glua2 n-terminus Search Results


glur2  (Alomone Labs)
93
Alomone Labs glur2
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: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/glua2+n-terminus/Anti-GluR2+(GluA2)+(extracellular)+Antibody/bio_rxiv__2022__08__03__502284-163-23-24
Average 93 stars, based on 1 article reviews
glur2 - by Bioz Stars, 2026-09
93/100 stars
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glua2 (n-terminus) alomone agp-073  (Alomone Labs)
93
Alomone Labs glua2 (n-terminus) alomone agp-073
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 .
Glua2 (N Terminus) Alomone Agp 073, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/glua2+n-terminus/Guinea+pig+Anti-GluR2+(GluA2)+(extracellular)+Antibody/pmc08814153__41467_2022_28301_MOESM2_ESM-29-46-48
Average 93 stars, based on 1 article reviews
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rabbit anti glur2  (Cell Signaling Technology Inc)
94
Cell Signaling Technology Inc rabbit anti glur2
Statistical results for measured mRNA
Rabbit Anti Glur2, supplied by Cell Signaling Technology Inc, 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/product/glua2+n-terminus/AMPA+Receptor+2+(GluA2)+Rabbit+mAb/pmc03605311-121-91-90
Average 94 stars, based on 1 article reviews
rabbit anti glur2 - by Bioz Stars, 2026-09
94/100 stars
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Image Search Results


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 .

Journal: bioRxiv

Article Title: Expansion microscopy at one nanometer resolution

doi: 10.1101/2022.08.03.502284

Figure Lengend 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 .

Article Snippet: The primary antibodies used were anti synaptotagmin1 (SYT1, #105011 Synaptic Systems), anti Homer1 (#160 003, Synpatic Systems), anti Shank2 (#162204 Synaptic Systems), anti GluR2 (Alomone Labs, #AGC-005, Jerusalem, Israel), anti GluN2b (Neuromab 75-101, California, USA), anti MAP2 (Novus Biologicals #NB300-213), anti vGluT1 (#135304, Synaptic Systems), anti Bassoon (#ADI-VAM-PS003-F, Enzo, New York, USA).

Techniques: Labeling, Extraction, MANN-WHITNEY, Immunostaining

Statistical results for measured mRNA

Journal: Neuroscience

Article Title: Connexin and AMPA Receptor Expression Changes Over Time in the Rat Olfactory Bulb

doi: 10.1016/j.neuroscience.2012.06.070

Figure Lengend Snippet: Statistical results for measured mRNA

Article Snippet: Primary antisera used in this study were purchased from Cell Signaling Technology (CST; Danvers, MA, USA), Invitrogen, Millipore (Billerica, MA, USA), and Sigma–Aldrich and are as follows, with the epitope, dilution/buffer, and catalog number in parentheses: Invitrogen rabbit anti-Cx36 (cytoplasmic loop between second and third transmembrane domains; 1:250 in 4% milk/TBST; 51-6200), Invitrogen rabbit anti-Cx36 (C-terminus; 1:250 in 1% milk/TBST; 51-6300), Invitrogen mouse anti-Cx36 (C-terminus; 1:500 in 4% milk/TBST; 37-4600), Invitrogen rabbit anti-Cx43 (C-terminus; 1:500 in OBBT; 71-0700), Invitrogen rabbit anti-Cx45 (C-terminus; 1:250/OBBT; 40-7000), Millipore mouse anti-GluR1 (N-terminus; 1:500/OBBT; MAB2263), CST rabbit anti-GluR2 (N-terminus; 1:500/OBBT; 5306S), CST rabbit anti-GluR3 (residues surrounding Pro590 of human GluR3; 1:1500/OBBT; 4676S), CST rabbit anti-GluR4 (residues surrounding Gln890 of human GluR4; 1:1000 in 5% bovine serum albumin/TBST*; 8070S), CST mouse anti-β-III-tubulin (C-terminus; 1:2000/OBBT; 4466S), and Sigma–Aldrich rabbit anti-β-III-tubulin (residues 442–446; 1:5000 in 4% milk/TBST; SAB4300623).

Techniques:

Changes in α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) subunit mRNA across dark and light phases in rat OB. Line plots of (A) GluR1, (B) GluR2, (C) GluR3, and (D) GluR4 mRNA expression over 48-h. Sample size and notation as in Fig. 1. GluR1, GluR2, and GluR3 mRNA changes were statistically significant across the 48-h (Kruskal–Wallis H test, P < 0.05) but only GluR1 was rhythmic for both 24-h periods (harmonic regression analysis, P < 0.05). GluR1 and GluR4 were rhythmic according to JTK_CYCLE analysis (P < 0.05).

Journal: Neuroscience

Article Title: Connexin and AMPA Receptor Expression Changes Over Time in the Rat Olfactory Bulb

doi: 10.1016/j.neuroscience.2012.06.070

Figure Lengend Snippet: Changes in α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) subunit mRNA across dark and light phases in rat OB. Line plots of (A) GluR1, (B) GluR2, (C) GluR3, and (D) GluR4 mRNA expression over 48-h. Sample size and notation as in Fig. 1. GluR1, GluR2, and GluR3 mRNA changes were statistically significant across the 48-h (Kruskal–Wallis H test, P < 0.05) but only GluR1 was rhythmic for both 24-h periods (harmonic regression analysis, P < 0.05). GluR1 and GluR4 were rhythmic according to JTK_CYCLE analysis (P < 0.05).

Article Snippet: Primary antisera used in this study were purchased from Cell Signaling Technology (CST; Danvers, MA, USA), Invitrogen, Millipore (Billerica, MA, USA), and Sigma–Aldrich and are as follows, with the epitope, dilution/buffer, and catalog number in parentheses: Invitrogen rabbit anti-Cx36 (cytoplasmic loop between second and third transmembrane domains; 1:250 in 4% milk/TBST; 51-6200), Invitrogen rabbit anti-Cx36 (C-terminus; 1:250 in 1% milk/TBST; 51-6300), Invitrogen mouse anti-Cx36 (C-terminus; 1:500 in 4% milk/TBST; 37-4600), Invitrogen rabbit anti-Cx43 (C-terminus; 1:500 in OBBT; 71-0700), Invitrogen rabbit anti-Cx45 (C-terminus; 1:250/OBBT; 40-7000), Millipore mouse anti-GluR1 (N-terminus; 1:500/OBBT; MAB2263), CST rabbit anti-GluR2 (N-terminus; 1:500/OBBT; 5306S), CST rabbit anti-GluR3 (residues surrounding Pro590 of human GluR3; 1:1500/OBBT; 4676S), CST rabbit anti-GluR4 (residues surrounding Gln890 of human GluR4; 1:1000 in 5% bovine serum albumin/TBST*; 8070S), CST mouse anti-β-III-tubulin (C-terminus; 1:2000/OBBT; 4466S), and Sigma–Aldrich rabbit anti-β-III-tubulin (residues 442–446; 1:5000 in 4% milk/TBST; SAB4300623).

Techniques: Expressing

Changes in AMPAR subunit protein expressed in the rat OB membrane across light and dark phases in rat OB. (A) Anti-GluR1 (1:500) and (B) anti-GluR2 (1:500) using experimental design, analysis, notation, sample size, and statistical metric as in Fig. 4. Nitrocellulose blots were stripped and reprobed with anti-β-III-tubulin (1:2000). Arrows indicate expected size in kilodaltons (Mr = 110 kDa for GluR1, 100 kDa for GluR2, and 50 kDa for tubulin). GluR1 and GluR2 protein changes were statistically significant across the 48 h (Kruskal–Wallis H test, P < 0.05) but only GluR2 protein expression was rhythmic in the 24-h tested (harmonic regression analysis, P < 0.05). GluR1 and GluR2 protein expression was statistically significant for JTK_CYCLE analysis (P < 0.05).

Journal: Neuroscience

Article Title: Connexin and AMPA Receptor Expression Changes Over Time in the Rat Olfactory Bulb

doi: 10.1016/j.neuroscience.2012.06.070

Figure Lengend Snippet: Changes in AMPAR subunit protein expressed in the rat OB membrane across light and dark phases in rat OB. (A) Anti-GluR1 (1:500) and (B) anti-GluR2 (1:500) using experimental design, analysis, notation, sample size, and statistical metric as in Fig. 4. Nitrocellulose blots were stripped and reprobed with anti-β-III-tubulin (1:2000). Arrows indicate expected size in kilodaltons (Mr = 110 kDa for GluR1, 100 kDa for GluR2, and 50 kDa for tubulin). GluR1 and GluR2 protein changes were statistically significant across the 48 h (Kruskal–Wallis H test, P < 0.05) but only GluR2 protein expression was rhythmic in the 24-h tested (harmonic regression analysis, P < 0.05). GluR1 and GluR2 protein expression was statistically significant for JTK_CYCLE analysis (P < 0.05).

Article Snippet: Primary antisera used in this study were purchased from Cell Signaling Technology (CST; Danvers, MA, USA), Invitrogen, Millipore (Billerica, MA, USA), and Sigma–Aldrich and are as follows, with the epitope, dilution/buffer, and catalog number in parentheses: Invitrogen rabbit anti-Cx36 (cytoplasmic loop between second and third transmembrane domains; 1:250 in 4% milk/TBST; 51-6200), Invitrogen rabbit anti-Cx36 (C-terminus; 1:250 in 1% milk/TBST; 51-6300), Invitrogen mouse anti-Cx36 (C-terminus; 1:500 in 4% milk/TBST; 37-4600), Invitrogen rabbit anti-Cx43 (C-terminus; 1:500 in OBBT; 71-0700), Invitrogen rabbit anti-Cx45 (C-terminus; 1:250/OBBT; 40-7000), Millipore mouse anti-GluR1 (N-terminus; 1:500/OBBT; MAB2263), CST rabbit anti-GluR2 (N-terminus; 1:500/OBBT; 5306S), CST rabbit anti-GluR3 (residues surrounding Pro590 of human GluR3; 1:1500/OBBT; 4676S), CST rabbit anti-GluR4 (residues surrounding Gln890 of human GluR4; 1:1000 in 5% bovine serum albumin/TBST*; 8070S), CST mouse anti-β-III-tubulin (C-terminus; 1:2000/OBBT; 4466S), and Sigma–Aldrich rabbit anti-β-III-tubulin (residues 442–446; 1:5000 in 4% milk/TBST; SAB4300623).

Techniques: Expressing

Statistical results for measured membrane/organelle protein

Journal: Neuroscience

Article Title: Connexin and AMPA Receptor Expression Changes Over Time in the Rat Olfactory Bulb

doi: 10.1016/j.neuroscience.2012.06.070

Figure Lengend Snippet: Statistical results for measured membrane/organelle protein

Article Snippet: Primary antisera used in this study were purchased from Cell Signaling Technology (CST; Danvers, MA, USA), Invitrogen, Millipore (Billerica, MA, USA), and Sigma–Aldrich and are as follows, with the epitope, dilution/buffer, and catalog number in parentheses: Invitrogen rabbit anti-Cx36 (cytoplasmic loop between second and third transmembrane domains; 1:250 in 4% milk/TBST; 51-6200), Invitrogen rabbit anti-Cx36 (C-terminus; 1:250 in 1% milk/TBST; 51-6300), Invitrogen mouse anti-Cx36 (C-terminus; 1:500 in 4% milk/TBST; 37-4600), Invitrogen rabbit anti-Cx43 (C-terminus; 1:500 in OBBT; 71-0700), Invitrogen rabbit anti-Cx45 (C-terminus; 1:250/OBBT; 40-7000), Millipore mouse anti-GluR1 (N-terminus; 1:500/OBBT; MAB2263), CST rabbit anti-GluR2 (N-terminus; 1:500/OBBT; 5306S), CST rabbit anti-GluR3 (residues surrounding Pro590 of human GluR3; 1:1500/OBBT; 4676S), CST rabbit anti-GluR4 (residues surrounding Gln890 of human GluR4; 1:1000 in 5% bovine serum albumin/TBST*; 8070S), CST mouse anti-β-III-tubulin (C-terminus; 1:2000/OBBT; 4466S), and Sigma–Aldrich rabbit anti-β-III-tubulin (residues 442–446; 1:5000 in 4% milk/TBST; SAB4300623).

Techniques: