agp  (Alomone Labs)


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    Alomone Labs agp
    Agp, 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/agp/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
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    agp - by Bioz Stars, 2023-02
    94/100 stars

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    agp  (Alomone Labs)


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    Alomone Labs agp
    Agp, 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/agp/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    agp - by Bioz Stars, 2023-02
    94/100 stars

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    guinea pig anti ampa receptor 2 subunit  (Alomone Labs)


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    Alomone Labs guinea pig anti ampa receptor 2 subunit
    Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse <t>Gria2</t> , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.
    Guinea Pig Anti Ampa Receptor 2 Subunit, 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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    94/100 stars

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    1) Product Images from "α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis"

    Article Title: α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis

    Journal: Brain Communications

    doi: 10.1093/braincomms/fcac081

    Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse Gria2 , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.
    Figure Legend Snippet: Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse Gria2 , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.

    Techniques Used: Quantitative RT-PCR, Expressing

    Expression of GluA2 in spinal cords of embryonic SOD1 G93A mice. Cross-sections of lumbar spinal cord from WT (HB9:GFP; WT) and SOD1 G93A (SOD1 G93A ; HB9:GFP) mice at (A–J) E12.5 and ( K–T ) E17.5. Double-immunolabelling for GFP, GluA2 and NeuN (Neuronal nuclei). Plots represent quantification analysis of GluA2 signal intensity in HB9:GFP motor neurons at ( U ) E12.5 and ( V ) E17.5. Data represent mean ± SEM, unpaired student t -test performed on n = 4 biological replicates, ∼50 neurons analysed per biological replicate, * P < 0.05. Scale bars 50 μm.
    Figure Legend Snippet: Expression of GluA2 in spinal cords of embryonic SOD1 G93A mice. Cross-sections of lumbar spinal cord from WT (HB9:GFP; WT) and SOD1 G93A (SOD1 G93A ; HB9:GFP) mice at (A–J) E12.5 and ( K–T ) E17.5. Double-immunolabelling for GFP, GluA2 and NeuN (Neuronal nuclei). Plots represent quantification analysis of GluA2 signal intensity in HB9:GFP motor neurons at ( U ) E12.5 and ( V ) E17.5. Data represent mean ± SEM, unpaired student t -test performed on n = 4 biological replicates, ∼50 neurons analysed per biological replicate, * P < 0.05. Scale bars 50 μm.

    Techniques Used: Expressing

    Expression of GRIA2 and ADAR2 in iPSC motor neurons derived from ALS patients with SOD1 mutations and healthy control lines. Representative images of iPSC mature motor neurons derived from ( A–E ) healthy control line and ( F–J ) SOD1 I114T line, immunolabelled with ChAT, GluA2 and TUJ1, counterstained with Hoechst. ( K ) Plot represents quantification analysis of GluA2 signal intensity in iPSC motor neurons. Data represent mean ± SEM, unpaired student t -test performed on n = 3 biological replicates, 50 neurons analysed per biological replicate. (L) Fold change expression of GRIA2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. ( M ) Fold change expression of ADAR2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. Data represent mean ± SEM, n = 3 biological replicates, one-way ANOVA with Dunnett's multiple comparison test, * P < 0.01, ** P < 0.005. Scale bars 50 μm.
    Figure Legend Snippet: Expression of GRIA2 and ADAR2 in iPSC motor neurons derived from ALS patients with SOD1 mutations and healthy control lines. Representative images of iPSC mature motor neurons derived from ( A–E ) healthy control line and ( F–J ) SOD1 I114T line, immunolabelled with ChAT, GluA2 and TUJ1, counterstained with Hoechst. ( K ) Plot represents quantification analysis of GluA2 signal intensity in iPSC motor neurons. Data represent mean ± SEM, unpaired student t -test performed on n = 3 biological replicates, 50 neurons analysed per biological replicate. (L) Fold change expression of GRIA2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. ( M ) Fold change expression of ADAR2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. Data represent mean ± SEM, n = 3 biological replicates, one-way ANOVA with Dunnett's multiple comparison test, * P < 0.01, ** P < 0.005. Scale bars 50 μm.

    Techniques Used: Expressing, Derivative Assay, Quantitative RT-PCR

    rabbit anti glua2  (Alomone Labs)


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    Alomone Labs rabbit anti glua2
    Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse <t>Gria2</t> , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.
    Rabbit Anti Glua2, 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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    rabbit anti glua2 - by Bioz Stars, 2023-02
    94/100 stars

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    1) Product Images from "α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis"

    Article Title: α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis

    Journal: Brain Communications

    doi: 10.1093/braincomms/fcac081

    Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse Gria2 , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.
    Figure Legend Snippet: Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse Gria2 , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.

    Techniques Used: Quantitative RT-PCR, Expressing

    Expression of GluA2 in spinal cords of embryonic SOD1 G93A mice. Cross-sections of lumbar spinal cord from WT (HB9:GFP; WT) and SOD1 G93A (SOD1 G93A ; HB9:GFP) mice at (A–J) E12.5 and ( K–T ) E17.5. Double-immunolabelling for GFP, GluA2 and NeuN (Neuronal nuclei). Plots represent quantification analysis of GluA2 signal intensity in HB9:GFP motor neurons at ( U ) E12.5 and ( V ) E17.5. Data represent mean ± SEM, unpaired student t -test performed on n = 4 biological replicates, ∼50 neurons analysed per biological replicate, * P < 0.05. Scale bars 50 μm.
    Figure Legend Snippet: Expression of GluA2 in spinal cords of embryonic SOD1 G93A mice. Cross-sections of lumbar spinal cord from WT (HB9:GFP; WT) and SOD1 G93A (SOD1 G93A ; HB9:GFP) mice at (A–J) E12.5 and ( K–T ) E17.5. Double-immunolabelling for GFP, GluA2 and NeuN (Neuronal nuclei). Plots represent quantification analysis of GluA2 signal intensity in HB9:GFP motor neurons at ( U ) E12.5 and ( V ) E17.5. Data represent mean ± SEM, unpaired student t -test performed on n = 4 biological replicates, ∼50 neurons analysed per biological replicate, * P < 0.05. Scale bars 50 μm.

    Techniques Used: Expressing

    Expression of GRIA2 and ADAR2 in iPSC motor neurons derived from ALS patients with SOD1 mutations and healthy control lines. Representative images of iPSC mature motor neurons derived from ( A–E ) healthy control line and ( F–J ) SOD1 I114T line, immunolabelled with ChAT, GluA2 and TUJ1, counterstained with Hoechst. ( K ) Plot represents quantification analysis of GluA2 signal intensity in iPSC motor neurons. Data represent mean ± SEM, unpaired student t -test performed on n = 3 biological replicates, 50 neurons analysed per biological replicate. (L) Fold change expression of GRIA2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. ( M ) Fold change expression of ADAR2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. Data represent mean ± SEM, n = 3 biological replicates, one-way ANOVA with Dunnett's multiple comparison test, * P < 0.01, ** P < 0.005. Scale bars 50 μm.
    Figure Legend Snippet: Expression of GRIA2 and ADAR2 in iPSC motor neurons derived from ALS patients with SOD1 mutations and healthy control lines. Representative images of iPSC mature motor neurons derived from ( A–E ) healthy control line and ( F–J ) SOD1 I114T line, immunolabelled with ChAT, GluA2 and TUJ1, counterstained with Hoechst. ( K ) Plot represents quantification analysis of GluA2 signal intensity in iPSC motor neurons. Data represent mean ± SEM, unpaired student t -test performed on n = 3 biological replicates, 50 neurons analysed per biological replicate. (L) Fold change expression of GRIA2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. ( M ) Fold change expression of ADAR2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. Data represent mean ± SEM, n = 3 biological replicates, one-way ANOVA with Dunnett's multiple comparison test, * P < 0.01, ** P < 0.005. Scale bars 50 μm.

    Techniques Used: Expressing, Derivative Assay, Quantitative RT-PCR

    glua2  (Alomone Labs)


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    Alomone Labs glua2
    Time-dependent changes of protein expression levels of GluA1 (a), <t>GluA2</t> (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC total homogenate of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01; ∗∗∗ p < 0.001.
    Glua2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Acute Footshock Stress Induces Time-Dependent Modifications of AMPA/NMDA Protein Expression and AMPA Phosphorylation"

    Article Title: Acute Footshock Stress Induces Time-Dependent Modifications of AMPA/NMDA Protein Expression and AMPA Phosphorylation

    Journal: Neural Plasticity

    doi: 10.1155/2016/7267865

    Time-dependent changes of protein expression levels of GluA1 (a), GluA2 (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC total homogenate of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01; ∗∗∗ p < 0.001.
    Figure Legend Snippet: Time-dependent changes of protein expression levels of GluA1 (a), GluA2 (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC total homogenate of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01; ∗∗∗ p < 0.001.

    Techniques Used: Expressing

    Time-dependent changes of protein expression levels of GluA1 (a), GluA2 (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC postsynaptic spine membranes of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01.
    Figure Legend Snippet: Time-dependent changes of protein expression levels of GluA1 (a), GluA2 (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC postsynaptic spine membranes of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01.

    Techniques Used: Expressing

    antibodies against mouse glua2  (Alomone Labs)


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    Alomone Labs antibodies against mouse glua2
    <t>GluA2</t> expression levels in human postmortem HD and PD hippocampus and striatum. (a) No significant changes in GluA2 expression in HD or PD hippocampal regions. (b) GluA2 specific changes occur in the putamen (Put) of HD and PD tissue. * P < 0.05, ** P < 0.005. (c) Representative images are shown for GluA2 in the dentate gyrus, CA3 and CA1 regions of the hippocampus. (d) Representative images of GluA2 immunostaining in the caudate nucleus and putamen of the striatum. Scale bar for (c) and (d) is 25 μ m. (e) High power example image of GluA2 immunolabelling, showing the somatic and dendritic localisations.
    Antibodies Against Mouse Glua2, 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/antibodies against mouse glua2/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibodies against mouse glua2 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Differential Changes in Postsynaptic Density Proteins in Postmortem Huntington's Disease and Parkinson's Disease Human Brains"

    Article Title: Differential Changes in Postsynaptic Density Proteins in Postmortem Huntington's Disease and Parkinson's Disease Human Brains

    Journal: Journal of Neurodegenerative Diseases

    doi: 10.1155/2014/938530

    GluA2 expression levels in human postmortem HD and PD hippocampus and striatum. (a) No significant changes in GluA2 expression in HD or PD hippocampal regions. (b) GluA2 specific changes occur in the putamen (Put) of HD and PD tissue. * P < 0.05, ** P < 0.005. (c) Representative images are shown for GluA2 in the dentate gyrus, CA3 and CA1 regions of the hippocampus. (d) Representative images of GluA2 immunostaining in the caudate nucleus and putamen of the striatum. Scale bar for (c) and (d) is 25 μ m. (e) High power example image of GluA2 immunolabelling, showing the somatic and dendritic localisations.
    Figure Legend Snippet: GluA2 expression levels in human postmortem HD and PD hippocampus and striatum. (a) No significant changes in GluA2 expression in HD or PD hippocampal regions. (b) GluA2 specific changes occur in the putamen (Put) of HD and PD tissue. * P < 0.05, ** P < 0.005. (c) Representative images are shown for GluA2 in the dentate gyrus, CA3 and CA1 regions of the hippocampus. (d) Representative images of GluA2 immunostaining in the caudate nucleus and putamen of the striatum. Scale bar for (c) and (d) is 25 μ m. (e) High power example image of GluA2 immunolabelling, showing the somatic and dendritic localisations.

    Techniques Used: Expressing, Immunostaining

    Quantitative immunohistochemistry of SAP97, PSD-95, GluN1, and GluA2 expression in YAC128 hippocampal sections. Sections were prepared from symptomatic 1-year-old YAC128 mice to provide a comparison to the end stage of human HD. (a)–(d). Top: Quantification of (a) SAP97, (b) PSD-95, (c) GluA2, and (d) GluN1 levels in dentate gyrus (DG), area CA3, and area CA1. Below: Example immunohistochemical staining for each glutamatergic synaptic protein in the hippocampal CA1 region in control (wildtype) and YAC128 mice. (e) Immunohistochemical quantification of DARPP-32 expression in wild-type and YAC128 striatum (caudate putamen, CPu). * P < 0.05.
    Figure Legend Snippet: Quantitative immunohistochemistry of SAP97, PSD-95, GluN1, and GluA2 expression in YAC128 hippocampal sections. Sections were prepared from symptomatic 1-year-old YAC128 mice to provide a comparison to the end stage of human HD. (a)–(d). Top: Quantification of (a) SAP97, (b) PSD-95, (c) GluA2, and (d) GluN1 levels in dentate gyrus (DG), area CA3, and area CA1. Below: Example immunohistochemical staining for each glutamatergic synaptic protein in the hippocampal CA1 region in control (wildtype) and YAC128 mice. (e) Immunohistochemical quantification of DARPP-32 expression in wild-type and YAC128 striatum (caudate putamen, CPu). * P < 0.05.

    Techniques Used: Immunohistochemistry, Expressing, Immunohistochemical staining, Staining

    glua2  (Alomone Labs)


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    Alomone Labs glua2
    KIBRA regulates the basal expression of extrasynaptic AMPA receptors in the adult hippocampus (A, C, E, and G) Representative western blot images from sub-region CA1 of the adult hippocampus. Samples are normalized to loading control and quantified as % WT in B, D, F, and H (see for details). (B) Adult-onset KIBRA deletion from neurons decreases the total expression <t>GluA2</t> and GluA1, but not the excitatory synaptic scaffold PSD-95 (unpaired t-tests, corrected for multiple comparisons). GluA2, WT = 100 ± 3%, cKO = 67 ±3; GluA1, WT = 100 ± 2%, cKO = 80 ± 4%; PSD95, WT = 100 ± 3%, cKO = 93 ± 3%. (D) Loss of KIBRA from the adult brain decreases expression of membrane-localized GluA2 (unpaired t-tests with Welch’s correction, corrected for multiple comparisons). GluA2, WT = 100 ± 2%, cKO = 83 ± 5%; GluA1, WT = 100 ± 4%, cKO = 102 ± 2%; PSD95, WT = 100 ± 6%, cKO = 105 ± 4%. (F) Adult-onset KIBRA deletion does not alter basal expression of synaptic AMPA receptors (unpaired Mann-Whitney tests, corrected for multiple comparisons). GluA2, WT = 100 ± 3%, cKO = 98 ± 6%; GluA1, WT = 100 ± 2%, cKO = 94 ± 8%; PSD95, WT = 100 ± 8%, cKO = 106 ± 5%. (H) Decrease in expression of the KIBRA homolog WWC2 following adult-onset deletion of KIBRA (unpaired t-tests, corrected for multiple comparisons). Total, WT = 100 ± 4%, cKO = 70 ± 2%; membrane, WT = 100 ± 5%, cKO = 92 ± 6%; synaptic, WT = 100 ± 5%, cKO = 87 ± 7%. (I) Representative western blot with equal protein loaded for total, cytosolic, membrane and synaptic fractions, demonstrating depletion of the postsynaptic scaffold PSD95 from the cytosolic fraction and enrichment in the membrane fraction with further enrichment in the synaptic fraction. Data shown as mean ± SEM, n on bar graphs = number of animals.
    Glua2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/glua2/product/Alomone Labs
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    glua2 - by Bioz Stars, 2023-02
    86/100 stars

    Images

    1) Product Images from "KIBRA regulates activity-induced AMPA receptor expression and synaptic plasticity in an age-dependent manner"

    Article Title: KIBRA regulates activity-induced AMPA receptor expression and synaptic plasticity in an age-dependent manner

    Journal: iScience

    doi: 10.1016/j.isci.2022.105623

    KIBRA regulates the basal expression of extrasynaptic AMPA receptors in the adult hippocampus (A, C, E, and G) Representative western blot images from sub-region CA1 of the adult hippocampus. Samples are normalized to loading control and quantified as % WT in B, D, F, and H (see for details). (B) Adult-onset KIBRA deletion from neurons decreases the total expression GluA2 and GluA1, but not the excitatory synaptic scaffold PSD-95 (unpaired t-tests, corrected for multiple comparisons). GluA2, WT = 100 ± 3%, cKO = 67 ±3; GluA1, WT = 100 ± 2%, cKO = 80 ± 4%; PSD95, WT = 100 ± 3%, cKO = 93 ± 3%. (D) Loss of KIBRA from the adult brain decreases expression of membrane-localized GluA2 (unpaired t-tests with Welch’s correction, corrected for multiple comparisons). GluA2, WT = 100 ± 2%, cKO = 83 ± 5%; GluA1, WT = 100 ± 4%, cKO = 102 ± 2%; PSD95, WT = 100 ± 6%, cKO = 105 ± 4%. (F) Adult-onset KIBRA deletion does not alter basal expression of synaptic AMPA receptors (unpaired Mann-Whitney tests, corrected for multiple comparisons). GluA2, WT = 100 ± 3%, cKO = 98 ± 6%; GluA1, WT = 100 ± 2%, cKO = 94 ± 8%; PSD95, WT = 100 ± 8%, cKO = 106 ± 5%. (H) Decrease in expression of the KIBRA homolog WWC2 following adult-onset deletion of KIBRA (unpaired t-tests, corrected for multiple comparisons). Total, WT = 100 ± 4%, cKO = 70 ± 2%; membrane, WT = 100 ± 5%, cKO = 92 ± 6%; synaptic, WT = 100 ± 5%, cKO = 87 ± 7%. (I) Representative western blot with equal protein loaded for total, cytosolic, membrane and synaptic fractions, demonstrating depletion of the postsynaptic scaffold PSD95 from the cytosolic fraction and enrichment in the membrane fraction with further enrichment in the synaptic fraction. Data shown as mean ± SEM, n on bar graphs = number of animals.
    Figure Legend Snippet: KIBRA regulates the basal expression of extrasynaptic AMPA receptors in the adult hippocampus (A, C, E, and G) Representative western blot images from sub-region CA1 of the adult hippocampus. Samples are normalized to loading control and quantified as % WT in B, D, F, and H (see for details). (B) Adult-onset KIBRA deletion from neurons decreases the total expression GluA2 and GluA1, but not the excitatory synaptic scaffold PSD-95 (unpaired t-tests, corrected for multiple comparisons). GluA2, WT = 100 ± 3%, cKO = 67 ±3; GluA1, WT = 100 ± 2%, cKO = 80 ± 4%; PSD95, WT = 100 ± 3%, cKO = 93 ± 3%. (D) Loss of KIBRA from the adult brain decreases expression of membrane-localized GluA2 (unpaired t-tests with Welch’s correction, corrected for multiple comparisons). GluA2, WT = 100 ± 2%, cKO = 83 ± 5%; GluA1, WT = 100 ± 4%, cKO = 102 ± 2%; PSD95, WT = 100 ± 6%, cKO = 105 ± 4%. (F) Adult-onset KIBRA deletion does not alter basal expression of synaptic AMPA receptors (unpaired Mann-Whitney tests, corrected for multiple comparisons). GluA2, WT = 100 ± 3%, cKO = 98 ± 6%; GluA1, WT = 100 ± 2%, cKO = 94 ± 8%; PSD95, WT = 100 ± 8%, cKO = 106 ± 5%. (H) Decrease in expression of the KIBRA homolog WWC2 following adult-onset deletion of KIBRA (unpaired t-tests, corrected for multiple comparisons). Total, WT = 100 ± 4%, cKO = 70 ± 2%; membrane, WT = 100 ± 5%, cKO = 92 ± 6%; synaptic, WT = 100 ± 5%, cKO = 87 ± 7%. (I) Representative western blot with equal protein loaded for total, cytosolic, membrane and synaptic fractions, demonstrating depletion of the postsynaptic scaffold PSD95 from the cytosolic fraction and enrichment in the membrane fraction with further enrichment in the synaptic fraction. Data shown as mean ± SEM, n on bar graphs = number of animals.

    Techniques Used: Expressing, Western Blot, MANN-WHITNEY

    Juvenile-onset deletion of KIBRA has minimal effect on hippocampal AMPAR expression (B, D, and F) Representative western blot images from sub-region CA1 of the juvenile hippocampus. (A) Acute reduction of KIBRA in the juvenile hippocampus decreases total expression of AMPAR subunit GluA2 but not GluA1 or PSD95 (unpaired t-tests, corrected for multiple comparisons, Welch’s correction for GluA2). GluA2, WT = 100 ± 1%, cKO = 86 ±3; GluA1, WT = 100 ± 3%, cKO = 95 ± 4%; PSD95, WT = 100 ± 4%, cKO = 95 ± 3%. (C) Larger decrease in total AMPAR expression in adult compared to juvenile KIBRA cKO mice (unpaired t-tests, corrected for multiple comparisons). For each group, data is shown as % decrease from respective WT (GluA2, juvenile cKO = −14 ± 4%, adult cKO = −33 ± 4%; GluA1, juvenile cKO = −3 ± 5%, adult cKO = −19 ± 4%). (E) Juvenile-onset deletion of KIBRA does not affect expression of membrane-associated AMPARs or PSD95 in the juvenile hippocampus (unpaired t- (GluA1, GluA2) or Mann-Whitney (PSD95) tests, corrected for multiple comparisons). GluA2, WT = 100 ± 6%, cKO = 95 ± 4%; GluA1, WT = 100 ± 6%, cKO = 101 ± 11%; PSD95, WT = 100 ± 3%, cKO = 98 ± 17%. (G) Loss of KIBRA in the juvenile brain does not alter basal expression of synaptic AMPA receptors or PSD95 (unpaired t- (GluA1, PSD95) or Mann-Whitney (GluA2) tests, corrected for multiple comparisons). GluA2, WT = 100 ± 14%, cKO = 89 ± 12%; GluA1, WT = 100 ± 7%, cKO = 85 ± 6%; PSD95, WT = 100 ± 7%, cKO = 96 ± 11%. Data shown as mean ± SEM, n on bar graphs = number of animals. ∗p < 0.05, ∗∗p < 0.01.
    Figure Legend Snippet: Juvenile-onset deletion of KIBRA has minimal effect on hippocampal AMPAR expression (B, D, and F) Representative western blot images from sub-region CA1 of the juvenile hippocampus. (A) Acute reduction of KIBRA in the juvenile hippocampus decreases total expression of AMPAR subunit GluA2 but not GluA1 or PSD95 (unpaired t-tests, corrected for multiple comparisons, Welch’s correction for GluA2). GluA2, WT = 100 ± 1%, cKO = 86 ±3; GluA1, WT = 100 ± 3%, cKO = 95 ± 4%; PSD95, WT = 100 ± 4%, cKO = 95 ± 3%. (C) Larger decrease in total AMPAR expression in adult compared to juvenile KIBRA cKO mice (unpaired t-tests, corrected for multiple comparisons). For each group, data is shown as % decrease from respective WT (GluA2, juvenile cKO = −14 ± 4%, adult cKO = −33 ± 4%; GluA1, juvenile cKO = −3 ± 5%, adult cKO = −19 ± 4%). (E) Juvenile-onset deletion of KIBRA does not affect expression of membrane-associated AMPARs or PSD95 in the juvenile hippocampus (unpaired t- (GluA1, GluA2) or Mann-Whitney (PSD95) tests, corrected for multiple comparisons). GluA2, WT = 100 ± 6%, cKO = 95 ± 4%; GluA1, WT = 100 ± 6%, cKO = 101 ± 11%; PSD95, WT = 100 ± 3%, cKO = 98 ± 17%. (G) Loss of KIBRA in the juvenile brain does not alter basal expression of synaptic AMPA receptors or PSD95 (unpaired t- (GluA1, PSD95) or Mann-Whitney (GluA2) tests, corrected for multiple comparisons). GluA2, WT = 100 ± 14%, cKO = 89 ± 12%; GluA1, WT = 100 ± 7%, cKO = 85 ± 6%; PSD95, WT = 100 ± 7%, cKO = 96 ± 11%. Data shown as mean ± SEM, n on bar graphs = number of animals. ∗p < 0.05, ∗∗p < 0.01.

    Techniques Used: Expressing, Western Blot, MANN-WHITNEY

    KIBRA is required for LTP-induced increases in AMPAR expression in the adult hippocampus (A) Experimental design. Transverse hippocampal slices were collected from adult mice following basal stimulation (0.033 Hz) or LTP (TBS). The stimulated region of CA1 was microdissected 30 or 120 min after LTP or basal stimulation. Data from both time points was combined as no difference in AMPAR induction was observed between 30 and 120min post LTP. (B–D) Representative GluA2 and GluA1 immunoblot images after baseline stimulation or LTP from adult WT (cre-negative tamoxifen treated) or KIBRA cKO (cre-positive tamoxifen treated) mice. LTP increases GluA2 (C) and GluA1 (E) expression in WT but not KIBRA cKO mice. Data plotted as % increase over baseline stimulation, mean ± SEM (GluA2, WT mean= 151 ± 15%, cKO = 100 ± 8%; GluA1, WT mean = 119 ± 8%, cKO = 101 ± 4%). LTP-stimulated slices were compared to baseline-stimulated slices from the same animal. Number of slices is indicated on each bar. One sample t-test, ∗p < 0.05, ∗∗p < 0.01.
    Figure Legend Snippet: KIBRA is required for LTP-induced increases in AMPAR expression in the adult hippocampus (A) Experimental design. Transverse hippocampal slices were collected from adult mice following basal stimulation (0.033 Hz) or LTP (TBS). The stimulated region of CA1 was microdissected 30 or 120 min after LTP or basal stimulation. Data from both time points was combined as no difference in AMPAR induction was observed between 30 and 120min post LTP. (B–D) Representative GluA2 and GluA1 immunoblot images after baseline stimulation or LTP from adult WT (cre-negative tamoxifen treated) or KIBRA cKO (cre-positive tamoxifen treated) mice. LTP increases GluA2 (C) and GluA1 (E) expression in WT but not KIBRA cKO mice. Data plotted as % increase over baseline stimulation, mean ± SEM (GluA2, WT mean= 151 ± 15%, cKO = 100 ± 8%; GluA1, WT mean = 119 ± 8%, cKO = 101 ± 4%). LTP-stimulated slices were compared to baseline-stimulated slices from the same animal. Number of slices is indicated on each bar. One sample t-test, ∗p < 0.05, ∗∗p < 0.01.

    Techniques Used: Expressing, Western Blot

    LTP does not increase AMPAR expression in juvenile WT or KIBRA cKO mice Transverse hippocampal slices were collected from juvenile mice following basal stimulation (0.033 Hz) or LTP (TBS). The stimulated region of CA1 was microdissected 30 min after LTP or basal stimulation. (A and C) Representative GluA2 and GluA1 immunoblot images after baseline stimulation or LTP from juvenile WT (cre-negative tamoxifen treated) or KIBRA cKO (cre-positive tamoxifen treated) mice. LTP did not induce increases in total GluA2 (B) or GluA1 (D) expression in juvenile WT or KIBRA cKO mice. Data plotted as % increase over baseline stimulation, mean ± SEM (GluA2, WT mean = 108 ± 11%, cKO = 107 ± 7 %; GluA1, WT mean = 106 ± 6%, cKO = 114 ± 7%). LTP-stimulated slices were compared to baseline-stimulated slices from the same animal. For each group, n = 18 slices from 10 mice. One sample Wilcoxon test, p > 0.05 for all comparisons shown.
    Figure Legend Snippet: LTP does not increase AMPAR expression in juvenile WT or KIBRA cKO mice Transverse hippocampal slices were collected from juvenile mice following basal stimulation (0.033 Hz) or LTP (TBS). The stimulated region of CA1 was microdissected 30 min after LTP or basal stimulation. (A and C) Representative GluA2 and GluA1 immunoblot images after baseline stimulation or LTP from juvenile WT (cre-negative tamoxifen treated) or KIBRA cKO (cre-positive tamoxifen treated) mice. LTP did not induce increases in total GluA2 (B) or GluA1 (D) expression in juvenile WT or KIBRA cKO mice. Data plotted as % increase over baseline stimulation, mean ± SEM (GluA2, WT mean = 108 ± 11%, cKO = 107 ± 7 %; GluA1, WT mean = 106 ± 6%, cKO = 114 ± 7%). LTP-stimulated slices were compared to baseline-stimulated slices from the same animal. For each group, n = 18 slices from 10 mice. One sample Wilcoxon test, p > 0.05 for all comparisons shown.

    Techniques Used: Expressing, Western Blot


    Figure Legend Snippet:

    Techniques Used: Recombinant, Blocking Assay, Software

    glur2  (Alomone Labs)


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    Alomone Labs glur2
    Astaxanthin inhibits a [Ca 2+ ]i increase in cortical neurons upon ionotropic glutamate receptor activation. ( A – C ) The average [Ca 2+ ]i response in control (black) and AST (red) preincubated neurons stimulated with 50 μM each of NMDA (+ 5 μM glycine), AMPA and KA for 15 min (NMDA: Con n = 23, AST n = 42; AMPA: con n = 27, AST n = 23; KA con n = 30, AST n = 40). ( D ) Dot plot representing the total calcium (area under the curve) after 15 min of NMDA, AMPA and KA stimulation. Arrow heads indicate point of glutamate receptor agonist applications. ( E ) Representative protein expression levels of NMDA (GluN1), AMPA <t>(GluA2)</t> and KA (GluK123) detected by the Western blot analysis with β-actin as the internal reference (individual Western blots figure are provided in ). ( F ) Dot plot indicate the average normalized protein expression for GluN1, GluA2 and GluK123. Data are represented as mean ± SEM from 3–4 different experiments, * p < 0.05. n.s: non-significant.
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    1) Product Images from "Astaxanthin Protection against Neuronal Excitotoxicity via Glutamate Receptor Inhibition and Improvement of Mitochondrial Function"

    Article Title: Astaxanthin Protection against Neuronal Excitotoxicity via Glutamate Receptor Inhibition and Improvement of Mitochondrial Function

    Journal: Marine Drugs

    doi: 10.3390/md20100645

    Astaxanthin inhibits a [Ca 2+ ]i increase in cortical neurons upon ionotropic glutamate receptor activation. ( A – C ) The average [Ca 2+ ]i response in control (black) and AST (red) preincubated neurons stimulated with 50 μM each of NMDA (+ 5 μM glycine), AMPA and KA for 15 min (NMDA: Con n = 23, AST n = 42; AMPA: con n = 27, AST n = 23; KA con n = 30, AST n = 40). ( D ) Dot plot representing the total calcium (area under the curve) after 15 min of NMDA, AMPA and KA stimulation. Arrow heads indicate point of glutamate receptor agonist applications. ( E ) Representative protein expression levels of NMDA (GluN1), AMPA (GluA2) and KA (GluK123) detected by the Western blot analysis with β-actin as the internal reference (individual Western blots figure are provided in ). ( F ) Dot plot indicate the average normalized protein expression for GluN1, GluA2 and GluK123. Data are represented as mean ± SEM from 3–4 different experiments, * p < 0.05. n.s: non-significant.
    Figure Legend Snippet: Astaxanthin inhibits a [Ca 2+ ]i increase in cortical neurons upon ionotropic glutamate receptor activation. ( A – C ) The average [Ca 2+ ]i response in control (black) and AST (red) preincubated neurons stimulated with 50 μM each of NMDA (+ 5 μM glycine), AMPA and KA for 15 min (NMDA: Con n = 23, AST n = 42; AMPA: con n = 27, AST n = 23; KA con n = 30, AST n = 40). ( D ) Dot plot representing the total calcium (area under the curve) after 15 min of NMDA, AMPA and KA stimulation. Arrow heads indicate point of glutamate receptor agonist applications. ( E ) Representative protein expression levels of NMDA (GluN1), AMPA (GluA2) and KA (GluK123) detected by the Western blot analysis with β-actin as the internal reference (individual Western blots figure are provided in ). ( F ) Dot plot indicate the average normalized protein expression for GluN1, GluA2 and GluK123. Data are represented as mean ± SEM from 3–4 different experiments, * p < 0.05. n.s: non-significant.

    Techniques Used: Activation Assay, Expressing, Western Blot

    glur2  (Alomone Labs)


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    a-c , Synaptic vesicles were labeled live using an antibody against a luminal epitope of synaptotagmin 1 (Syt1, magenta). The vesicular glutamate transporter (vGluT1, blue) and PSD95 (gray) were immunostained using an antibody and a nanobody, respectively. a , Recently endocytosed vesicle exhibiting circular morphology. b , Readily retrievable pool molecules form patches containing Syt1/vGluT1 (top), which are dispersed by cholesterol extraction using MβCD (bottom). c , MβCD causes molecules to spread across larger areas (left: N = 22-19, 2 independent experiments, p < 0.0044, Mann-Whitney test; right: N = 22-22, 2 independent experiments, p = 0.8937), although the signal per vesicle (the Syt1 copy number) remains unchanged. d , A visualization of PSDs (top and side views), after immunostaining PSD95 with the same nanobody used in a-c, and Shank2 and Homer1 with specific antibodies. The graph indicates the axial positioning, which agrees well with the literature . N = 11 measurements for each protein, 2 independent experiments; symbols show the medians, SEM and SD. e , Side view of a postsynapse displaying PSD95, MAP2 and two glutamate receptors <t>(GluR2,</t> AMPA type, and GluN2b, NMDA type). f , ONE images of PSD95 (top views), before or after the addition of 10% 1,6-hexanediol (Hex). g , Line scans through the PSD95 stainings shown in panel f. h , An analysis of PSD95 spot profiles; N = 10-7 synapses, Friedman test followed by Dunn-Sidak testing, p = 0.0027; the error bars show the SEM. For details on the analysis, see .
    Glur2, 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 "Expansion microscopy at one nanometer resolution"

    Article Title: Expansion microscopy at one nanometer resolution

    Journal: bioRxiv

    doi: 10.1101/2022.08.03.502284

    a-c , Synaptic vesicles were labeled live using an antibody against a luminal epitope of synaptotagmin 1 (Syt1, magenta). The vesicular glutamate transporter (vGluT1, blue) and PSD95 (gray) were immunostained using an antibody and a nanobody, respectively. a , Recently endocytosed vesicle exhibiting circular morphology. b , Readily retrievable pool molecules form patches containing Syt1/vGluT1 (top), which are dispersed by cholesterol extraction using MβCD (bottom). c , MβCD causes molecules to spread across larger areas (left: N = 22-19, 2 independent experiments, p < 0.0044, Mann-Whitney test; right: N = 22-22, 2 independent experiments, p = 0.8937), although the signal per vesicle (the Syt1 copy number) remains unchanged. d , A visualization of PSDs (top and side views), after immunostaining PSD95 with the same nanobody used in a-c, and Shank2 and Homer1 with specific antibodies. The graph indicates the axial positioning, which agrees well with the literature . N = 11 measurements for each protein, 2 independent experiments; symbols show the medians, SEM and SD. e , Side view of a postsynapse displaying PSD95, MAP2 and two glutamate receptors (GluR2, AMPA type, and GluN2b, NMDA type). f , ONE images of PSD95 (top views), before or after the addition of 10% 1,6-hexanediol (Hex). g , Line scans through the PSD95 stainings shown in panel f. h , An analysis of PSD95 spot profiles; N = 10-7 synapses, Friedman test followed by Dunn-Sidak testing, p = 0.0027; the error bars show the SEM. For details on the analysis, see .
    Figure Legend Snippet: a-c , Synaptic vesicles were labeled live using an antibody against a luminal epitope of synaptotagmin 1 (Syt1, magenta). The vesicular glutamate transporter (vGluT1, blue) and PSD95 (gray) were immunostained using an antibody and a nanobody, respectively. a , Recently endocytosed vesicle exhibiting circular morphology. b , Readily retrievable pool molecules form patches containing Syt1/vGluT1 (top), which are dispersed by cholesterol extraction using MβCD (bottom). c , MβCD causes molecules to spread across larger areas (left: N = 22-19, 2 independent experiments, p < 0.0044, Mann-Whitney test; right: N = 22-22, 2 independent experiments, p = 0.8937), although the signal per vesicle (the Syt1 copy number) remains unchanged. d , A visualization of PSDs (top and side views), after immunostaining PSD95 with the same nanobody used in a-c, and Shank2 and Homer1 with specific antibodies. The graph indicates the axial positioning, which agrees well with the literature . N = 11 measurements for each protein, 2 independent experiments; symbols show the medians, SEM and SD. e , Side view of a postsynapse displaying PSD95, MAP2 and two glutamate receptors (GluR2, AMPA type, and GluN2b, NMDA type). f , ONE images of PSD95 (top views), before or after the addition of 10% 1,6-hexanediol (Hex). g , Line scans through the PSD95 stainings shown in panel f. h , An analysis of PSD95 spot profiles; N = 10-7 synapses, Friedman test followed by Dunn-Sidak testing, p = 0.0027; the error bars show the SEM. For details on the analysis, see .

    Techniques Used: Labeling, MANN-WHITNEY, Immunostaining

    anti glur2 glua2  (Alomone Labs)


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    Alomone Labs anti glur2 glua2
    Anti Glur2 Glua2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    polyclonal rabbit glua2 antibody  (Alomone Labs)


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    Astaxanthin inhibits a [Ca 2+ ]i increase in cortical neurons upon ionotropic glutamate receptor activation. ( A – C ) The average [Ca 2+ ]i response in control (black) and AST (red) preincubated neurons stimulated with 50 μM each of NMDA (+ 5 μM glycine), AMPA and KA for 15 min (NMDA: Con n = 23, AST n = 42; AMPA: con n = 27, AST n = 23; KA con n = 30, AST n = 40). ( D ) Dot plot representing the total calcium (area under the curve) after 15 min of NMDA, AMPA and KA stimulation. Arrow heads indicate point of glutamate receptor agonist applications. ( E ) Representative protein expression levels of NMDA (GluN1), AMPA <t>(GluA2)</t> and KA (GluK123) detected by the Western blot analysis with β-actin as the internal reference (individual Western blots figure are provided in ). ( F ) Dot plot indicate the average normalized protein expression for GluN1, GluA2 and GluK123. Data are represented as mean ± SEM from 3–4 different experiments, * p < 0.05. n.s: non-significant.
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    Alomone Labs anti glur2 glua2
    Astaxanthin inhibits a [Ca 2+ ]i increase in cortical neurons upon ionotropic glutamate receptor activation. ( A – C ) The average [Ca 2+ ]i response in control (black) and AST (red) preincubated neurons stimulated with 50 μM each of NMDA (+ 5 μM glycine), AMPA and KA for 15 min (NMDA: Con n = 23, AST n = 42; AMPA: con n = 27, AST n = 23; KA con n = 30, AST n = 40). ( D ) Dot plot representing the total calcium (area under the curve) after 15 min of NMDA, AMPA and KA stimulation. Arrow heads indicate point of glutamate receptor agonist applications. ( E ) Representative protein expression levels of NMDA (GluN1), AMPA <t>(GluA2)</t> and KA (GluK123) detected by the Western blot analysis with β-actin as the internal reference (individual Western blots figure are provided in ). ( F ) Dot plot indicate the average normalized protein expression for GluN1, GluA2 and GluK123. Data are represented as mean ± SEM from 3–4 different experiments, * p < 0.05. n.s: non-significant.
    Anti Glur2 Glua2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
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    anti glur2 glua2 - by Bioz Stars, 2023-02
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    Alomone Labs polyclonal rabbit glua2 antibody
    Astaxanthin inhibits a [Ca 2+ ]i increase in cortical neurons upon ionotropic glutamate receptor activation. ( A – C ) The average [Ca 2+ ]i response in control (black) and AST (red) preincubated neurons stimulated with 50 μM each of NMDA (+ 5 μM glycine), AMPA and KA for 15 min (NMDA: Con n = 23, AST n = 42; AMPA: con n = 27, AST n = 23; KA con n = 30, AST n = 40). ( D ) Dot plot representing the total calcium (area under the curve) after 15 min of NMDA, AMPA and KA stimulation. Arrow heads indicate point of glutamate receptor agonist applications. ( E ) Representative protein expression levels of NMDA (GluN1), AMPA <t>(GluA2)</t> and KA (GluK123) detected by the Western blot analysis with β-actin as the internal reference (individual Western blots figure are provided in ). ( F ) Dot plot indicate the average normalized protein expression for GluN1, GluA2 and GluK123. Data are represented as mean ± SEM from 3–4 different experiments, * p < 0.05. n.s: non-significant.
    Polyclonal Rabbit Glua2 Antibody, 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/polyclonal rabbit glua2 antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyclonal rabbit glua2 antibody - by Bioz Stars, 2023-02
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    Image Search Results


    Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse Gria2 , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.

    Journal: Brain Communications

    Article Title: α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis

    doi: 10.1093/braincomms/fcac081

    Figure Lengend Snippet: Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse Gria2 , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.

    Article Snippet: Primary antibodies were as follows: chicken anti-GFP (1:1000; Abcam; AB13970), rabbit anti-NeuN (1:1000; Abcam; AB104225), goat anti-ChAT (1:500; Abcam; AB34419) and guinea pig anti-AMPA receptor 2 subunit (GluA2) (1:500; Alomone Labs; AGP-073).

    Techniques: Quantitative RT-PCR, Expressing

    Expression of GluA2 in spinal cords of embryonic SOD1 G93A mice. Cross-sections of lumbar spinal cord from WT (HB9:GFP; WT) and SOD1 G93A (SOD1 G93A ; HB9:GFP) mice at (A–J) E12.5 and ( K–T ) E17.5. Double-immunolabelling for GFP, GluA2 and NeuN (Neuronal nuclei). Plots represent quantification analysis of GluA2 signal intensity in HB9:GFP motor neurons at ( U ) E12.5 and ( V ) E17.5. Data represent mean ± SEM, unpaired student t -test performed on n = 4 biological replicates, ∼50 neurons analysed per biological replicate, * P < 0.05. Scale bars 50 μm.

    Journal: Brain Communications

    Article Title: α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis

    doi: 10.1093/braincomms/fcac081

    Figure Lengend Snippet: Expression of GluA2 in spinal cords of embryonic SOD1 G93A mice. Cross-sections of lumbar spinal cord from WT (HB9:GFP; WT) and SOD1 G93A (SOD1 G93A ; HB9:GFP) mice at (A–J) E12.5 and ( K–T ) E17.5. Double-immunolabelling for GFP, GluA2 and NeuN (Neuronal nuclei). Plots represent quantification analysis of GluA2 signal intensity in HB9:GFP motor neurons at ( U ) E12.5 and ( V ) E17.5. Data represent mean ± SEM, unpaired student t -test performed on n = 4 biological replicates, ∼50 neurons analysed per biological replicate, * P < 0.05. Scale bars 50 μm.

    Article Snippet: Primary antibodies were as follows: chicken anti-GFP (1:1000; Abcam; AB13970), rabbit anti-NeuN (1:1000; Abcam; AB104225), goat anti-ChAT (1:500; Abcam; AB34419) and guinea pig anti-AMPA receptor 2 subunit (GluA2) (1:500; Alomone Labs; AGP-073).

    Techniques: Expressing

    Expression of GRIA2 and ADAR2 in iPSC motor neurons derived from ALS patients with SOD1 mutations and healthy control lines. Representative images of iPSC mature motor neurons derived from ( A–E ) healthy control line and ( F–J ) SOD1 I114T line, immunolabelled with ChAT, GluA2 and TUJ1, counterstained with Hoechst. ( K ) Plot represents quantification analysis of GluA2 signal intensity in iPSC motor neurons. Data represent mean ± SEM, unpaired student t -test performed on n = 3 biological replicates, 50 neurons analysed per biological replicate. (L) Fold change expression of GRIA2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. ( M ) Fold change expression of ADAR2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. Data represent mean ± SEM, n = 3 biological replicates, one-way ANOVA with Dunnett's multiple comparison test, * P < 0.01, ** P < 0.005. Scale bars 50 μm.

    Journal: Brain Communications

    Article Title: α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis

    doi: 10.1093/braincomms/fcac081

    Figure Lengend Snippet: Expression of GRIA2 and ADAR2 in iPSC motor neurons derived from ALS patients with SOD1 mutations and healthy control lines. Representative images of iPSC mature motor neurons derived from ( A–E ) healthy control line and ( F–J ) SOD1 I114T line, immunolabelled with ChAT, GluA2 and TUJ1, counterstained with Hoechst. ( K ) Plot represents quantification analysis of GluA2 signal intensity in iPSC motor neurons. Data represent mean ± SEM, unpaired student t -test performed on n = 3 biological replicates, 50 neurons analysed per biological replicate. (L) Fold change expression of GRIA2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. ( M ) Fold change expression of ADAR2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. Data represent mean ± SEM, n = 3 biological replicates, one-way ANOVA with Dunnett's multiple comparison test, * P < 0.01, ** P < 0.005. Scale bars 50 μm.

    Article Snippet: Primary antibodies were as follows: chicken anti-GFP (1:1000; Abcam; AB13970), rabbit anti-NeuN (1:1000; Abcam; AB104225), goat anti-ChAT (1:500; Abcam; AB34419) and guinea pig anti-AMPA receptor 2 subunit (GluA2) (1:500; Alomone Labs; AGP-073).

    Techniques: Expressing, Derivative Assay, Quantitative RT-PCR

    Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse Gria2 , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.

    Journal: Brain Communications

    Article Title: α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis

    doi: 10.1093/braincomms/fcac081

    Figure Lengend Snippet: Validation of differentially expressed genes using qRT-PCR. ( A–E ) qPCR verification of the expression of genes involved in biological process identified as enriched by GO analysis compared with WT control. (F) Fold change expression of Ca 2+ -permeable AMPAR subunit Gria1 , Gria3 and Gria4 mRNAs, relative to WT motor neurons at E12.5. (G) Relative expression of Adarb1 mRNA in SOD1 G93A motor neurons at E12.5. ( H ) Schema showing the position of the fully complementary miR-124 target site at the 5′-end of the mouse Gria2 , 3′-UTR. The seed region of miR-124 is shown. Data represent mean ± SEM, unpaired student t -test, n = 5–7 biological replicates, * P < 0.05.

    Article Snippet: Cells were blocked in 10% (v/v) normal donkey serum with 0.1% (v/v) Triton-X 100 in 0.1 M PBS and incubated overnight at 4°C in the following primary antibodies: goat anti-ChAT (1:500, Millipore; AB144P), chicken anti-β III tubulin (1:1000, Abcam; AB41489) and rabbit anti-GluA2 (1:500; Alomone Labs; AGC-005).

    Techniques: Quantitative RT-PCR, Expressing

    Expression of GluA2 in spinal cords of embryonic SOD1 G93A mice. Cross-sections of lumbar spinal cord from WT (HB9:GFP; WT) and SOD1 G93A (SOD1 G93A ; HB9:GFP) mice at (A–J) E12.5 and ( K–T ) E17.5. Double-immunolabelling for GFP, GluA2 and NeuN (Neuronal nuclei). Plots represent quantification analysis of GluA2 signal intensity in HB9:GFP motor neurons at ( U ) E12.5 and ( V ) E17.5. Data represent mean ± SEM, unpaired student t -test performed on n = 4 biological replicates, ∼50 neurons analysed per biological replicate, * P < 0.05. Scale bars 50 μm.

    Journal: Brain Communications

    Article Title: α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis

    doi: 10.1093/braincomms/fcac081

    Figure Lengend Snippet: Expression of GluA2 in spinal cords of embryonic SOD1 G93A mice. Cross-sections of lumbar spinal cord from WT (HB9:GFP; WT) and SOD1 G93A (SOD1 G93A ; HB9:GFP) mice at (A–J) E12.5 and ( K–T ) E17.5. Double-immunolabelling for GFP, GluA2 and NeuN (Neuronal nuclei). Plots represent quantification analysis of GluA2 signal intensity in HB9:GFP motor neurons at ( U ) E12.5 and ( V ) E17.5. Data represent mean ± SEM, unpaired student t -test performed on n = 4 biological replicates, ∼50 neurons analysed per biological replicate, * P < 0.05. Scale bars 50 μm.

    Article Snippet: Cells were blocked in 10% (v/v) normal donkey serum with 0.1% (v/v) Triton-X 100 in 0.1 M PBS and incubated overnight at 4°C in the following primary antibodies: goat anti-ChAT (1:500, Millipore; AB144P), chicken anti-β III tubulin (1:1000, Abcam; AB41489) and rabbit anti-GluA2 (1:500; Alomone Labs; AGC-005).

    Techniques: Expressing

    Expression of GRIA2 and ADAR2 in iPSC motor neurons derived from ALS patients with SOD1 mutations and healthy control lines. Representative images of iPSC mature motor neurons derived from ( A–E ) healthy control line and ( F–J ) SOD1 I114T line, immunolabelled with ChAT, GluA2 and TUJ1, counterstained with Hoechst. ( K ) Plot represents quantification analysis of GluA2 signal intensity in iPSC motor neurons. Data represent mean ± SEM, unpaired student t -test performed on n = 3 biological replicates, 50 neurons analysed per biological replicate. (L) Fold change expression of GRIA2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. ( M ) Fold change expression of ADAR2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. Data represent mean ± SEM, n = 3 biological replicates, one-way ANOVA with Dunnett's multiple comparison test, * P < 0.01, ** P < 0.005. Scale bars 50 μm.

    Journal: Brain Communications

    Article Title: α-Amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptor and RNA processing gene dysregulation are early determinants of selective motor neuron vulnerability in a mouse model of amyotrophic lateral sclerosis

    doi: 10.1093/braincomms/fcac081

    Figure Lengend Snippet: Expression of GRIA2 and ADAR2 in iPSC motor neurons derived from ALS patients with SOD1 mutations and healthy control lines. Representative images of iPSC mature motor neurons derived from ( A–E ) healthy control line and ( F–J ) SOD1 I114T line, immunolabelled with ChAT, GluA2 and TUJ1, counterstained with Hoechst. ( K ) Plot represents quantification analysis of GluA2 signal intensity in iPSC motor neurons. Data represent mean ± SEM, unpaired student t -test performed on n = 3 biological replicates, 50 neurons analysed per biological replicate. (L) Fold change expression of GRIA2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. ( M ) Fold change expression of ADAR2 in SOD1 lines, compared with healthy control line determined by qRT-PCR. Data represent mean ± SEM, n = 3 biological replicates, one-way ANOVA with Dunnett's multiple comparison test, * P < 0.01, ** P < 0.005. Scale bars 50 μm.

    Article Snippet: Cells were blocked in 10% (v/v) normal donkey serum with 0.1% (v/v) Triton-X 100 in 0.1 M PBS and incubated overnight at 4°C in the following primary antibodies: goat anti-ChAT (1:500, Millipore; AB144P), chicken anti-β III tubulin (1:1000, Abcam; AB41489) and rabbit anti-GluA2 (1:500; Alomone Labs; AGC-005).

    Techniques: Expressing, Derivative Assay, Quantitative RT-PCR

    Time-dependent changes of protein expression levels of GluA1 (a), GluA2 (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC total homogenate of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01; ∗∗∗ p < 0.001.

    Journal: Neural Plasticity

    Article Title: Acute Footshock Stress Induces Time-Dependent Modifications of AMPA/NMDA Protein Expression and AMPA Phosphorylation

    doi: 10.1155/2016/7267865

    Figure Lengend Snippet: Time-dependent changes of protein expression levels of GluA1 (a), GluA2 (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC total homogenate of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01; ∗∗∗ p < 0.001.

    Article Snippet: AGC004, Alomone Labs, Jerusalem, Israel) and GluA2 (1 : 2500, cod.

    Techniques: Expressing

    Time-dependent changes of protein expression levels of GluA1 (a), GluA2 (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC postsynaptic spine membranes of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01.

    Journal: Neural Plasticity

    Article Title: Acute Footshock Stress Induces Time-Dependent Modifications of AMPA/NMDA Protein Expression and AMPA Phosphorylation

    doi: 10.1155/2016/7267865

    Figure Lengend Snippet: Time-dependent changes of protein expression levels of GluA1 (a), GluA2 (b), GluA1 phospho-Ser 831 (c), GluA1 phospho-Ser 845 (d), and GluA2 phospho-Ser 880 (e) in PFC/FC postsynaptic spine membranes of rats subjected to FS-stress and sacrificed immediately after stress and 2 h and 24 h from stress beginning. Data are represented as percentage of controls at each time point, as means ± SEM ( n = 8). Statistics: Generalized Linear Models (GLM) and Bonferroni Post Hoc Test (see for details). ∗∗ p < 0.01.

    Article Snippet: AGC004, Alomone Labs, Jerusalem, Israel) and GluA2 (1 : 2500, cod.

    Techniques: Expressing

    GluA2 expression levels in human postmortem HD and PD hippocampus and striatum. (a) No significant changes in GluA2 expression in HD or PD hippocampal regions. (b) GluA2 specific changes occur in the putamen (Put) of HD and PD tissue. * P < 0.05, ** P < 0.005. (c) Representative images are shown for GluA2 in the dentate gyrus, CA3 and CA1 regions of the hippocampus. (d) Representative images of GluA2 immunostaining in the caudate nucleus and putamen of the striatum. Scale bar for (c) and (d) is 25 μ m. (e) High power example image of GluA2 immunolabelling, showing the somatic and dendritic localisations.

    Journal: Journal of Neurodegenerative Diseases

    Article Title: Differential Changes in Postsynaptic Density Proteins in Postmortem Huntington's Disease and Parkinson's Disease Human Brains

    doi: 10.1155/2014/938530

    Figure Lengend Snippet: GluA2 expression levels in human postmortem HD and PD hippocampus and striatum. (a) No significant changes in GluA2 expression in HD or PD hippocampal regions. (b) GluA2 specific changes occur in the putamen (Put) of HD and PD tissue. * P < 0.05, ** P < 0.005. (c) Representative images are shown for GluA2 in the dentate gyrus, CA3 and CA1 regions of the hippocampus. (d) Representative images of GluA2 immunostaining in the caudate nucleus and putamen of the striatum. Scale bar for (c) and (d) is 25 μ m. (e) High power example image of GluA2 immunolabelling, showing the somatic and dendritic localisations.

    Article Snippet: Sections were then incubated for 72 hours (4°C) in primary antibodies against mouse GluA2 (Alomone) 1 : 200 (WT n = 6, YAC n = 5), rabbit PSD-95 (Sigma) 1 : 200 (WT n = 6, YAC n = 5), rabbit SAP97 (ABR) 1 : 1000 (WT n = 6, YAC n = 5), and mouse GluN1 (Neuromab) 1 : 300 (WT n = 5, YAC n = 6).

    Techniques: Expressing, Immunostaining

    Quantitative immunohistochemistry of SAP97, PSD-95, GluN1, and GluA2 expression in YAC128 hippocampal sections. Sections were prepared from symptomatic 1-year-old YAC128 mice to provide a comparison to the end stage of human HD. (a)–(d). Top: Quantification of (a) SAP97, (b) PSD-95, (c) GluA2, and (d) GluN1 levels in dentate gyrus (DG), area CA3, and area CA1. Below: Example immunohistochemical staining for each glutamatergic synaptic protein in the hippocampal CA1 region in control (wildtype) and YAC128 mice. (e) Immunohistochemical quantification of DARPP-32 expression in wild-type and YAC128 striatum (caudate putamen, CPu). * P < 0.05.

    Journal: Journal of Neurodegenerative Diseases

    Article Title: Differential Changes in Postsynaptic Density Proteins in Postmortem Huntington's Disease and Parkinson's Disease Human Brains

    doi: 10.1155/2014/938530

    Figure Lengend Snippet: Quantitative immunohistochemistry of SAP97, PSD-95, GluN1, and GluA2 expression in YAC128 hippocampal sections. Sections were prepared from symptomatic 1-year-old YAC128 mice to provide a comparison to the end stage of human HD. (a)–(d). Top: Quantification of (a) SAP97, (b) PSD-95, (c) GluA2, and (d) GluN1 levels in dentate gyrus (DG), area CA3, and area CA1. Below: Example immunohistochemical staining for each glutamatergic synaptic protein in the hippocampal CA1 region in control (wildtype) and YAC128 mice. (e) Immunohistochemical quantification of DARPP-32 expression in wild-type and YAC128 striatum (caudate putamen, CPu). * P < 0.05.

    Article Snippet: Sections were then incubated for 72 hours (4°C) in primary antibodies against mouse GluA2 (Alomone) 1 : 200 (WT n = 6, YAC n = 5), rabbit PSD-95 (Sigma) 1 : 200 (WT n = 6, YAC n = 5), rabbit SAP97 (ABR) 1 : 1000 (WT n = 6, YAC n = 5), and mouse GluN1 (Neuromab) 1 : 300 (WT n = 5, YAC n = 6).

    Techniques: Immunohistochemistry, Expressing, Immunohistochemical staining, Staining

    Astaxanthin inhibits a [Ca 2+ ]i increase in cortical neurons upon ionotropic glutamate receptor activation. ( A – C ) The average [Ca 2+ ]i response in control (black) and AST (red) preincubated neurons stimulated with 50 μM each of NMDA (+ 5 μM glycine), AMPA and KA for 15 min (NMDA: Con n = 23, AST n = 42; AMPA: con n = 27, AST n = 23; KA con n = 30, AST n = 40). ( D ) Dot plot representing the total calcium (area under the curve) after 15 min of NMDA, AMPA and KA stimulation. Arrow heads indicate point of glutamate receptor agonist applications. ( E ) Representative protein expression levels of NMDA (GluN1), AMPA (GluA2) and KA (GluK123) detected by the Western blot analysis with β-actin as the internal reference (individual Western blots figure are provided in ). ( F ) Dot plot indicate the average normalized protein expression for GluN1, GluA2 and GluK123. Data are represented as mean ± SEM from 3–4 different experiments, * p < 0.05. n.s: non-significant.

    Journal: Marine Drugs

    Article Title: Astaxanthin Protection against Neuronal Excitotoxicity via Glutamate Receptor Inhibition and Improvement of Mitochondrial Function

    doi: 10.3390/md20100645

    Figure Lengend Snippet: Astaxanthin inhibits a [Ca 2+ ]i increase in cortical neurons upon ionotropic glutamate receptor activation. ( A – C ) The average [Ca 2+ ]i response in control (black) and AST (red) preincubated neurons stimulated with 50 μM each of NMDA (+ 5 μM glycine), AMPA and KA for 15 min (NMDA: Con n = 23, AST n = 42; AMPA: con n = 27, AST n = 23; KA con n = 30, AST n = 40). ( D ) Dot plot representing the total calcium (area under the curve) after 15 min of NMDA, AMPA and KA stimulation. Arrow heads indicate point of glutamate receptor agonist applications. ( E ) Representative protein expression levels of NMDA (GluN1), AMPA (GluA2) and KA (GluK123) detected by the Western blot analysis with β-actin as the internal reference (individual Western blots figure are provided in ). ( F ) Dot plot indicate the average normalized protein expression for GluN1, GluA2 and GluK123. Data are represented as mean ± SEM from 3–4 different experiments, * p < 0.05. n.s: non-significant.

    Article Snippet: Membranes were then probed with specific primary antibodies GluN1 (NMDAR1, 1:1000, Alomone Lab Jerusalem, Israel), GluR2 (GluA2, 1:1000, Alomone Lab), GluK 123 (GluR 567, 1:2000, Santa Cruz, Dallas, TX, USA) and β-Actin, 1:2000, BD).

    Techniques: Activation Assay, Expressing, Western Blot