anti psd 95 antibody  (Alomone Labs)


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    Alomone Labs anti psd 95 antibody
    <t>PSD-95</t> expression pattern depends on culture duration. ( A , B ) Representative tdTomato-positive hRGCs ( red ) cultured for 1 ( A ) and 4 ( B ) weeks and immunolabeled against PSD-95 ( green ). Scale bar = 20 µm. ( C ) PSD-95 labeling within hRGC somas significantly decreased after 4 weeks versus earlier time points ( P ≤ 0.033). ( D ) Quantification of PSD-95 labeling within hRGC primary neurites. PSD-95 labeling significantly increased by 3 and 4 weeks in culture compared with 1-week cells. Significance indicators: * comparison with 1-week cells, # comparison with 2-week cells, ^ comparison with 3-week cells. Statistics: one-way analysis of variance, Tukey post hoc test ( C , D ). Data are mean ± standard error of the mean.
    Anti Psd 95 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti psd 95 antibody/product/Alomone Labs
    Average 93 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    anti psd 95 antibody - by Bioz Stars, 2022-12
    93/100 stars

    Images

    1) Product Images from "Intrinsic Morphologic and Physiologic Development of Human Derived Retinal Ganglion Cells In Vitro"

    Article Title: Intrinsic Morphologic and Physiologic Development of Human Derived Retinal Ganglion Cells In Vitro

    Journal: Translational Vision Science & Technology

    doi: 10.1167/tvst.10.10.1

    PSD-95 expression pattern depends on culture duration. ( A , B ) Representative tdTomato-positive hRGCs ( red ) cultured for 1 ( A ) and 4 ( B ) weeks and immunolabeled against PSD-95 ( green ). Scale bar = 20 µm. ( C ) PSD-95 labeling within hRGC somas significantly decreased after 4 weeks versus earlier time points ( P ≤ 0.033). ( D ) Quantification of PSD-95 labeling within hRGC primary neurites. PSD-95 labeling significantly increased by 3 and 4 weeks in culture compared with 1-week cells. Significance indicators: * comparison with 1-week cells, # comparison with 2-week cells, ^ comparison with 3-week cells. Statistics: one-way analysis of variance, Tukey post hoc test ( C , D ). Data are mean ± standard error of the mean.
    Figure Legend Snippet: PSD-95 expression pattern depends on culture duration. ( A , B ) Representative tdTomato-positive hRGCs ( red ) cultured for 1 ( A ) and 4 ( B ) weeks and immunolabeled against PSD-95 ( green ). Scale bar = 20 µm. ( C ) PSD-95 labeling within hRGC somas significantly decreased after 4 weeks versus earlier time points ( P ≤ 0.033). ( D ) Quantification of PSD-95 labeling within hRGC primary neurites. PSD-95 labeling significantly increased by 3 and 4 weeks in culture compared with 1-week cells. Significance indicators: * comparison with 1-week cells, # comparison with 2-week cells, ^ comparison with 3-week cells. Statistics: one-way analysis of variance, Tukey post hoc test ( C , D ). Data are mean ± standard error of the mean.

    Techniques Used: Expressing, Cell Culture, Immunolabeling, Labeling

    2) Product Images from "ERβ and ApoE isoforms interact to regulate BDNF–5-HT2A signaling and synaptic function in the female brain"

    Article Title: ERβ and ApoE isoforms interact to regulate BDNF–5-HT2A signaling and synaptic function in the female brain

    Journal: Alzheimer's Research & Therapy

    doi: 10.1186/s13195-017-0305-3

    Estrogen receptor β activation leads to an upregulation of select postsynaptic proteins independent of apolipoprotein E (ApoE) status. Three-month-old human ApoE2, ApoE3, and ApoE4 gene-targeted replacement female mice were treated with a phytoestrogenic estrogen receptor β-selective modulator (phyto-β-SERM)-supplemented diet or a control diet for 3 months and killed at the age of 6 months. Cortical tissues were probed for a ) PSD95 and b ) SHANK3 immunoreactivity. The integrated density value of the bands in Western blots was determined using densitometry, and data were normalized to an internal loading control (β-tubulin) and to the untreated group of each genotype. Data are shown as mean ± SD ( n = 5). * p
    Figure Legend Snippet: Estrogen receptor β activation leads to an upregulation of select postsynaptic proteins independent of apolipoprotein E (ApoE) status. Three-month-old human ApoE2, ApoE3, and ApoE4 gene-targeted replacement female mice were treated with a phytoestrogenic estrogen receptor β-selective modulator (phyto-β-SERM)-supplemented diet or a control diet for 3 months and killed at the age of 6 months. Cortical tissues were probed for a ) PSD95 and b ) SHANK3 immunoreactivity. The integrated density value of the bands in Western blots was determined using densitometry, and data were normalized to an internal loading control (β-tubulin) and to the untreated group of each genotype. Data are shown as mean ± SD ( n = 5). * p

    Techniques Used: Activation Assay, Mouse Assay, Western Blot

    Pre- and postsynaptic proteins are differentially modulated by apolipoprotein E (ApoE) isoforms. Expression levels of ( a ) presynaptic proteins synaptophysin and synaptobrevin2, and ( b ) postsynaptic proteins PSD95 and SHANK3 were examined in the cortices of 6-month-old human ApoE2, ApoE3, and ApoE4 gene-targeted replacement female mice. The integrated density value of the bands in Western blots was determined using densitometry, and data were normalized to an internal loading control (β-tubulin) and to the ApoE2 group. Data are shown as mean ± SD ( n = 5). * p
    Figure Legend Snippet: Pre- and postsynaptic proteins are differentially modulated by apolipoprotein E (ApoE) isoforms. Expression levels of ( a ) presynaptic proteins synaptophysin and synaptobrevin2, and ( b ) postsynaptic proteins PSD95 and SHANK3 were examined in the cortices of 6-month-old human ApoE2, ApoE3, and ApoE4 gene-targeted replacement female mice. The integrated density value of the bands in Western blots was determined using densitometry, and data were normalized to an internal loading control (β-tubulin) and to the ApoE2 group. Data are shown as mean ± SD ( n = 5). * p

    Techniques Used: Expressing, Mouse Assay, Western Blot

    3) Product Images from "Trafficking of the NMDAR2B Receptor Subunit Distal Cytoplasmic Tail from Endoplasmic Reticulum to the Synapse"

    Article Title: Trafficking of the NMDAR2B Receptor Subunit Distal Cytoplasmic Tail from Endoplasmic Reticulum to the Synapse

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0039585

    VE-2B interacted directly with SAP102, and VE-2B, SAP102 and PSD-95 formed co-clusters. (A) Western blotting was performed on cortical neurons infected with VE-2B and immunoprecipitated with i1 antibody to VSVG at 10 minutes and 3 hours after switch to permissive temperature (24 fold enrichment). Immunoblots were performed with rabbit anti-VSVG, PSD-95, and SAP102. Input, unbound, and immunoprecipitation fractions (IP) were run for each blot. To minimize the possibility of false-positives, buffer only was added to the lanes adjacent to the VE-2B IP lanes. Identical film exposure times for both anti-PSD-95 and anti-SAP102 indicate that SAP102 associates at 10 minutes and 3 hours after ER exit whereas PSD-95 does not. Longer film exposure times did not unambiguously indicate that PSD-95 was directly associated. (B) Western blotting was performed on cortical neurons infected with VE and immunoprecipitated with antibody to VSVG at 10 minutes after switch to permissive temperature. Immunoblots were then performed with rabbit anti-VSVG, and SAP102. Input, unbound, and IP fractions were run for each blot. The results indicated that VE (left panel) did not co-immunoprecipitate measurable quantities of SAP102 (right panel). (C) VE-2B transfected neurons 3 hours after ER release were immunostained for PSD-95 (red) and SAP102 (blue; scale bar, 5 µm). Aqua-colored arrows indicate VE-2B co-localized with SAP102 primarily. White arrows indicate VE-2B co-localized with both PSD-95 and SAP102.
    Figure Legend Snippet: VE-2B interacted directly with SAP102, and VE-2B, SAP102 and PSD-95 formed co-clusters. (A) Western blotting was performed on cortical neurons infected with VE-2B and immunoprecipitated with i1 antibody to VSVG at 10 minutes and 3 hours after switch to permissive temperature (24 fold enrichment). Immunoblots were performed with rabbit anti-VSVG, PSD-95, and SAP102. Input, unbound, and immunoprecipitation fractions (IP) were run for each blot. To minimize the possibility of false-positives, buffer only was added to the lanes adjacent to the VE-2B IP lanes. Identical film exposure times for both anti-PSD-95 and anti-SAP102 indicate that SAP102 associates at 10 minutes and 3 hours after ER exit whereas PSD-95 does not. Longer film exposure times did not unambiguously indicate that PSD-95 was directly associated. (B) Western blotting was performed on cortical neurons infected with VE and immunoprecipitated with antibody to VSVG at 10 minutes after switch to permissive temperature. Immunoblots were then performed with rabbit anti-VSVG, and SAP102. Input, unbound, and IP fractions were run for each blot. The results indicated that VE (left panel) did not co-immunoprecipitate measurable quantities of SAP102 (right panel). (C) VE-2B transfected neurons 3 hours after ER release were immunostained for PSD-95 (red) and SAP102 (blue; scale bar, 5 µm). Aqua-colored arrows indicate VE-2B co-localized with SAP102 primarily. White arrows indicate VE-2B co-localized with both PSD-95 and SAP102.

    Techniques Used: Western Blot, Infection, Immunoprecipitation, Transfection

    VE-2B co-localized with PSD-95 from the TGN to the plasma membrane. (A) At 10 minutes after release from the ER, VE-2B showed little colocalization with antibody staining to endogenous PSD-95 in the soma (top panels; scale bars are 10 µm). Forty-five minutes after ER release (second row), a time point at which the leading edge of VE-2B reaches the surface, PSD-95 showed significant colocalization with VE-2B. Similar results were obtained with VE-2A (see Table S1 ). (B) Colocalization with PSD-95 was also evident in dendrites at 45 minutes and later time points, such as 3 hours (see Fig. 6). VE-2B (top panel) showed co-localization with endogenous PSD-95 (middle panel) in dendrites at 45 minutes after permissive temperature, and later (scale bar 5 µm). (C) Neurons transfected with VE-2B were subjected to 40°C then the medium was exchanged with medium equilibrated at 20°C. Cultures were maintained at 20°C for 1 hour to allow VE-2B cargo exiting the ER to build up in the TGN. Immunostaining for endogenous TGN38 (a TGN marker; top panels) and PSD-95 (second row) in VE-2B transfected neurons subjected to the 20°C temperature manipulation showed robust colocalization (scale bars 5 µm). (D) Quantification of PSD-95 co-localization at different stages of the secretory pathway. There was a significant difference among the groups using a one-way Anova. However, post hoc comparisons demonstrated an insignificant pairwise difference at 10 minutes following ER exit. PSD-95 showed levels of co-localization with VE-2B (open circles) not significantly different from those of VE-2BΔ7 (filled triangles) 10 minutes after ER release. Forty-five minutes after ER exit, VE-2B co-localization with PSD-95 (filled circles) was significantly enhanced at most thresholds when compared to VE-2B colocalization at 10 minutes after ER exit. The significant increase in colocalization of VE-2B with PSD-95 seen at 45 minutes after ER exit could be reproduced by switching media to 20°C for 1 hour (open squares). To verify that VE-2B was concentrated in the TGN after 1 hour 20°C incubation, colocalization of VE-2B with TGN38 was quantified (filled squares).
    Figure Legend Snippet: VE-2B co-localized with PSD-95 from the TGN to the plasma membrane. (A) At 10 minutes after release from the ER, VE-2B showed little colocalization with antibody staining to endogenous PSD-95 in the soma (top panels; scale bars are 10 µm). Forty-five minutes after ER release (second row), a time point at which the leading edge of VE-2B reaches the surface, PSD-95 showed significant colocalization with VE-2B. Similar results were obtained with VE-2A (see Table S1 ). (B) Colocalization with PSD-95 was also evident in dendrites at 45 minutes and later time points, such as 3 hours (see Fig. 6). VE-2B (top panel) showed co-localization with endogenous PSD-95 (middle panel) in dendrites at 45 minutes after permissive temperature, and later (scale bar 5 µm). (C) Neurons transfected with VE-2B were subjected to 40°C then the medium was exchanged with medium equilibrated at 20°C. Cultures were maintained at 20°C for 1 hour to allow VE-2B cargo exiting the ER to build up in the TGN. Immunostaining for endogenous TGN38 (a TGN marker; top panels) and PSD-95 (second row) in VE-2B transfected neurons subjected to the 20°C temperature manipulation showed robust colocalization (scale bars 5 µm). (D) Quantification of PSD-95 co-localization at different stages of the secretory pathway. There was a significant difference among the groups using a one-way Anova. However, post hoc comparisons demonstrated an insignificant pairwise difference at 10 minutes following ER exit. PSD-95 showed levels of co-localization with VE-2B (open circles) not significantly different from those of VE-2BΔ7 (filled triangles) 10 minutes after ER release. Forty-five minutes after ER exit, VE-2B co-localization with PSD-95 (filled circles) was significantly enhanced at most thresholds when compared to VE-2B colocalization at 10 minutes after ER exit. The significant increase in colocalization of VE-2B with PSD-95 seen at 45 minutes after ER exit could be reproduced by switching media to 20°C for 1 hour (open squares). To verify that VE-2B was concentrated in the TGN after 1 hour 20°C incubation, colocalization of VE-2B with TGN38 was quantified (filled squares).

    Techniques Used: Staining, Transfection, Immunostaining, Marker, Incubation

    VE-2B and the MAGUKs are consistent with co-transportation to the synapse. (A) VE-2B chimeras co-localized with high intensity PSD-95 (left graph) and SAP102 (right graph) in dendrites 3 hours after release with the red threshold fixed at 4X background (104–255 inclusive gray scale). Colocalization was quantified as described in Experimental Methods. VE, VE-2B, and VE-2BΔ7 colocalization was assessed across the range of inclusive thresholds for green indicated on the x-axis. There was a significant group effect by one-way Anova even at even the lowest green threshold (p
    Figure Legend Snippet: VE-2B and the MAGUKs are consistent with co-transportation to the synapse. (A) VE-2B chimeras co-localized with high intensity PSD-95 (left graph) and SAP102 (right graph) in dendrites 3 hours after release with the red threshold fixed at 4X background (104–255 inclusive gray scale). Colocalization was quantified as described in Experimental Methods. VE, VE-2B, and VE-2BΔ7 colocalization was assessed across the range of inclusive thresholds for green indicated on the x-axis. There was a significant group effect by one-way Anova even at even the lowest green threshold (p

    Techniques Used:

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    Alomone Labs anti psd 95 antibody
    <t>PSD-95</t> expression pattern depends on culture duration. ( A , B ) Representative tdTomato-positive hRGCs ( red ) cultured for 1 ( A ) and 4 ( B ) weeks and immunolabeled against PSD-95 ( green ). Scale bar = 20 µm. ( C ) PSD-95 labeling within hRGC somas significantly decreased after 4 weeks versus earlier time points ( P ≤ 0.033). ( D ) Quantification of PSD-95 labeling within hRGC primary neurites. PSD-95 labeling significantly increased by 3 and 4 weeks in culture compared with 1-week cells. Significance indicators: * comparison with 1-week cells, # comparison with 2-week cells, ^ comparison with 3-week cells. Statistics: one-way analysis of variance, Tukey post hoc test ( C , D ). Data are mean ± standard error of the mean.
    Anti Psd 95 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti psd 95 antibody/product/Alomone Labs
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    anti psd 95 antibody - by Bioz Stars, 2022-12
    93/100 stars
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    PSD-95 expression pattern depends on culture duration. ( A , B ) Representative tdTomato-positive hRGCs ( red ) cultured for 1 ( A ) and 4 ( B ) weeks and immunolabeled against PSD-95 ( green ). Scale bar = 20 µm. ( C ) PSD-95 labeling within hRGC somas significantly decreased after 4 weeks versus earlier time points ( P ≤ 0.033). ( D ) Quantification of PSD-95 labeling within hRGC primary neurites. PSD-95 labeling significantly increased by 3 and 4 weeks in culture compared with 1-week cells. Significance indicators: * comparison with 1-week cells, # comparison with 2-week cells, ^ comparison with 3-week cells. Statistics: one-way analysis of variance, Tukey post hoc test ( C , D ). Data are mean ± standard error of the mean.

    Journal: Translational Vision Science & Technology

    Article Title: Intrinsic Morphologic and Physiologic Development of Human Derived Retinal Ganglion Cells In Vitro

    doi: 10.1167/tvst.10.10.1

    Figure Lengend Snippet: PSD-95 expression pattern depends on culture duration. ( A , B ) Representative tdTomato-positive hRGCs ( red ) cultured for 1 ( A ) and 4 ( B ) weeks and immunolabeled against PSD-95 ( green ). Scale bar = 20 µm. ( C ) PSD-95 labeling within hRGC somas significantly decreased after 4 weeks versus earlier time points ( P ≤ 0.033). ( D ) Quantification of PSD-95 labeling within hRGC primary neurites. PSD-95 labeling significantly increased by 3 and 4 weeks in culture compared with 1-week cells. Significance indicators: * comparison with 1-week cells, # comparison with 2-week cells, ^ comparison with 3-week cells. Statistics: one-way analysis of variance, Tukey post hoc test ( C , D ). Data are mean ± standard error of the mean.

    Article Snippet: After electrophysiologic recordings, hRGCs were fixed with 4% paraformaldehyde overnight at 4°C and immunolabeled with the following primary antibodies: RNA-binding protein with multiple splicing (RBPMS, GTX118619,1:200, Genetex, Irvine, CA) postsynaptic density 95 (PSD-95, APZ-009, 1:400, Alomone Labs, Jerusalem, Israel), and AnkG (338800, 1:250, Invitrogen, Carlsbad, CA).

    Techniques: Expressing, Cell Culture, Immunolabeling, Labeling

    Estrogen receptor β activation leads to an upregulation of select postsynaptic proteins independent of apolipoprotein E (ApoE) status. Three-month-old human ApoE2, ApoE3, and ApoE4 gene-targeted replacement female mice were treated with a phytoestrogenic estrogen receptor β-selective modulator (phyto-β-SERM)-supplemented diet or a control diet for 3 months and killed at the age of 6 months. Cortical tissues were probed for a ) PSD95 and b ) SHANK3 immunoreactivity. The integrated density value of the bands in Western blots was determined using densitometry, and data were normalized to an internal loading control (β-tubulin) and to the untreated group of each genotype. Data are shown as mean ± SD ( n = 5). * p

    Journal: Alzheimer's Research & Therapy

    Article Title: ERβ and ApoE isoforms interact to regulate BDNF–5-HT2A signaling and synaptic function in the female brain

    doi: 10.1186/s13195-017-0305-3

    Figure Lengend Snippet: Estrogen receptor β activation leads to an upregulation of select postsynaptic proteins independent of apolipoprotein E (ApoE) status. Three-month-old human ApoE2, ApoE3, and ApoE4 gene-targeted replacement female mice were treated with a phytoestrogenic estrogen receptor β-selective modulator (phyto-β-SERM)-supplemented diet or a control diet for 3 months and killed at the age of 6 months. Cortical tissues were probed for a ) PSD95 and b ) SHANK3 immunoreactivity. The integrated density value of the bands in Western blots was determined using densitometry, and data were normalized to an internal loading control (β-tubulin) and to the untreated group of each genotype. Data are shown as mean ± SD ( n = 5). * p

    Article Snippet: The following primary antibodies were used: rabbit polyclonal anti-BDNF (1:500; Santa Cruz Biotechnology, Dallas, TX, USA), rabbit polyclonal anti-tropomyosin receptor kinase B (anti-TrkB, 1:1000; Abcam, Cambridge, MA, USA), mouse monoclonal anti-β tubulin (1:3000; Thermo Fisher Scientific, Waltham, MA, USA), rabbit polyclonal anti-PSD95 (1:500; Alomone Labs, Jerusalem, Israel), rabbit monoclonal anti-synaptophysin (1:1000; Abcam), mouse monoclonal anti-SHANK3 (1:1000; NeuroMab/Antibodies Inc., Davis, CA, USA), rabbit polyclonal anti-synaptobrevin 2 (1:1000; Enzo Life Sciences, Farmingdale, NY, USA), rabbit polyclonal anti-5-hydroxytryptamine (serotonin) (anti-5-HT1A , 1:1000; Abcam), and rabbit polyclonal anti-5-HT2A (1:20,000; a generous gift from Dr. Nancy Muma).

    Techniques: Activation Assay, Mouse Assay, Western Blot

    Pre- and postsynaptic proteins are differentially modulated by apolipoprotein E (ApoE) isoforms. Expression levels of ( a ) presynaptic proteins synaptophysin and synaptobrevin2, and ( b ) postsynaptic proteins PSD95 and SHANK3 were examined in the cortices of 6-month-old human ApoE2, ApoE3, and ApoE4 gene-targeted replacement female mice. The integrated density value of the bands in Western blots was determined using densitometry, and data were normalized to an internal loading control (β-tubulin) and to the ApoE2 group. Data are shown as mean ± SD ( n = 5). * p

    Journal: Alzheimer's Research & Therapy

    Article Title: ERβ and ApoE isoforms interact to regulate BDNF–5-HT2A signaling and synaptic function in the female brain

    doi: 10.1186/s13195-017-0305-3

    Figure Lengend Snippet: Pre- and postsynaptic proteins are differentially modulated by apolipoprotein E (ApoE) isoforms. Expression levels of ( a ) presynaptic proteins synaptophysin and synaptobrevin2, and ( b ) postsynaptic proteins PSD95 and SHANK3 were examined in the cortices of 6-month-old human ApoE2, ApoE3, and ApoE4 gene-targeted replacement female mice. The integrated density value of the bands in Western blots was determined using densitometry, and data were normalized to an internal loading control (β-tubulin) and to the ApoE2 group. Data are shown as mean ± SD ( n = 5). * p

    Article Snippet: The following primary antibodies were used: rabbit polyclonal anti-BDNF (1:500; Santa Cruz Biotechnology, Dallas, TX, USA), rabbit polyclonal anti-tropomyosin receptor kinase B (anti-TrkB, 1:1000; Abcam, Cambridge, MA, USA), mouse monoclonal anti-β tubulin (1:3000; Thermo Fisher Scientific, Waltham, MA, USA), rabbit polyclonal anti-PSD95 (1:500; Alomone Labs, Jerusalem, Israel), rabbit monoclonal anti-synaptophysin (1:1000; Abcam), mouse monoclonal anti-SHANK3 (1:1000; NeuroMab/Antibodies Inc., Davis, CA, USA), rabbit polyclonal anti-synaptobrevin 2 (1:1000; Enzo Life Sciences, Farmingdale, NY, USA), rabbit polyclonal anti-5-hydroxytryptamine (serotonin) (anti-5-HT1A , 1:1000; Abcam), and rabbit polyclonal anti-5-HT2A (1:20,000; a generous gift from Dr. Nancy Muma).

    Techniques: Expressing, Mouse Assay, Western Blot