak current (top, n = 14 for WT; n = 4 for T1444L, M1445L, I1446F, and T1448A; n = 5 for L1449I and E1450L; n = 3 for N1451K) and the persistent current (bottom, n = 14 for WT; n = 4 for T1444L, I1446F, T1448A, and N1451K; n = 5 for M1445L, L1449I, and E1450L). Key residues involved in the interaction between HpTx1 and hNa v 1.9 are labeled (one-way ANOVA with Dunnett’s multiple comparison test, I 95 /I peak : F (7,35) = 17.72, P < 0.0001; I/I max : F (7,38) = 8.157, P < 0.0001). d (top) Sequence alignments corresponding to the DII s3b-s4 region of Na v subtypes. The highlighted sequences show the regions swapped between Na v 1.7 and Na v 1.8. Representative current traces from Na v 1.7/1.8 DII s3b-s4 (bottom left) and Na v 1.8/1.7 DII s3b-s4 (bottom right) chimaera channels in the absence (black) or presence of 5 μM HpTx1 (red). e Dose-dependent inhibitory curves show the effect of HpTx1 on WT ( n = 7) and mutant hNa v 1.7 channels ( n = 4 for F813S, n = 6 for L814A and A815S, n = 3 for D816K, n = 6 for V817K, n = 7 for E818G, n = 4 for E818R, n = 5 for G819S and n = 3 for Na v 1.7/1.8 DII s3b-s4) and the Na v 1.8/1.7 DII s3b-s4 chimaera channel ( n = 5). f Bars show the fold changes in IC 50 values of HpTx1 for mutant channels compared with that for the WT hNa v 1.7 channel. Data are presented as the mean ± S.E.M. Exact P ( c ) are presented in Supplementary Data  . Source data are provided as a  .   .
    Figure Legend Snippet: a Sequence alignments corresponding to the DIV s3b-s4 region of Na v subtypes. The highlighted sequences show the regions swapped between Na v 1.8 and Na v 1.9. b Representative current traces from Na v 1.9/1.8 DIV s3b-s4 P1 (top) and Na v 1.8/1.9 DIV s3b-s4 P1 (bottom) chimaera channels in the absence (black) and presence (red) of HpTx1. c Effects of HpTx1 on WT and mutant hNa v 1.9 channels. Dot plots display the effect of 0.75 μM HpTx1 on the peak current (top, n = 14 for WT; n = 4 for T1444L, M1445L, I1446F, and T1448A; n = 5 for L1449I and E1450L; n = 3 for N1451K) and the persistent current (bottom, n = 14 for WT; n = 4 for T1444L, I1446F, T1448A, and N1451K; n = 5 for M1445L, L1449I, and E1450L). Key residues involved in the interaction between HpTx1 and hNa v 1.9 are labeled (one-way ANOVA with Dunnett’s multiple comparison test, I 95 /I peak : F (7,35) = 17.72, P < 0.0001; I/I max : F (7,38) = 8.157, P < 0.0001). d (top) Sequence alignments corresponding to the DII s3b-s4 region of Na v subtypes. The highlighted sequences show the regions swapped between Na v 1.7 and Na v 1.8. Representative current traces from Na v 1.7/1.8 DII s3b-s4 (bottom left) and Na v 1.8/1.7 DII s3b-s4 (bottom right) chimaera channels in the absence (black) or presence of 5 μM HpTx1 (red). e Dose-dependent inhibitory curves show the effect of HpTx1 on WT ( n = 7) and mutant hNa v 1.7 channels ( n = 4 for F813S, n = 6 for L814A and A815S, n = 3 for D816K, n = 6 for V817K, n = 7 for E818G, n = 4 for E818R, n = 5 for G819S and n = 3 for Na v 1.7/1.8 DII s3b-s4) and the Na v 1.8/1.7 DII s3b-s4 chimaera channel ( n = 5). f Bars show the fold changes in IC 50 values of HpTx1 for mutant channels compared with that for the WT hNa v 1.7 channel. Data are presented as the mean ± S.E.M. Exact P ( c ) are presented in Supplementary Data . Source data are provided as a . .

    Techniques Used: Sequencing, Mutagenesis, Labeling

    rabbit polyclonal antibodies against gat 1  (Alomone Labs)


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    Alomone Labs rabbit polyclonal antibodies against gat 1
    (A) Schematic representation of <t>GAT-1</t> protein topology and locations of GAT-1 variants identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. G234S is located at the junction of the second intracellular loop and the 5th transmembrane domain of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. (B) Amino acid sequence homology shows that glycine (G) at residue 234 is highly conserved in SCL6A1 in human (Accession NO. NP_003033.3) and across species. (C) Tertiary structures of both the wildtype and G234S mutant protein GAT-1 are predicted by I-TASSER. Residue 234 is highlighted as red and Glycine is mutated to Serine. (D) From interatomic interactions predictions by DynaMut, wild-type (upper) and G234S mutation (bottom) residues are colored in light-green and are also represented as sticks alongside with the surrounding residues. Halogen bonds are depicted in blue. Hydrogen bonds are colored in red. Machine learning methods as Supplementary Table 1 predicted this mutation destabilized the global conformation of the GAT-1 protein.
    Rabbit Polyclonal Antibodies Against Gat 1, 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 "A missense mutation in SLC6A1 associated with Lennox-Gastaut syndrome impairs GABA transporter 1 protein trafficking and function"

    Article Title: A missense mutation in SLC6A1 associated with Lennox-Gastaut syndrome impairs GABA transporter 1 protein trafficking and function

    Journal: Experimental neurology

    doi: 10.1016/j.expneurol.2019.112973

    (A) Schematic representation of GAT-1 protein topology and locations of GAT-1 variants identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. G234S is located at the junction of the second intracellular loop and the 5th transmembrane domain of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. (B) Amino acid sequence homology shows that glycine (G) at residue 234 is highly conserved in SCL6A1 in human (Accession NO. NP_003033.3) and across species. (C) Tertiary structures of both the wildtype and G234S mutant protein GAT-1 are predicted by I-TASSER. Residue 234 is highlighted as red and Glycine is mutated to Serine. (D) From interatomic interactions predictions by DynaMut, wild-type (upper) and G234S mutation (bottom) residues are colored in light-green and are also represented as sticks alongside with the surrounding residues. Halogen bonds are depicted in blue. Hydrogen bonds are colored in red. Machine learning methods as Supplementary Table 1 predicted this mutation destabilized the global conformation of the GAT-1 protein.
    Figure Legend Snippet: (A) Schematic representation of GAT-1 protein topology and locations of GAT-1 variants identified in patients associated with a spectrum of epilepsy syndromes. It is predicted that GAT-1 contains 12 transmembrane domains. G234S is located at the junction of the second intracellular loop and the 5th transmembrane domain of the GAT-1 protein. The positions of variants are based on the published LeuT crystal structure. (B) Amino acid sequence homology shows that glycine (G) at residue 234 is highly conserved in SCL6A1 in human (Accession NO. NP_003033.3) and across species. (C) Tertiary structures of both the wildtype and G234S mutant protein GAT-1 are predicted by I-TASSER. Residue 234 is highlighted as red and Glycine is mutated to Serine. (D) From interatomic interactions predictions by DynaMut, wild-type (upper) and G234S mutation (bottom) residues are colored in light-green and are also represented as sticks alongside with the surrounding residues. Halogen bonds are depicted in blue. Hydrogen bonds are colored in red. Machine learning methods as Supplementary Table 1 predicted this mutation destabilized the global conformation of the GAT-1 protein.

    Techniques Used: Sequencing, Mutagenesis

    A-B. HEK293T cells were transfected with GAT-1YFP (3μg) for 48 hrs. (A) Total lysates were analyzed by SDS-PAGE and western blot. The membranes were blotted with mouse anti-GFP antibody. (B) Rat cortical neurons were transfected with the wildtype or the mutant GAT-1(G234S)YFP cDNAs at day 7 days old in cultured dish. The total lysates were harvested from rat cortical neurons expressing the wildtype GAT-1YFP (wt) or mutant GAT-1(G234S)YFP (G234S) transporters after 8 days of transfection. The total lysates were then analyzed by SDS-PAGE. In HEK 293T cells (A), three protein bands were detected in both the wildtype and the mutant conditions. In rat cortical neurons (B), only a single strong band was detected in both the wildtype and the mutant conditions. In A and B, 1:500 means the ratio of the GFP antibody in buffer (1μg of GFP in 500 μl 1XPBS). (C, D). The total protein integrated density values (IDVs) were measured. The abundance of the mutant (GAT-1(G234S) transporter was normalized to the wildtype condition. In C, the total protein abundance was measured by adding up all the three bands run between 90–110 KDa. In both C and D, the total protein IDVs of either the wildtype or the mutant was normalized to its loading control. The abundance of the mutant transporter was then normalized to the wildtype. (***p < 0.001 vs. wt, n=4 different transfections).
    Figure Legend Snippet: A-B. HEK293T cells were transfected with GAT-1YFP (3μg) for 48 hrs. (A) Total lysates were analyzed by SDS-PAGE and western blot. The membranes were blotted with mouse anti-GFP antibody. (B) Rat cortical neurons were transfected with the wildtype or the mutant GAT-1(G234S)YFP cDNAs at day 7 days old in cultured dish. The total lysates were harvested from rat cortical neurons expressing the wildtype GAT-1YFP (wt) or mutant GAT-1(G234S)YFP (G234S) transporters after 8 days of transfection. The total lysates were then analyzed by SDS-PAGE. In HEK 293T cells (A), three protein bands were detected in both the wildtype and the mutant conditions. In rat cortical neurons (B), only a single strong band was detected in both the wildtype and the mutant conditions. In A and B, 1:500 means the ratio of the GFP antibody in buffer (1μg of GFP in 500 μl 1XPBS). (C, D). The total protein integrated density values (IDVs) were measured. The abundance of the mutant (GAT-1(G234S) transporter was normalized to the wildtype condition. In C, the total protein abundance was measured by adding up all the three bands run between 90–110 KDa. In both C and D, the total protein IDVs of either the wildtype or the mutant was normalized to its loading control. The abundance of the mutant transporter was then normalized to the wildtype. (***p < 0.001 vs. wt, n=4 different transfections).

    Techniques Used: Transfection, SDS Page, Western Blot, Mutagenesis, Cell Culture, Expressing

    (A) The flow cytometry histograms depict surface expression levels of GAT-1 from HEK293T cells were transfected with wildtype GAT-1YFP (wt), or the mutant GAT-1(G234S)YFP cDNAs or control (insert). Cell surface wild type and mutant GAT-1 stained with polyclonal anti-GAT-1 antibody that was fluorescently conjugated with Alexa Fluor-555. (B) Surface protein was isolated by biotinylating live cells expressing wildtype GAT-1YFP (wt), or the mutant GAT-1(G234S)YFP and analyzed by SDS-PAGE. The membranes were visualized by polyclonal anti-GAT-1 protein. (C) The normalized relative fluorescence intensity (FI) (C) or the surface protein intensity values (IDVs) (D) were normalized to those obtained with wildtype GAT-1 while the FI or protein IDVs in the wildtype was arbitrarily taken as 1 in each experiment (***p < 0.001 vs. wt, n=4 different transfections). (E). The GABA uptake assay was carried out with 3H radioactive GABA transport in HeLa cells transiently expressing the wildtype or the mutant GAT-1YFP for 48 hrs. GABA flux was measured after 15 min transport at room temperature (**p < 0.01 vs. wt, n=6 for wildtype and 7 for the mutant which represents number of transfections).
    Figure Legend Snippet: (A) The flow cytometry histograms depict surface expression levels of GAT-1 from HEK293T cells were transfected with wildtype GAT-1YFP (wt), or the mutant GAT-1(G234S)YFP cDNAs or control (insert). Cell surface wild type and mutant GAT-1 stained with polyclonal anti-GAT-1 antibody that was fluorescently conjugated with Alexa Fluor-555. (B) Surface protein was isolated by biotinylating live cells expressing wildtype GAT-1YFP (wt), or the mutant GAT-1(G234S)YFP and analyzed by SDS-PAGE. The membranes were visualized by polyclonal anti-GAT-1 protein. (C) The normalized relative fluorescence intensity (FI) (C) or the surface protein intensity values (IDVs) (D) were normalized to those obtained with wildtype GAT-1 while the FI or protein IDVs in the wildtype was arbitrarily taken as 1 in each experiment (***p < 0.001 vs. wt, n=4 different transfections). (E). The GABA uptake assay was carried out with 3H radioactive GABA transport in HeLa cells transiently expressing the wildtype or the mutant GAT-1YFP for 48 hrs. GABA flux was measured after 15 min transport at room temperature (**p < 0.01 vs. wt, n=6 for wildtype and 7 for the mutant which represents number of transfections).

    Techniques Used: Flow Cytometry, Expressing, Transfection, Mutagenesis, Staining, Isolation, SDS Page, Fluorescence

    gat 1  (Alomone Labs)


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    Alomone Labs gat 1
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    anti gat1  (Alomone Labs)


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    Alomone Labs anti gat1
    Primary antibodies used in this study
    Anti Gat1, 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 "Sex- and age-related changes in GABA signaling components in the human cortex"

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    Journal: Biology of Sex Differences

    doi: 10.1186/s13293-018-0214-6

    Primary antibodies used in this study
    Figure Legend Snippet: Primary antibodies used in this study

    Techniques Used: Concentration Assay, Recombinant, Purification

    Western blot against human brain protein homogenates probed with GABA A receptor α1, α2, α3, α5, β3, and γ2 subunit, GAT1, GAT3, GAD65 and GAD67 and GABA B R R2 subunit antibodies. Each lane has 20 μg of protein loaded. Observed band sizes: α1, α2: ~ 52 kDa; α3, α5: ~ 55 kDa; β3: ~ 63 kDa; γ2: ~ 44 kDa; GAT1: ~ 85 kDa, GAT3: ~ 80 kDa; GABA B R R2: ~ 120 kDa
    Figure Legend Snippet: Western blot against human brain protein homogenates probed with GABA A receptor α1, α2, α3, α5, β3, and γ2 subunit, GAT1, GAT3, GAD65 and GAD67 and GABA B R R2 subunit antibodies. Each lane has 20 μg of protein loaded. Observed band sizes: α1, α2: ~ 52 kDa; α3, α5: ~ 55 kDa; β3: ~ 63 kDa; γ2: ~ 44 kDa; GAT1: ~ 85 kDa, GAT3: ~ 80 kDa; GABA B R R2: ~ 120 kDa

    Techniques Used: Western Blot

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) sensory cortex homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Signal intensity for each GABA signaling component Western blot band was measured and normalized to their corresponding β-actin signal for each age group. The data is graphed as mean ± SEM ( n = 6; Kruskal-Wallis test; p * < 0.05)
    Figure Legend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) sensory cortex homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Signal intensity for each GABA signaling component Western blot band was measured and normalized to their corresponding β-actin signal for each age group. The data is graphed as mean ± SEM ( n = 6; Kruskal-Wallis test; p * < 0.05)

    Techniques Used: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) motor cortex homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details
    Figure Legend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) motor cortex homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Techniques Used: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) cerebellum homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details
    Figure Legend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) cerebellum homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Techniques Used: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) inferior temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details
    Figure Legend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) inferior temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Techniques Used: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) medial temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details
    Figure Legend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) medial temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Techniques Used: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) superior temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details
    Figure Legend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) superior temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Techniques Used: Western Blot, Incubation

    agt 001  (Alomone Labs)


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    Alomone Labs rabbit polyclonal anti ca v 1 2
    (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.
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    (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.
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    (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.
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    a – c Current-clamp recordings show that HpTx1 decreases the membrane excitability of small DRG neurons from Na v 1.9-KO mice. a Bars show no significant changes in RMP (left, n = 29) or AP amplitude (right, n = 25), but a significant increase in rheobase (middle, n = 25, nonparametric Wilcoxon matched-pair signed-rank two-tailed test: P = 0.008) in the presence of 0.75 μM HpTx1. b AP traces recorded from a representative small Na v 1.9-KO DRG neuron before (black) and after (red) application of 0.75 μM HpTx1. The dashed lines indicate 0 mV. c Statistics plots show significant decreases in AP spike number in the presence of 0.75 μM HpTx1 ( n = 25, two-way repeated measures ANOVA followed by Bonferroni’s multiple comparisons test, treatment × inject current: F (7,168) = 8.834, P < 0.0001; treatment: F (1,24) = 25.49, #### P < 0.0001; inject current: F (7,168) = 25.28, P < 0.0001). d Comparison of nocifensive behaviors (licking or biting) following intraplantar injection of vehicle (10 μl 0.9% saline, n = 6) versus HpTx1 (1 μM or 10 μM in 10 μl saline, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 8.551, P = 0.0012; treatment: F (2,30) = 11.04, P = 0.0003; genotype: F (1,30) = 24.37, P < 0.0001). e Mechanical response thresholds measured in paws in response to vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) injections (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 18.68, P < 0.0001; treatment: F (2,30) = 0.0356, P = 0.9651; genotype: F (1,30) = 67.3, P < 0.0001). f Latency of WD to noxious heat stimuli measured after intraplantar injection of vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 44.54, P < 0.0001; treatment: F (2,30) = 9.701, P = 0.0006; genotype: F (1,30) = 113.5, P < 0.0001). All DRG neurons recorded were held at −53 ± 2 mV. Data are presented as the mean ± S.E.M. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Exact P ( c – f ) are presented in Supplementary Data  . Source data are provided as a  .   .
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    Alomone Labs gat 1
    a – c Current-clamp recordings show that HpTx1 decreases the membrane excitability of small DRG neurons from Na v 1.9-KO mice. a Bars show no significant changes in RMP (left, n = 29) or AP amplitude (right, n = 25), but a significant increase in rheobase (middle, n = 25, nonparametric Wilcoxon matched-pair signed-rank two-tailed test: P = 0.008) in the presence of 0.75 μM HpTx1. b AP traces recorded from a representative small Na v 1.9-KO DRG neuron before (black) and after (red) application of 0.75 μM HpTx1. The dashed lines indicate 0 mV. c Statistics plots show significant decreases in AP spike number in the presence of 0.75 μM HpTx1 ( n = 25, two-way repeated measures ANOVA followed by Bonferroni’s multiple comparisons test, treatment × inject current: F (7,168) = 8.834, P < 0.0001; treatment: F (1,24) = 25.49, #### P < 0.0001; inject current: F (7,168) = 25.28, P < 0.0001). d Comparison of nocifensive behaviors (licking or biting) following intraplantar injection of vehicle (10 μl 0.9% saline, n = 6) versus HpTx1 (1 μM or 10 μM in 10 μl saline, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 8.551, P = 0.0012; treatment: F (2,30) = 11.04, P = 0.0003; genotype: F (1,30) = 24.37, P < 0.0001). e Mechanical response thresholds measured in paws in response to vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) injections (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 18.68, P < 0.0001; treatment: F (2,30) = 0.0356, P = 0.9651; genotype: F (1,30) = 67.3, P < 0.0001). f Latency of WD to noxious heat stimuli measured after intraplantar injection of vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 44.54, P < 0.0001; treatment: F (2,30) = 9.701, P = 0.0006; genotype: F (1,30) = 113.5, P < 0.0001). All DRG neurons recorded were held at −53 ± 2 mV. Data are presented as the mean ± S.E.M. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Exact P ( c – f ) are presented in Supplementary Data  . Source data are provided as a  .   .
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    Primary antibodies used in this study
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    Image Search Results


    (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.

    Journal: bioRxiv

    Article Title: Aging impairs the clustering and reduces the activity of L-type calcium channels in cardiac pacemaker cells

    doi: 10.1101/2022.06.22.497267

    Figure Lengend Snippet: (A) Representative western blots for Ca V 1.2 and Ca V 1.3 channels and total protein stains from pacemaker tissue explants from young and old mice. (B) Fold change of Ca V 1.2 and Ca V 1.3 channel total expression in old animals relative to young. Expression was normalized to total protein and each data point represents an animal. Statistical comparisons used a two-tail Mann-Whitney test. (C-F) Small insets to the right are representative AiryScan high-resolution images of the footprint of young and old pacemaker cells labeled against Ca V 1.2 (magenta) or Ca V 1.3 (orange). Magnified panels to the left are 5 by 5 µm footprint regions from each of the cells shown to the right. (G) Comparison of Ca V 1.2 and Ca V 1.3 particle density between young (Ca V 1.2, n = 22, N = 3; Ca V 1.3, n = 16, N = 3) and old (Ca V 1.2, n= 33, N = 3; Ca V 1.3, n = 23, N = 3) cells. Statistical comparisons used a two-tail t-test.

    Article Snippet: Cells were immunostained using the following antibodies: rabbit polyclonal anti-Ca V 1.2 (anti-CNC1), rabbit polyclonal Ca V 1.3 (anti-CND1), guinea pig anti-HCN4 (Alomone, AGP-004)).

    Techniques: Western Blot, Expressing, MANN-WHITNEY, Labeling

    (A, B) Representative super-resolution (GSD) images of Ca V 1.2 and Ca V 1.3 channels in young and old pacemaker cells. Panels to the right of each image are zoom in. (C) Average cluster area for Ca V 1.2 and Ca V 1.3 channel clusters in young and old pacemaker cells. (D) Comparison of Ca V 1.2 and Ca V 1.3 cluster density between young and old cells. (E , F) Comparison of the frequency distributions of the area of Ca V 1.2 and Ca V 1.3 channel clusters between young and old cells. In all the scattered plots bars represent the mean and error bars the SEM. Statistical comparisons used a two-tail t-test comparing a population of n = 8 cells, N = 3 mice for Ca V 1.2 young; n = 12 cells, N = 4 mice for Ca V 1.3 young; n = 6 cells, N = 3 mice for Ca V 1.2 old; and n = 8 cells, N = 3 mice for Ca V 1.3 old.

    Journal: bioRxiv

    Article Title: Aging impairs the clustering and reduces the activity of L-type calcium channels in cardiac pacemaker cells

    doi: 10.1101/2022.06.22.497267

    Figure Lengend Snippet: (A, B) Representative super-resolution (GSD) images of Ca V 1.2 and Ca V 1.3 channels in young and old pacemaker cells. Panels to the right of each image are zoom in. (C) Average cluster area for Ca V 1.2 and Ca V 1.3 channel clusters in young and old pacemaker cells. (D) Comparison of Ca V 1.2 and Ca V 1.3 cluster density between young and old cells. (E , F) Comparison of the frequency distributions of the area of Ca V 1.2 and Ca V 1.3 channel clusters between young and old cells. In all the scattered plots bars represent the mean and error bars the SEM. Statistical comparisons used a two-tail t-test comparing a population of n = 8 cells, N = 3 mice for Ca V 1.2 young; n = 12 cells, N = 4 mice for Ca V 1.3 young; n = 6 cells, N = 3 mice for Ca V 1.2 old; and n = 8 cells, N = 3 mice for Ca V 1.3 old.

    Article Snippet: Cells were immunostained using the following antibodies: rabbit polyclonal anti-Ca V 1.2 (anti-CNC1), rabbit polyclonal Ca V 1.3 (anti-CND1), guinea pig anti-HCN4 (Alomone, AGP-004)).

    Techniques:

    a – c Current-clamp recordings show that HpTx1 decreases the membrane excitability of small DRG neurons from Na v 1.9-KO mice. a Bars show no significant changes in RMP (left, n = 29) or AP amplitude (right, n = 25), but a significant increase in rheobase (middle, n = 25, nonparametric Wilcoxon matched-pair signed-rank two-tailed test: P = 0.008) in the presence of 0.75 μM HpTx1. b AP traces recorded from a representative small Na v 1.9-KO DRG neuron before (black) and after (red) application of 0.75 μM HpTx1. The dashed lines indicate 0 mV. c Statistics plots show significant decreases in AP spike number in the presence of 0.75 μM HpTx1 ( n = 25, two-way repeated measures ANOVA followed by Bonferroni’s multiple comparisons test, treatment × inject current: F (7,168) = 8.834, P < 0.0001; treatment: F (1,24) = 25.49, #### P < 0.0001; inject current: F (7,168) = 25.28, P < 0.0001). d Comparison of nocifensive behaviors (licking or biting) following intraplantar injection of vehicle (10 μl 0.9% saline, n = 6) versus HpTx1 (1 μM or 10 μM in 10 μl saline, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 8.551, P = 0.0012; treatment: F (2,30) = 11.04, P = 0.0003; genotype: F (1,30) = 24.37, P < 0.0001). e Mechanical response thresholds measured in paws in response to vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) injections (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 18.68, P < 0.0001; treatment: F (2,30) = 0.0356, P = 0.9651; genotype: F (1,30) = 67.3, P < 0.0001). f Latency of WD to noxious heat stimuli measured after intraplantar injection of vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 44.54, P < 0.0001; treatment: F (2,30) = 9.701, P = 0.0006; genotype: F (1,30) = 113.5, P < 0.0001). All DRG neurons recorded were held at −53 ± 2 mV. Data are presented as the mean ± S.E.M. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Exact P ( c – f ) are presented in Supplementary Data  . Source data are provided as a  .   .

    Journal: Nature Communications

    Article Title: Spider venom-derived peptide induces hyperalgesia in Na v 1.7 knockout mice by activating Na v 1.9 channels

    doi: 10.1038/s41467-020-16210-y

    Figure Lengend Snippet: a – c Current-clamp recordings show that HpTx1 decreases the membrane excitability of small DRG neurons from Na v 1.9-KO mice. a Bars show no significant changes in RMP (left, n = 29) or AP amplitude (right, n = 25), but a significant increase in rheobase (middle, n = 25, nonparametric Wilcoxon matched-pair signed-rank two-tailed test: P = 0.008) in the presence of 0.75 μM HpTx1. b AP traces recorded from a representative small Na v 1.9-KO DRG neuron before (black) and after (red) application of 0.75 μM HpTx1. The dashed lines indicate 0 mV. c Statistics plots show significant decreases in AP spike number in the presence of 0.75 μM HpTx1 ( n = 25, two-way repeated measures ANOVA followed by Bonferroni’s multiple comparisons test, treatment × inject current: F (7,168) = 8.834, P < 0.0001; treatment: F (1,24) = 25.49, #### P < 0.0001; inject current: F (7,168) = 25.28, P < 0.0001). d Comparison of nocifensive behaviors (licking or biting) following intraplantar injection of vehicle (10 μl 0.9% saline, n = 6) versus HpTx1 (1 μM or 10 μM in 10 μl saline, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 8.551, P = 0.0012; treatment: F (2,30) = 11.04, P = 0.0003; genotype: F (1,30) = 24.37, P < 0.0001). e Mechanical response thresholds measured in paws in response to vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) injections (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 18.68, P < 0.0001; treatment: F (2,30) = 0.0356, P = 0.9651; genotype: F (1,30) = 67.3, P < 0.0001). f Latency of WD to noxious heat stimuli measured after intraplantar injection of vehicle (black circles, n = 6), 1 μM HpTx1 (yellow squares, n = 6) or 10 μM HpTx1 (red triangles, n = 6) (two-way ANOVA followed by Tukey’s multiple comparisons test, treatment × genotype: F (2,30) = 44.54, P < 0.0001; treatment: F (2,30) = 9.701, P = 0.0006; genotype: F (1,30) = 113.5, P < 0.0001). All DRG neurons recorded were held at −53 ± 2 mV. Data are presented as the mean ± S.E.M. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. Exact P ( c – f ) are presented in Supplementary Data . Source data are provided as a . .

    Article Snippet: The sections were permeabilized in PBS containing 0.5% TritonX-100) for 10 min, and were blocked with 10% goat serum for 1 h. The sections were incubated for 24 h at 4 °C with polyclonal rabbit anti-Na v 1.9 (1:200; alomone labs).

    Techniques: Two Tailed Test, Injection

    a Sequence alignments corresponding to the DIV s3b-s4 region of Na v subtypes. The highlighted sequences show the regions swapped between Na v 1.8 and Na v 1.9. b Representative current traces from Na v 1.9/1.8 DIV s3b-s4 P1 (top) and Na v 1.8/1.9 DIV s3b-s4 P1 (bottom) chimaera channels in the absence (black) and presence (red) of HpTx1. c Effects of HpTx1 on WT and mutant hNa v 1.9 channels. Dot plots display the effect of 0.75 μM HpTx1 on the peak current (top, n = 14 for WT; n = 4 for T1444L, M1445L, I1446F, and T1448A; n = 5 for L1449I and E1450L; n = 3 for N1451K) and the persistent current (bottom, n = 14 for WT; n = 4 for T1444L, I1446F, T1448A, and N1451K; n = 5 for M1445L, L1449I, and E1450L). Key residues involved in the interaction between HpTx1 and hNa v 1.9 are labeled (one-way ANOVA with Dunnett’s multiple comparison test, I 95 /I peak : F (7,35) = 17.72, P < 0.0001; I/I max : F (7,38) = 8.157, P < 0.0001). d (top) Sequence alignments corresponding to the DII s3b-s4 region of Na v subtypes. The highlighted sequences show the regions swapped between Na v 1.7 and Na v 1.8. Representative current traces from Na v 1.7/1.8 DII s3b-s4 (bottom left) and Na v 1.8/1.7 DII s3b-s4 (bottom right) chimaera channels in the absence (black) or presence of 5 μM HpTx1 (red). e Dose-dependent inhibitory curves show the effect of HpTx1 on WT ( n = 7) and mutant hNa v 1.7 channels ( n = 4 for F813S, n = 6 for L814A and A815S, n = 3 for D816K, n = 6 for V817K, n = 7 for E818G, n = 4 for E818R, n = 5 for G819S and n = 3 for Na v 1.7/1.8 DII s3b-s4) and the Na v 1.8/1.7 DII s3b-s4 chimaera channel ( n = 5). f Bars show the fold changes in IC 50 values of HpTx1 for mutant channels compared with that for the WT hNa v 1.7 channel. Data are presented as the mean ± S.E.M. Exact P ( c ) are presented in Supplementary Data  . Source data are provided as a  .   .

    Journal: Nature Communications

    Article Title: Spider venom-derived peptide induces hyperalgesia in Na v 1.7 knockout mice by activating Na v 1.9 channels

    doi: 10.1038/s41467-020-16210-y

    Figure Lengend Snippet: a Sequence alignments corresponding to the DIV s3b-s4 region of Na v subtypes. The highlighted sequences show the regions swapped between Na v 1.8 and Na v 1.9. b Representative current traces from Na v 1.9/1.8 DIV s3b-s4 P1 (top) and Na v 1.8/1.9 DIV s3b-s4 P1 (bottom) chimaera channels in the absence (black) and presence (red) of HpTx1. c Effects of HpTx1 on WT and mutant hNa v 1.9 channels. Dot plots display the effect of 0.75 μM HpTx1 on the peak current (top, n = 14 for WT; n = 4 for T1444L, M1445L, I1446F, and T1448A; n = 5 for L1449I and E1450L; n = 3 for N1451K) and the persistent current (bottom, n = 14 for WT; n = 4 for T1444L, I1446F, T1448A, and N1451K; n = 5 for M1445L, L1449I, and E1450L). Key residues involved in the interaction between HpTx1 and hNa v 1.9 are labeled (one-way ANOVA with Dunnett’s multiple comparison test, I 95 /I peak : F (7,35) = 17.72, P < 0.0001; I/I max : F (7,38) = 8.157, P < 0.0001). d (top) Sequence alignments corresponding to the DII s3b-s4 region of Na v subtypes. The highlighted sequences show the regions swapped between Na v 1.7 and Na v 1.8. Representative current traces from Na v 1.7/1.8 DII s3b-s4 (bottom left) and Na v 1.8/1.7 DII s3b-s4 (bottom right) chimaera channels in the absence (black) or presence of 5 μM HpTx1 (red). e Dose-dependent inhibitory curves show the effect of HpTx1 on WT ( n = 7) and mutant hNa v 1.7 channels ( n = 4 for F813S, n = 6 for L814A and A815S, n = 3 for D816K, n = 6 for V817K, n = 7 for E818G, n = 4 for E818R, n = 5 for G819S and n = 3 for Na v 1.7/1.8 DII s3b-s4) and the Na v 1.8/1.7 DII s3b-s4 chimaera channel ( n = 5). f Bars show the fold changes in IC 50 values of HpTx1 for mutant channels compared with that for the WT hNa v 1.7 channel. Data are presented as the mean ± S.E.M. Exact P ( c ) are presented in Supplementary Data . Source data are provided as a . .

    Article Snippet: The sections were permeabilized in PBS containing 0.5% TritonX-100) for 10 min, and were blocked with 10% goat serum for 1 h. The sections were incubated for 24 h at 4 °C with polyclonal rabbit anti-Na v 1.9 (1:200; alomone labs).

    Techniques: Sequencing, Mutagenesis, Labeling

    Primary antibodies used in this study

    Journal: Biology of Sex Differences

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    doi: 10.1186/s13293-018-0214-6

    Figure Lengend Snippet: Primary antibodies used in this study

    Article Snippet: Anti-GAT1 , Rabbit, Alomone, AGT-001 , 1:100 , Peptide (C)ERNMHQMTDGLDK.

    Techniques: Concentration Assay, Recombinant, Purification

    Western blot against human brain protein homogenates probed with GABA A receptor α1, α2, α3, α5, β3, and γ2 subunit, GAT1, GAT3, GAD65 and GAD67 and GABA B R R2 subunit antibodies. Each lane has 20 μg of protein loaded. Observed band sizes: α1, α2: ~ 52 kDa; α3, α5: ~ 55 kDa; β3: ~ 63 kDa; γ2: ~ 44 kDa; GAT1: ~ 85 kDa, GAT3: ~ 80 kDa; GABA B R R2: ~ 120 kDa

    Journal: Biology of Sex Differences

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    doi: 10.1186/s13293-018-0214-6

    Figure Lengend Snippet: Western blot against human brain protein homogenates probed with GABA A receptor α1, α2, α3, α5, β3, and γ2 subunit, GAT1, GAT3, GAD65 and GAD67 and GABA B R R2 subunit antibodies. Each lane has 20 μg of protein loaded. Observed band sizes: α1, α2: ~ 52 kDa; α3, α5: ~ 55 kDa; β3: ~ 63 kDa; γ2: ~ 44 kDa; GAT1: ~ 85 kDa, GAT3: ~ 80 kDa; GABA B R R2: ~ 120 kDa

    Article Snippet: Anti-GAT1 , Rabbit, Alomone, AGT-001 , 1:100 , Peptide (C)ERNMHQMTDGLDK.

    Techniques: Western Blot

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) sensory cortex homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Signal intensity for each GABA signaling component Western blot band was measured and normalized to their corresponding β-actin signal for each age group. The data is graphed as mean ± SEM ( n = 6; Kruskal-Wallis test; p * < 0.05)

    Journal: Biology of Sex Differences

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    doi: 10.1186/s13293-018-0214-6

    Figure Lengend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) sensory cortex homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Signal intensity for each GABA signaling component Western blot band was measured and normalized to their corresponding β-actin signal for each age group. The data is graphed as mean ± SEM ( n = 6; Kruskal-Wallis test; p * < 0.05)

    Article Snippet: Anti-GAT1 , Rabbit, Alomone, AGT-001 , 1:100 , Peptide (C)ERNMHQMTDGLDK.

    Techniques: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) motor cortex homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Journal: Biology of Sex Differences

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    doi: 10.1186/s13293-018-0214-6

    Figure Lengend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) motor cortex homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Article Snippet: Anti-GAT1 , Rabbit, Alomone, AGT-001 , 1:100 , Peptide (C)ERNMHQMTDGLDK.

    Techniques: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) cerebellum homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Journal: Biology of Sex Differences

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    doi: 10.1186/s13293-018-0214-6

    Figure Lengend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) cerebellum homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Article Snippet: Anti-GAT1 , Rabbit, Alomone, AGT-001 , 1:100 , Peptide (C)ERNMHQMTDGLDK.

    Techniques: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) inferior temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Journal: Biology of Sex Differences

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    doi: 10.1186/s13293-018-0214-6

    Figure Lengend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) inferior temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Article Snippet: Anti-GAT1 , Rabbit, Alomone, AGT-001 , 1:100 , Peptide (C)ERNMHQMTDGLDK.

    Techniques: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) medial temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Journal: Biology of Sex Differences

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    doi: 10.1186/s13293-018-0214-6

    Figure Lengend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) medial temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Article Snippet: Anti-GAT1 , Rabbit, Alomone, AGT-001 , 1:100 , Peptide (C)ERNMHQMTDGLDK.

    Techniques: Western Blot, Incubation

    Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) superior temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Journal: Biology of Sex Differences

    Article Title: Sex- and age-related changes in GABA signaling components in the human cortex

    doi: 10.1186/s13293-018-0214-6

    Figure Lengend Snippet: Representative immunoreactive Western blot bands from younger female (YF), older female (OF), younger male (YM), and older male (OM) superior temporal gyrus homogenates following incubation with antibodies to the GABA A R subunits α1, α2, α3, α5, β3, and γ2 and GABA B R subunit R2, GAT1, GAT3, GAD65, and GAD67 ( a ) and corresponding signal intensity graphs ( b ). Also, see figure legend on Fig. for details

    Article Snippet: Anti-GAT1 , Rabbit, Alomone, AGT-001 , 1:100 , Peptide (C)ERNMHQMTDGLDK.

    Techniques: Western Blot, Incubation