anti nr2b (Alomone Labs)

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Alomone Labs anti nr2b

Leptin signaling increases pNR2B Y1472 levels and surface expression. ( A ) Representative Western blot of hippocampal neurons treated with leptin (50 nM), PP1 (10 µM), or both for 2 hours. ( B ) Quantification of pNR2B Y1472 intensity normalized to total <t>NR2B</t> intensity (n = 3). ( C ) Representative Western blot of hippocampal protein extracts from P10 wild-type and ob/ob mice pups (wild-type: n = 5; ob/ob : n = 5). ( D ) Quantification of pNR2B Y1472 intensity normalized to total NR2B intensity and total NR2B intensity normalized to the neuronal marker MAP2B intensity (n = 3). ( E ) Representative Western blot of surface biotinylated hippocampal cultures treated with leptin (50 nM, 2 hours). Biotinylated proteins were affinity purified (AP) with streptavidin magnetic beads. ( F ) Quantification of biotinylated NR2B intensity normalized to NR2B intensity in total lysate (n = 3). All experiments were repeated in 3 independent culture preparations and expressed as the mean ± SEM, * P

Anti Nr2b, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti nr2b/product/Alomone Labs
Average 94 stars, based on 3 article reviews
Price from $9.99 to $1999.99

anti nr2b - by Bioz Stars, 2022-12

94/100 stars

Images

1) Product Images from "Leptin Controls Glutamatergic Synaptogenesis and NMDA-Receptor Trafficking via Fyn Kinase Regulation of NR2B"

Article Title: Leptin Controls Glutamatergic Synaptogenesis and NMDA-Receptor Trafficking via Fyn Kinase Regulation of NR2B

Journal: Endocrinology

doi: 10.1210/endocr/bqz030

Figure Legend Snippet: Leptin signaling increases pNR2B Y1472 levels and surface expression. ( A ) Representative Western blot of hippocampal neurons treated with leptin (50 nM), PP1 (10 µM), or both for 2 hours. ( B ) Quantification of pNR2B Y1472 intensity normalized to total NR2B intensity (n = 3). ( C ) Representative Western blot of hippocampal protein extracts from P10 wild-type and ob/ob mice pups (wild-type: n = 5; ob/ob : n = 5). ( D ) Quantification of pNR2B Y1472 intensity normalized to total NR2B intensity and total NR2B intensity normalized to the neuronal marker MAP2B intensity (n = 3). ( E ) Representative Western blot of surface biotinylated hippocampal cultures treated with leptin (50 nM, 2 hours). Biotinylated proteins were affinity purified (AP) with streptavidin magnetic beads. ( F ) Quantification of biotinylated NR2B intensity normalized to NR2B intensity in total lysate (n = 3). All experiments were repeated in 3 independent culture preparations and expressed as the mean ± SEM, * P

Techniques Used: Expressing, Western Blot, Mouse Assay, Marker, Affinity Purification, Magnetic Beads

Leptin-regulated NR2B Y1472 phosphorylation and surface expression is Fyn dependent. ( A ) Representative Western blot of HEK293T cells transfected with NR2B-V5, NR1, LepRb-myc, and either V5-Fyn or V5-DN Fyn and treated with leptin (50 nM, 2 hours). ( B ) Quantification of pNR2B Y1472 intensity normalized to total NR2B-V5 intensity (n = 3). ( C ) Hippocampal neurons were transfected with Clover and EGFP-NR2B-V5 and either V5-Fyn or V5-DN Fyn ± leptin stimulation (50 nM, 2 hours) and live immunostained for surface EGFP–NR2B. Quantification of immunostained EGFP-integrated signal density (n = 15). All experiments were repeated in 3 independent culture preparations and expressed as the mean ± SEM, * P

Figure Legend Snippet: Leptin-regulated NR2B Y1472 phosphorylation and surface expression is Fyn dependent. ( A ) Representative Western blot of HEK293T cells transfected with NR2B-V5, NR1, LepRb-myc, and either V5-Fyn or V5-DN Fyn and treated with leptin (50 nM, 2 hours). ( B ) Quantification of pNR2B Y1472 intensity normalized to total NR2B-V5 intensity (n = 3). ( C ) Hippocampal neurons were transfected with Clover and EGFP-NR2B-V5 and either V5-Fyn or V5-DN Fyn ± leptin stimulation (50 nM, 2 hours) and live immunostained for surface EGFP–NR2B. Quantification of immunostained EGFP-integrated signal density (n = 15). All experiments were repeated in 3 independent culture preparations and expressed as the mean ± SEM, * P

Techniques Used: Expressing, Western Blot, Transfection

LepRb directly interacts with NR2B. ( A ) Schematic of LepRb–BioID experiment with representative Western blot of NR2B-V5 immunoprecipitated from HEK293T cells expressing the designated BioID constructs and NR2B-V5 and NR1-Clover to the right. ( B ) Quantification of IP biotinylated NR2B-V5 intensity normalized to total NR2B-V5 intensity in the same lane (n = 3). ( C ) Schematic of NR2B–BioID experiment with representative Western blot of LepRb-V5 immunoprecipitated from HEK293T cells expressing designated BioID constructs and LepRb-V5 and NR1-Clover. ( D ) Representative Western blot of LepRb-myc immunoprecipitated from HEK293T cells stimulated with leptin (50 nM, 2 hours) and expressing LepRb-myc, NR2B-V5, and NR1-Clover. ( E ) Quantification of coimmunoprecipitated NR2B-V5 intensity normalized to immunoprecipitated LepRb-myc intensity from the same lane (n = 3). ( F ) Representative fluorescent images of hippocampal cultures expressing Flag-LepRb and Clover. Surface Flag-LepRb and endogenous surface NR2B were live immunostained after stimulation with leptin (50 nM, 2 hours). ( G ) Quantification of NR2B/Flag-LepRb puncta colocalization compared to total NR2B puncta. Colocalization experiments were repeated in 2 independent hippocampal culture preparations. All BioID experiments were stimulated with biotin (50 µM) at the time of transfection. All experiments were repeated in 3 independent culture preparations and expressed as the mean ± SEM, * P

Figure Legend Snippet: LepRb directly interacts with NR2B. ( A ) Schematic of LepRb–BioID experiment with representative Western blot of NR2B-V5 immunoprecipitated from HEK293T cells expressing the designated BioID constructs and NR2B-V5 and NR1-Clover to the right. ( B ) Quantification of IP biotinylated NR2B-V5 intensity normalized to total NR2B-V5 intensity in the same lane (n = 3). ( C ) Schematic of NR2B–BioID experiment with representative Western blot of LepRb-V5 immunoprecipitated from HEK293T cells expressing designated BioID constructs and LepRb-V5 and NR1-Clover. ( D ) Representative Western blot of LepRb-myc immunoprecipitated from HEK293T cells stimulated with leptin (50 nM, 2 hours) and expressing LepRb-myc, NR2B-V5, and NR1-Clover. ( E ) Quantification of coimmunoprecipitated NR2B-V5 intensity normalized to immunoprecipitated LepRb-myc intensity from the same lane (n = 3). ( F ) Representative fluorescent images of hippocampal cultures expressing Flag-LepRb and Clover. Surface Flag-LepRb and endogenous surface NR2B were live immunostained after stimulation with leptin (50 nM, 2 hours). ( G ) Quantification of NR2B/Flag-LepRb puncta colocalization compared to total NR2B puncta. Colocalization experiments were repeated in 2 independent hippocampal culture preparations. All BioID experiments were stimulated with biotin (50 µM) at the time of transfection. All experiments were repeated in 3 independent culture preparations and expressed as the mean ± SEM, * P

Techniques Used: Western Blot, Immunoprecipitation, Expressing, Construct, Transfection

pNR2B Y1472 is necessary for leptin-stimulated spine formation. ( A ) Representative fluorescent images of hippocampal neurons expressing Clover and EGFP-NR2B-V5 or EGFP-NR2B Y1472F -V5 ± leptin stimulation (50 nM, 2 hours) and live immunostained for surface EGFP-NR2B. White bar = 20 µm. ( B ) Quantification of immunostained EGFP-integrated signal density (n = 23). ( C-E ) Hippocampal neurons that were transfected with a fluorescent Clover-βactin and EGFP-NR2B Y1472F -V5. Neurons were stimulated with leptin (50 nM) on DIV8, and on DIV11 to 12 spine density was measured by hand using ImageJ with the NeuronJ plugin ( C,D ), or electrophysiological recordings were performed ( E ). White bar = 5 µm. ( D ) Quantification of dendritic spine density from a minimum of 2 to 3 dendritic segments from 15 neurons. ( E ) Quantification of mEPSC frequency, amplitude, and decay time normalized to control condition (control: n = 32; control + leptin: n = 34; NR2B Y1472F : n = 33; NR2B Y1472F + leptin: n = 33). All experiments were repeated in 3 independent culture preparations and expressed as the mean ± SEM, * P

Figure Legend Snippet: pNR2B Y1472 is necessary for leptin-stimulated spine formation. ( A ) Representative fluorescent images of hippocampal neurons expressing Clover and EGFP-NR2B-V5 or EGFP-NR2B Y1472F -V5 ± leptin stimulation (50 nM, 2 hours) and live immunostained for surface EGFP-NR2B. White bar = 20 µm. ( B ) Quantification of immunostained EGFP-integrated signal density (n = 23). ( C-E ) Hippocampal neurons that were transfected with a fluorescent Clover-βactin and EGFP-NR2B Y1472F -V5. Neurons were stimulated with leptin (50 nM) on DIV8, and on DIV11 to 12 spine density was measured by hand using ImageJ with the NeuronJ plugin ( C,D ), or electrophysiological recordings were performed ( E ). White bar = 5 µm. ( D ) Quantification of dendritic spine density from a minimum of 2 to 3 dendritic segments from 15 neurons. ( E ) Quantification of mEPSC frequency, amplitude, and decay time normalized to control condition (control: n = 32; control + leptin: n = 34; NR2B Y1472F : n = 33; NR2B Y1472F + leptin: n = 33). All experiments were repeated in 3 independent culture preparations and expressed as the mean ± SEM, * P

Techniques Used: Expressing, Transfection

2) Product Images from "N-methyl D-Aspartate Channels Link Ammonia and Epithelial Cell Death Mechanisms in Helicobacter pylori Infection"

Article Title: N-methyl D-Aspartate Channels Link Ammonia and Epithelial Cell Death Mechanisms in Helicobacter pylori Infection

Journal: Gastroenterology

doi: 10.1053/j.gastro.2011.08.048

NMDA channel subunit NR2B expression in surface, parietal, and chief cells is transcriptionally regulated in HP-infected tissues. Paraffin-embedded tissues from ( A ) sham- (Contr-20 wkPI) or ( B ) 6 and ( C ) 20 wkPI HP-infected mice were stained for the NR2B

Figure Legend Snippet: NMDA channel subunit NR2B expression in surface, parietal, and chief cells is transcriptionally regulated in HP-infected tissues. Paraffin-embedded tissues from ( A ) sham- (Contr-20 wkPI) or ( B ) 6 and ( C ) 20 wkPI HP-infected mice were stained for the NR2B

Techniques Used: Expressing, Infection, Mouse Assay, Staining

3) Product Images from "CXCL12 inhibits expression of the NMDA receptor's NR2B subunit through a histone deacetylase-dependent pathway contributing to neuronal survival"

Article Title: CXCL12 inhibits expression of the NMDA receptor's NR2B subunit through a histone deacetylase-dependent pathway contributing to neuronal survival

Journal: Cell Death & Disease

doi: 10.1038/cddis.2010.10

In vivo AMD3100 administration increases NR2B protein levels in the rat cortex. ( a ) AMD3100 treatment decreases CXCR4 phosphorylation in brain slices of treated animals as detected through immunohistochemistry, using phospho-specific antibodies against ligand-activated CXCR4. Three animals per group were analyzed and no changes were observed in total levels of CXCR4. ( b ) Studies in homogenized tissue samples (cerebral cortex and hippocampus) also show a reduction in phosphorylated levels of CXCR4 compared with total CXCR4 ( * P

Figure Legend Snippet: In vivo AMD3100 administration increases NR2B protein levels in the rat cortex. ( a ) AMD3100 treatment decreases CXCR4 phosphorylation in brain slices of treated animals as detected through immunohistochemistry, using phospho-specific antibodies against ligand-activated CXCR4. Three animals per group were analyzed and no changes were observed in total levels of CXCR4. ( b ) Studies in homogenized tissue samples (cerebral cortex and hippocampus) also show a reduction in phosphorylated levels of CXCR4 compared with total CXCR4 ( * P

Techniques Used: In Vivo, Immunohistochemistry

CXCL12 treatment reduces levels of NR2B protein and mRNA but does not alter other NMDA subunits. ( a ) Addition of CXCL12 (20 nM, 1–24 h) to neuronal culture media decreases NR2B protein levels in a time-dependent manner. Graph shows data from three independent experiments ( * P

Figure Legend Snippet: CXCL12 treatment reduces levels of NR2B protein and mRNA but does not alter other NMDA subunits. ( a ) Addition of CXCL12 (20 nM, 1–24 h) to neuronal culture media decreases NR2B protein levels in a time-dependent manner. Graph shows data from three independent experiments ( * P

Techniques Used:

CXCL12 reduces global histone H3 acetylation in neurons, and histone deacetylase (HDAC) inhibitors prevent the effects of CXCL12 on the NR2B. ( a ) Global H3 acetylation levels were measured through a colorimetric acetylation assay as indicated in the ‘Materials and methods' section. Reduced levels of histone acetylation were found in CXCL12-treated (20 nM) neurons compared with control; this effect is blocked by cotreatment with TSA (100 nM) ( * P

Figure Legend Snippet: CXCL12 reduces global histone H3 acetylation in neurons, and histone deacetylase (HDAC) inhibitors prevent the effects of CXCL12 on the NR2B. ( a ) Global H3 acetylation levels were measured through a colorimetric acetylation assay as indicated in the ‘Materials and methods' section. Reduced levels of histone acetylation were found in CXCL12-treated (20 nM) neurons compared with control; this effect is blocked by cotreatment with TSA (100 nM) ( * P

Techniques Used: Histone Deacetylase Assay, Acetylation Assay