mouse anti-glun2a antibody (Millipore)
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Mouse Anti Glun2a Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti-glun2a/glun2a+antibody/pm37930965-80-47-50
Average 90 stars, based on 1 article reviews
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other:Article Title: miR-146a and miR-200b alter cognition by targeting NMDA receptor subunits Article Snippet: The primary antibodies used were: rabbit anti-GluN1 (1:1000, Abcam), rabbit anti-GluN2B (1:1000, Abcam), Article Title: Subtype selective NMDA receptor antagonists induce recovery of synapses lost following exposure to HIV-1 Tat. Article Snippet: After permeabilization, the cells were incubated with Article Title: Intracellular zinc signaling influences NMDA receptor function by enhancing the interaction of ZnT1 with GluN2A. Article Snippet: Zinc, loaded into glutamate-containing presynaptic vesicles and released into the synapse in an activitydependent manner, modulates neurotransmission through its actions on postsynaptic targets, prominently via high-affinity inhibition of GluN2A-containing NMDA receptors.. Recently, we identified a postsynaptic transport mechanism that regulates endogenous zinc inhibition of NMDARs.. In this new model of zinc regulation, the postsynaptic transporter ZnT1 mediates zinc inhibition of NMDARs by binding to GluN2A. Article Title: Subtype selective NMDA receptor antagonists induce recovery of synapses lost following exposure to HIV-1 Tat Article Snippet: After permeabilization, the cells were incubated with Article Title: Immunohistochemical localization of ionotropic glutamate receptors in the rat red nucleus Article Snippet: The sections were incubated in |
![Expression of <t>GluN2A</t> (A) and GluN2B (B) and basal extracellular levels of L‐glutamate (C) and D‐serine (D) in 4‐weeks and 8‐weeks of age S286L‐TG and wild‐type littermate. Ordinates indicate mean ± SD ( n = 6) of (A) expression levels of GluN2A relative to GAPDH in the plasma membrane fraction (B) expression levels of GluN2B relative to GAPDH in the plasma membrane fraction, (C) basal extracellular L‐glutamate level (μM) and (D) basal extracellular D‐serine level (μM) in the frontal cortex of wild‐type (gray column) and S286L‐TG (blue column). The lower‐side panels in A and B indicate pseudo‐gel images of capillary immunoblotting. Circles indicate the values of each individual rat. * p < 0.05, relative to 4‐weeks of age (4 W) and # p < 0.05 relative to wild‐type using two‐way ANOVA with Scheffe's post hoc test. F ‐values were in (A) expression of GluN2A ( F age [1, 20] = 46.7 [ p < 0.05], F genotype [1, 20] = 5.34 [ p < 0.05], F age*genotype [1, 20] = 1.1 [ p > 0.05]), (B) expression of GluN2B ( F age [1, 20] = 22.4 [ p < 0.05], F genotype [1, 20] = 8.3 [ p < 0.05], F age*genotype [1, 20] = 2.0 [ p > 0.05]), (C) L‐glutamate level ( F age [1, 20] = 3.2 [ p > 0.05], F genotype [1, 20] = 21.2 [ p < 0.05], F age*genotype [1, 20] = 1.9 [ p > 0.05]) and (D) D‐serine level ( F age [1, 20] = 8.4 [ p < 0.05], F genotype [1, 20] = 21.6 [ p < 0.05], F age*genotype [1, 20] = 2.8 [ p > 0.05]).](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9079/pmc13109079/pmc13109079__PRP2-14-e70256-g002.jpg)
