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Cell Signaling Technology Inc rabbit anti nr2a
Rabbit Anti Nr2a, supplied by Cell Signaling Technology Inc, 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/product/anti+nr2a/sec_filing____878719_slash_000119312517004357_slash_d277182dncsr-117-32-43
Average 86 stars, based on 1 article reviews

rabbit anti nr2a - by Bioz Stars, 2026-11

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Article Title: Chronic postoperative pain induces contextual fear extinction dysfunction through hippocampal NMDAR/BDNF/TrkB signaling pathway in mice.
Article Snippet: Proteins in the lysed tissue were separated using 10% and 13.5% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to nitrocellulose membranes (PVDF) (Millipore, Bedford, MA, USA). .. The membrane was blocked using TBST containing 0.1% Tween-20 and 5% skim milk, followed by incubation with the following antibodies: anti-NR2A(1:1000, #4205S, Cell Signaling Technology, USA); anti-NR2B(1:1000, #14544S, Cell Signaling Technology, USA); anti-ERK1/2(1:1000, #4695 T, Cell Signaling Technology, USA); anti-P-p44/42MAPK(1:1000, #9101S, Cell Signaling Technology, USA); anti-CREB(1:1000, #9197 T, Cell Signaling Technology, USA); anti-P-CREB(1:1000, #9198S, Cell Signaling Technology, USA); antiBDNF(1:1000, #EPR1292, Abcam, USA); anti-β3-Tubllin(1:1000, #5666S, Cell Signaling Technology, USA); anti-PSD-95(1:1000, #2507S, Cell Signaling Technology, USA); anti-TrkB(1:1000, #4603, Cell Signaling Technology, USA); anti-TrkB(B-3) (1:500, #sc-7268, Santa Cruz Biotechnology, USA). .. The membranes were then incubated with HRP-conjugated anti-rabbit and anti-mouse IgG (Cell Signaling Technology, USA) for 1 h at room temperature and washed.

Article Title: Electroacupuncture Exerts Analgesic Effects by Restoring Hyperactivity via Cannabinoid Type 1 Receptors in the Anterior Cingulate Cortex in Chronic Inflammatory Pain.
Article Snippet: After the membrane was washed with TBST solution, the membrane was blocked at room temperature for 15 min with Quick Blocking Buffer (Beyotime, China). .. After washing again, the membrane was soaked in primary antibodies, including anti-CB1R (1:1000, rabbit, Abcam), anti-NR2A (1:1000, rabbit, CST), anti-NR2B (1:1000, rabbit, CST), anti-NR1 (1:1000, rabbit, Abcam), and anti-HINT1(1:1000, rabbit, Abcam), and placed in a 4 °C refrigerator overnight. .. Finally, after the membrane was washed, the goat anti-rabbit HRP-conjugated secondary antibodies (1:10000, Abcam) were incubated at room temperature for 2 h. The membrane was immersed in enhanced chemiluminescence (ECL) luminescent solution (Meilunbio, China) and then western blotting was observed using a chemiluminescence system (Peiqing Technology Co, China).

Article Title: Chronic postoperative pain induces contextual fear extinction dysfunction through hippocampal NMDAR/BDNF/TrkB signaling pathway in mice
Article Snippet: Proteins in the lysed tissue were separated using 10% and 13.5% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to nitrocellulose membranes (PVDF) (Millipore, Bedford, MA, USA). .. The membrane was blocked using TBST containing 0.1% Tween-20 and 5% skim milk, followed by incubation with the following antibodies: anti-NR2A(1:1000, #4205S, Cell Signaling Technology, USA); anti-NR2B(1:1000, #14544S, Cell Signaling Technology, USA); anti-ERK1/2(1:1000, #4695 T, Cell Signaling Technology, USA); anti-P-p44/42MAPK(1:1000, #9101S, Cell Signaling Technology, USA); anti-CREB(1:1000, #9197 T, Cell Signaling Technology, USA); anti-P-CREB(1:1000, #9198S, Cell Signaling Technology, USA); anti-BDNF(1:1000, #EPR1292, Abcam, USA); anti-β3-Tubllin(1:1000, #5666S, Cell Signaling Technology, USA); anti-PSD-95(1:1000, #2507S, Cell Signaling Technology, USA); anti-TrkB(1:1000, #4603, Cell Signaling Technology, USA); anti-TrkB(B-3) (1:500, #sc-7268, Santa Cruz Biotechnology, USA). .. The membranes were then incubated with HRP-conjugated anti-rabbit and anti-mouse IgG (Cell Signaling Technology, USA) for 1 h at room temperature and washed.

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Article Title: Enhancing HIF-1α–P2X2 signaling in dorsal raphe serotonergic neurons promotes psychological resilience
Article Snippet: Cytoplasmic and nuclear extracts from brain tissues were separated using NE-PER Nuclear and Cytoplasmic Extraction Reagents (#78833; Thermo Fisher Scientific, Waltham, MA, USA).

Article Title: EphB1-NR2B receptor signaling in glutamatergic neurons of the ventroposteromedial thalamic nucleus regulates emergence from anesthesia.
Article Snippet: The Imaris microscopy image analysis software (Oxford Instruments) was used to correct for mechanical drift and tracing neurons, and the mean intensity of MQAE and GCaMP6f fluorescence signals in each cell was averaged over the whole- cell body area and extracted for each time point using the Fiji software (https:// fiji.sc).

Article Title: Neuroligin 1 Regulates Autistic‐Like Repetitive Behavior through Modulating the Activity of Striatal D2 Receptor‐Expressing Medium Spiny Neurons
Article Snippet: Primary antibodies include anti‐NLGN1 (1:2000; Cat# 129013, Synaptic System), anti‐NLGN2 (1:2000; Cat# 129203, Synaptic System), anti‐NLGN3 (1:2000; Cat#129103, Synaptic System), anti‐GluA1 (1:2000; Cat# MAB2263, Millipore), anti‐GluA2 (1:2000; Cat# MAB397, Millipore), anti‐NR1 (1:2000; Cat# 5704, Cell Signaling Technology), anti‐NR2A (1:2000; Cat# 4205, Cell Signaling Technology), anti‐NR2B (1:2000; Cat# 14544, Cell Signaling Technology), anti‐HA (1:2000; Cat# 51064‐2‐AP, Proteintech), anti‐Drd1(1:2000; Cat# 17934‐1‐AP, Proteintech), anti‐Drd2 (Cat# 55084‐1‐AP, Proteintech), anti‐PKC(1:2000, Cat# 2056, Cell Signaling Technology), anti‐PKC alpha (phospho T497) (1:2000; Cat# ab76016, Abcam), anti‐PKA C‐α(1:2000; Cat#5842, Cell Signaling Technology), anti‐phospho‐PKA C (Thr197) (1:2000; Cat#5661, Cell Signaling Technology), anti‐Erk1/2 (1:2000; Cat#4695, Cell Signaling Technology), anti‐phospho‐Erk1/2 (Thr202/Tyr204) (1:2000; Cat#4370, Cell Signaling Technology), anti‐p38 MAPK (1:2000; Cat#9212, Cell Signaling Technology), anti‐Phospho‐p38 MAPK (Thr180/Tyr182) (1:2000; Cat#4511,Cell Signaling Technology), anti‐ChAT (1:50; Cat#AB144, Sigma‐Aldrich), anti‐GAPDH (1:4000; Cat# 60004‐1‐Ig, Proteintech).

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ZIP1 and ZIP3 localization in the DCN. A . Immunofluorescent imaging of DCN slices labeled with ZnT3 (red) and the postsynaptic markers GluN2A or CaMKII (green). B . Immunofluorescent staining of ZnT3, ZIP1 or ZIP3 (red) with the synaptic terminal marker VGLUT1 (green). C . GluN2A or CaMKII (green) immunofluorescent co-labeling with ZnT1, ZIP1 or ZIP3 (red), bottom panels show colocalization analyses, represented by Mander’s colocalization coefficient, calculated between the postsynaptic marker and each of the Zn 2+ transporters. For GluN2A colocalization, Tukey’s multiple comparisons test analysis shows a significant difference between ZnT3 and ZIP3 p-value: 0.016, as well as between ZnT3 and ZnT1 p-value: 0.031, F (1.669, 4.451) = 22.32. In case of CaMKII, Tukey’s multiple comparisons test shows significance for ZIP3 p-value: 0.009 and ZnT1 p-value: 0.016, F (3, 15) = 7.202. D . Immunofluorescent staining of PAX6 or Tbr2 (green) with ZIP1 or ZIP3 (red). The colocalization analyses for PAX6, bottom panel, shows Mander’s coefficients of the two Zn 2+ transporters (Mann Whitney test, p-value: 0.003). White arrows indicate examples of cells that show co-localization of the markers

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: ZIP-ZnT1 complexes mediate a local Zn 2+ -cycle regulating neuronal Zn²⁺ transport

doi: 10.1007/s00018-026-06137-w

Figure Lengend Snippet: ZIP1 and ZIP3 localization in the DCN. A . Immunofluorescent imaging of DCN slices labeled with ZnT3 (red) and the postsynaptic markers GluN2A or CaMKII (green). B . Immunofluorescent staining of ZnT3, ZIP1 or ZIP3 (red) with the synaptic terminal marker VGLUT1 (green). C . GluN2A or CaMKII (green) immunofluorescent co-labeling with ZnT1, ZIP1 or ZIP3 (red), bottom panels show colocalization analyses, represented by Mander’s colocalization coefficient, calculated between the postsynaptic marker and each of the Zn 2+ transporters. For GluN2A colocalization, Tukey’s multiple comparisons test analysis shows a significant difference between ZnT3 and ZIP3 p-value: 0.016, as well as between ZnT3 and ZnT1 p-value: 0.031, F (1.669, 4.451) = 22.32. In case of CaMKII, Tukey’s multiple comparisons test shows significance for ZIP3 p-value: 0.009 and ZnT1 p-value: 0.016, F (3, 15) = 7.202. D . Immunofluorescent staining of PAX6 or Tbr2 (green) with ZIP1 or ZIP3 (red). The colocalization analyses for PAX6, bottom panel, shows Mander’s coefficients of the two Zn 2+ transporters (Mann Whitney test, p-value: 0.003). White arrows indicate examples of cells that show co-localization of the markers

Article Snippet: GluN2A , NeuroMab , 75,288 , 1:300.

Techniques: Imaging, Labeling, Staining, Marker, MANN-WHITNEY

ZIP3 and ZnT1 are in direct contact, which enhances ZnT1 efflux rates. A. Co-immunoprecipitation assay in SH-SY5Y cells over expressing ZnT1 and ZIP3, with or without the murine subunit GluN2A (mGluN2A) or the human glutamate receptor (hGluN2A) subunit. The samples were immunoprecipitated with an antibody against ZnT1. The lysates were then separated on SDS-PAGE and subjected to immunoblotting with antibodies against ZIP3, representative of 3 repetitions. Lysis buffer shown as control. B. Co-immunoprecipitation in HEK293 cells expressing ZnT1 and ZIP3. Samples were immunoprecipitated either with an antibody against ZnT1 (left) or ZIP3 (right). Lysates were then separated on SDS-PAGE and subjected to immunoblotting with antibodies against ZIP3 or ZnT1, representative of 3 repetitions. Lysisbuffer shown as control. Note that expected MW for ZIP3 is 37kDa, identified MW likelyrepresents its dimerization and glycosylation; full blots shown in Supplementary Information. C. Representative traces of FluoZin-3 fluorescence changes in SH-SY5Y cells expressing ZnT1+ZIP3 (orange) or ZnT1+PCDNA as control (blue). Cells were perfused with 200μM Zn2+ in Ringer’s solution added with or without pyrithione (see Methods) at the indicated time. The initial Zn 2+ influx and efflux rates were monitored and compared between the two conditions. Unpaired ttest analysis, *** p-value: 0.0003, t(28)=4.131

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: ZIP-ZnT1 complexes mediate a local Zn 2+ -cycle regulating neuronal Zn²⁺ transport

doi: 10.1007/s00018-026-06137-w

Figure Lengend Snippet: ZIP3 and ZnT1 are in direct contact, which enhances ZnT1 efflux rates. A. Co-immunoprecipitation assay in SH-SY5Y cells over expressing ZnT1 and ZIP3, with or without the murine subunit GluN2A (mGluN2A) or the human glutamate receptor (hGluN2A) subunit. The samples were immunoprecipitated with an antibody against ZnT1. The lysates were then separated on SDS-PAGE and subjected to immunoblotting with antibodies against ZIP3, representative of 3 repetitions. Lysis buffer shown as control. B. Co-immunoprecipitation in HEK293 cells expressing ZnT1 and ZIP3. Samples were immunoprecipitated either with an antibody against ZnT1 (left) or ZIP3 (right). Lysates were then separated on SDS-PAGE and subjected to immunoblotting with antibodies against ZIP3 or ZnT1, representative of 3 repetitions. Lysisbuffer shown as control. Note that expected MW for ZIP3 is 37kDa, identified MW likelyrepresents its dimerization and glycosylation; full blots shown in Supplementary Information. C. Representative traces of FluoZin-3 fluorescence changes in SH-SY5Y cells expressing ZnT1+ZIP3 (orange) or ZnT1+PCDNA as control (blue). Cells were perfused with 200μM Zn2+ in Ringer’s solution added with or without pyrithione (see Methods) at the indicated time. The initial Zn 2+ influx and efflux rates were monitored and compared between the two conditions. Unpaired ttest analysis, *** p-value: 0.0003, t(28)=4.131

Article Snippet: GluN2A , NeuroMab , 75,288 , 1:300.

Techniques: Co-Immunoprecipitation Assay, Expressing, Immunoprecipitation, SDS Page, Western Blot, Lysis, Control, Glycoproteomics, Fluorescence

ZIP3- ZnT1 physical interaction in DCN cartwheel cells. A . Proximity ligation assay (PLA) performed on DCN slices using probes for GluN2A and either ZnT1, ZIP3, or ZIP1. Analysis of PLA puncta (red) was done on the molecular layer (outlined in white) to assess protein–protein interactions in postsynaptic cells of the parallel fibers. The graph (right panel) quantifies PLA puncta normalized to ZnT1-GluN2A puncta. Statistical analysis Dunnett’s multiple comparisons test, p-value: 0.0014, F (2, 11) = 11. B . Co-immunoprecipitation assay using DCN and hippocampal lysates. Protein samples were immunoprecipitated with antibodies against GluN2A, followed by SDS-PAGE separation and immunoblotting with antibodies against ZIP3 to confirm physical interactions. Note that expected MW for ZIP3 is 37 kDa, identified MW likely represents its dimerization and glycosylation; full blots shown in Supplementary Information. C . Schematic representation of Zn 2+ transporters in DCN, indicating the ZIP3-ZnT1-GluN2A complex on the cartwheel cells of the DCN

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: ZIP-ZnT1 complexes mediate a local Zn 2+ -cycle regulating neuronal Zn²⁺ transport

doi: 10.1007/s00018-026-06137-w

Figure Lengend Snippet: ZIP3- ZnT1 physical interaction in DCN cartwheel cells. A . Proximity ligation assay (PLA) performed on DCN slices using probes for GluN2A and either ZnT1, ZIP3, or ZIP1. Analysis of PLA puncta (red) was done on the molecular layer (outlined in white) to assess protein–protein interactions in postsynaptic cells of the parallel fibers. The graph (right panel) quantifies PLA puncta normalized to ZnT1-GluN2A puncta. Statistical analysis Dunnett’s multiple comparisons test, p-value: 0.0014, F (2, 11) = 11. B . Co-immunoprecipitation assay using DCN and hippocampal lysates. Protein samples were immunoprecipitated with antibodies against GluN2A, followed by SDS-PAGE separation and immunoblotting with antibodies against ZIP3 to confirm physical interactions. Note that expected MW for ZIP3 is 37 kDa, identified MW likely represents its dimerization and glycosylation; full blots shown in Supplementary Information. C . Schematic representation of Zn 2+ transporters in DCN, indicating the ZIP3-ZnT1-GluN2A complex on the cartwheel cells of the DCN

Article Snippet: GluN2A , NeuroMab , 75,288 , 1:300.

Techniques: Proximity Ligation Assay, Protein-Protein interactions, Co-Immunoprecipitation Assay, Immunoprecipitation, SDS Page, Western Blot, Glycoproteomics

ZIP1- ZnT1 physical interaction in the hippocampus. A . Co-immunoprecipitation assay using SH-SY5Y cells that were immunoprecipitated with ZnT1 and then exposed to ZIP1 (left panel) or ZIP3 (right panel) antibodies. Note that the right panel is taken from the gel presented in Fig. , the right lane for mGluN2A-ZIP3-ZnT1 expressing cells overlaps with that figure. Note that expected MW for ZIP3 is 37 kDa, identified MW likely represents its dimerization and glycosylation; full blots shown in Supplementary Information. B . Representative traces of fluorescent imaging of FluoZin-3 changes in SH-SY5Y cells expressing ZnT1 + ZIP1 (green) or ZnT1 + PCDNA as control (blue). Cells were perfused with 200 µM Zn 2+ in Ringer’s solution added at the indicated time, with or without pyrithione (see methods). The initial Zn 2+ influx (middle panel) and efflux (right panel) rates are shown in the bar graphs. Unpaired t-test analysis, *** p-value: 0.0001, t(23) = 5.613. C . Co-immunoprecipitation assay using DCN and hippocampal lysates. Protein samples were immunoprecipitated with antibodies against ZIP1, followed by SDS-PAGE separation and immunoblotting with antibodies against GluN2A. D . Proximity ligation assay (PLA) performed on CA3 hippocampal slices using probes for GluN2A and either ZnT1 or ZIP1. Red puncta represent the GluN2A-ZnT1 or ZIP1 interaction in the CA3 pyramidal cell layer (marked by white lines). Analysis of PLA puncta, performed with the GluN2A and either ZnT1, ZIP1 or ZIP3, on CA3 pyramidal layer to assess protein–protein interactions in postsynaptic cells. The graph (bottom panel) quantifies PLA puncta normalized to ZnT1-GluN2A puncta. Statistical analysis Dunnett’s multiple comparisons test, p-value: 0.013, F (2, 6) = 9.81. E . Schematic presentation of the Zn 2+ -cycle proteins, ZIP1-ZnT1-GluN2A, expressed on the postsynaptic CA3 pyramidal cells that are adjacent to the ZnT-3 and ZIP3 expressing mossy fiber terminals, consistent with previous work

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: ZIP-ZnT1 complexes mediate a local Zn 2+ -cycle regulating neuronal Zn²⁺ transport

doi: 10.1007/s00018-026-06137-w

Figure Lengend Snippet: ZIP1- ZnT1 physical interaction in the hippocampus. A . Co-immunoprecipitation assay using SH-SY5Y cells that were immunoprecipitated with ZnT1 and then exposed to ZIP1 (left panel) or ZIP3 (right panel) antibodies. Note that the right panel is taken from the gel presented in Fig. , the right lane for mGluN2A-ZIP3-ZnT1 expressing cells overlaps with that figure. Note that expected MW for ZIP3 is 37 kDa, identified MW likely represents its dimerization and glycosylation; full blots shown in Supplementary Information. B . Representative traces of fluorescent imaging of FluoZin-3 changes in SH-SY5Y cells expressing ZnT1 + ZIP1 (green) or ZnT1 + PCDNA as control (blue). Cells were perfused with 200 µM Zn 2+ in Ringer’s solution added at the indicated time, with or without pyrithione (see methods). The initial Zn 2+ influx (middle panel) and efflux (right panel) rates are shown in the bar graphs. Unpaired t-test analysis, *** p-value: 0.0001, t(23) = 5.613. C . Co-immunoprecipitation assay using DCN and hippocampal lysates. Protein samples were immunoprecipitated with antibodies against ZIP1, followed by SDS-PAGE separation and immunoblotting with antibodies against GluN2A. D . Proximity ligation assay (PLA) performed on CA3 hippocampal slices using probes for GluN2A and either ZnT1 or ZIP1. Red puncta represent the GluN2A-ZnT1 or ZIP1 interaction in the CA3 pyramidal cell layer (marked by white lines). Analysis of PLA puncta, performed with the GluN2A and either ZnT1, ZIP1 or ZIP3, on CA3 pyramidal layer to assess protein–protein interactions in postsynaptic cells. The graph (bottom panel) quantifies PLA puncta normalized to ZnT1-GluN2A puncta. Statistical analysis Dunnett’s multiple comparisons test, p-value: 0.013, F (2, 6) = 9.81. E . Schematic presentation of the Zn 2+ -cycle proteins, ZIP1-ZnT1-GluN2A, expressed on the postsynaptic CA3 pyramidal cells that are adjacent to the ZnT-3 and ZIP3 expressing mossy fiber terminals, consistent with previous work

Article Snippet: GluN2A , NeuroMab , 75,288 , 1:300.

Techniques: Co-Immunoprecipitation Assay, Immunoprecipitation, Expressing, Glycoproteomics, Imaging, Control, SDS Page, Western Blot, Proximity Ligation Assay, Protein-Protein interactions

(A, C, E) Real-time RT-PCR was applied to detect NR1, NR2A and NR2B mRNA levels. (B, D, F) Protein levels of NR1, NR2A and NR2B were measured by WB. Images were the representative blots and statistical analysis of protein levels. Data were shown as mean ± SD, n = 6. P < 0.05, * vs. the control, # vs. NaAsO 2 group.

Journal: PLOS One

Article Title: The role of DAAO in cognitive impairment of offspring mice induced by arsenic exposure during early developmental stage

doi: 10.1371/journal.pone.0333414

Figure Lengend Snippet: (A, C, E) Real-time RT-PCR was applied to detect NR1, NR2A and NR2B mRNA levels. (B, D, F) Protein levels of NR1, NR2A and NR2B were measured by WB. Images were the representative blots and statistical analysis of protein levels. Data were shown as mean ± SD, n = 6. P < 0.05, * vs. the control, # vs. NaAsO 2 group.

Article Snippet: Antibodies were DAAO (1:500), NR1 (1:500) (Boster, China), SR (1:500), NR2A (1:500), NR2B (1:500) (Proteintech, China), SYP (1:1000), PSD95 (1:1000) (Abcam, UK), β-actin (1:10000) (Santa Cruz, USA).

Techniques: Quantitative RT-PCR, Control

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