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Cell Signaling Technology Inc anti eaat2 antibody
Anti Eaat2 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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a Increased <t>EAAT2</t> protein level in GFAP-NLG3 KO (n = 6 mice) compared to GFAP-NLG3 WT mice (n = 6 mice, p = 0.0494). b , c Increased EAAT2 fluorescence intensity in total hippocampus (top, n = 10 sections, 3 mice, p = 0.00754) and GFAP+ cells (bottom, p = 0.0000453) in GFAP-NLG3 KO (n = 36 cells, 3 mice) compared to GFAP-NLG3 WT (n = 35 cells, 3 mice) mice. d Reduced EAAT2 protein level in GFAP-NLG3 KO mice virally expressing WT NLG3-HA compared to control EGFP (n = 4 mice, p = 0.0265). e , f Increased surface EAAT2 fluorescence intensity in total hippocampus (n = 10 sections, 3 mice, p = 0.0260) and in GFAP+ cells (n = 40 cells from 3 mice, p = 0.00000871) in GFAP-NLG3 KO compared to GFAP-NLG3 WT mice. g , h AAV virus construct, iGluSnFR expression and normalized data ( h ) showing increased iGluSnFR signals in response to social sniffing episodes in GFAP-NLG3 WT (n = 5 recordings, 5 mice), but not in GFAP-NLG3 KO mice (n = 4 recordings, 4 mice). i Reduced iGluSnFR signals after initial social sniffing in GFAP-NLG3 KO mice compared to GFAP-NLG3 WT (n = 5 mice for each genotype, p = 0.0437). Data represent mean ± SEM; two-tailed t test for ( c , d , f and i ); *p < 0.05, **p < 0.01, ***p < 0.001. Scale bar: 100 μm in left ( b , e ), 10 μm in right ( b and e ); Source data are provided as a Source Data file.
Eaat2 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Figure 6. AptB1 interacting with <t>EAAT2,</t> Nucleolin, and YB-1. (a) Results of AptB1-AP/MS study revealed three candidate AptB1- interacting proteins: EAAT2, YB-1, and Nucleolin. (b) AP-immunoblots verified the interaction between AptB1 and EAAT2, Nucleolin, as well as YB-1 in the PC9 cells and in the mouse brain. (c) The confocal microscopy images showed colocalization (yellow) of AptB1 (red) and Nucleolin (green, upper panel) or YB-1 (green, lower panel) in the PC9 cells. (d) AptB1-treated cells were fractionated into cytosol and nucleus fractions. GAPDH is a cytosolic marker, and Histone H3 is a nucleus marker. The AptB1 sequences were successfully amplified in both cellular fractions. (e) The Coomassie Blue stain and the immunoblots showed the purified GST and GST-YB-1 proteins. (f) The YB-1 exonuclease assay results supported the role of YB-1 as an exonuclease for AptB1. (g) Scheme illustrating the proposed mechanism of AptBCis1 as therapeutics for lung cancer with and without LM.
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Figure 6. AptB1 interacting with <t>EAAT2,</t> Nucleolin, and YB-1. (a) Results of AptB1-AP/MS study revealed three candidate AptB1- interacting proteins: EAAT2, YB-1, and Nucleolin. (b) AP-immunoblots verified the interaction between AptB1 and EAAT2, Nucleolin, as well as YB-1 in the PC9 cells and in the mouse brain. (c) The confocal microscopy images showed colocalization (yellow) of AptB1 (red) and Nucleolin (green, upper panel) or YB-1 (green, lower panel) in the PC9 cells. (d) AptB1-treated cells were fractionated into cytosol and nucleus fractions. GAPDH is a cytosolic marker, and Histone H3 is a nucleus marker. The AptB1 sequences were successfully amplified in both cellular fractions. (e) The Coomassie Blue stain and the immunoblots showed the purified GST and GST-YB-1 proteins. (f) The YB-1 exonuclease assay results supported the role of YB-1 as an exonuclease for AptB1. (g) Scheme illustrating the proposed mechanism of AptBCis1 as therapeutics for lung cancer with and without LM.
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Figure 6. AptB1 interacting with <t>EAAT2,</t> Nucleolin, and YB-1. (a) Results of AptB1-AP/MS study revealed three candidate AptB1- interacting proteins: EAAT2, YB-1, and Nucleolin. (b) AP-immunoblots verified the interaction between AptB1 and EAAT2, Nucleolin, as well as YB-1 in the PC9 cells and in the mouse brain. (c) The confocal microscopy images showed colocalization (yellow) of AptB1 (red) and Nucleolin (green, upper panel) or YB-1 (green, lower panel) in the PC9 cells. (d) AptB1-treated cells were fractionated into cytosol and nucleus fractions. GAPDH is a cytosolic marker, and Histone H3 is a nucleus marker. The AptB1 sequences were successfully amplified in both cellular fractions. (e) The Coomassie Blue stain and the immunoblots showed the purified GST and GST-YB-1 proteins. (f) The YB-1 exonuclease assay results supported the role of YB-1 as an exonuclease for AptB1. (g) Scheme illustrating the proposed mechanism of AptBCis1 as therapeutics for lung cancer with and without LM.
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Figure 6. AptB1 interacting with <t>EAAT2,</t> Nucleolin, and YB-1. (a) Results of AptB1-AP/MS study revealed three candidate AptB1- interacting proteins: EAAT2, YB-1, and Nucleolin. (b) AP-immunoblots verified the interaction between AptB1 and EAAT2, Nucleolin, as well as YB-1 in the PC9 cells and in the mouse brain. (c) The confocal microscopy images showed colocalization (yellow) of AptB1 (red) and Nucleolin (green, upper panel) or YB-1 (green, lower panel) in the PC9 cells. (d) AptB1-treated cells were fractionated into cytosol and nucleus fractions. GAPDH is a cytosolic marker, and Histone H3 is a nucleus marker. The AptB1 sequences were successfully amplified in both cellular fractions. (e) The Coomassie Blue stain and the immunoblots showed the purified GST and GST-YB-1 proteins. (f) The YB-1 exonuclease assay results supported the role of YB-1 as an exonuclease for AptB1. (g) Scheme illustrating the proposed mechanism of AptBCis1 as therapeutics for lung cancer with and without LM.
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Image Search Results


a Increased EAAT2 protein level in GFAP-NLG3 KO (n = 6 mice) compared to GFAP-NLG3 WT mice (n = 6 mice, p = 0.0494). b , c Increased EAAT2 fluorescence intensity in total hippocampus (top, n = 10 sections, 3 mice, p = 0.00754) and GFAP+ cells (bottom, p = 0.0000453) in GFAP-NLG3 KO (n = 36 cells, 3 mice) compared to GFAP-NLG3 WT (n = 35 cells, 3 mice) mice. d Reduced EAAT2 protein level in GFAP-NLG3 KO mice virally expressing WT NLG3-HA compared to control EGFP (n = 4 mice, p = 0.0265). e , f Increased surface EAAT2 fluorescence intensity in total hippocampus (n = 10 sections, 3 mice, p = 0.0260) and in GFAP+ cells (n = 40 cells from 3 mice, p = 0.00000871) in GFAP-NLG3 KO compared to GFAP-NLG3 WT mice. g , h AAV virus construct, iGluSnFR expression and normalized data ( h ) showing increased iGluSnFR signals in response to social sniffing episodes in GFAP-NLG3 WT (n = 5 recordings, 5 mice), but not in GFAP-NLG3 KO mice (n = 4 recordings, 4 mice). i Reduced iGluSnFR signals after initial social sniffing in GFAP-NLG3 KO mice compared to GFAP-NLG3 WT (n = 5 mice for each genotype, p = 0.0437). Data represent mean ± SEM; two-tailed t test for ( c , d , f and i ); *p < 0.05, **p < 0.01, ***p < 0.001. Scale bar: 100 μm in left ( b , e ), 10 μm in right ( b and e ); Source data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Astrocytic neuroligin 3 regulates social memory and synaptic plasticity through adenosine signaling in male mice

doi: 10.1038/s41467-024-52974-3

Figure Lengend Snippet: a Increased EAAT2 protein level in GFAP-NLG3 KO (n = 6 mice) compared to GFAP-NLG3 WT mice (n = 6 mice, p = 0.0494). b , c Increased EAAT2 fluorescence intensity in total hippocampus (top, n = 10 sections, 3 mice, p = 0.00754) and GFAP+ cells (bottom, p = 0.0000453) in GFAP-NLG3 KO (n = 36 cells, 3 mice) compared to GFAP-NLG3 WT (n = 35 cells, 3 mice) mice. d Reduced EAAT2 protein level in GFAP-NLG3 KO mice virally expressing WT NLG3-HA compared to control EGFP (n = 4 mice, p = 0.0265). e , f Increased surface EAAT2 fluorescence intensity in total hippocampus (n = 10 sections, 3 mice, p = 0.0260) and in GFAP+ cells (n = 40 cells from 3 mice, p = 0.00000871) in GFAP-NLG3 KO compared to GFAP-NLG3 WT mice. g , h AAV virus construct, iGluSnFR expression and normalized data ( h ) showing increased iGluSnFR signals in response to social sniffing episodes in GFAP-NLG3 WT (n = 5 recordings, 5 mice), but not in GFAP-NLG3 KO mice (n = 4 recordings, 4 mice). i Reduced iGluSnFR signals after initial social sniffing in GFAP-NLG3 KO mice compared to GFAP-NLG3 WT (n = 5 mice for each genotype, p = 0.0437). Data represent mean ± SEM; two-tailed t test for ( c , d , f and i ); *p < 0.05, **p < 0.01, ***p < 0.001. Scale bar: 100 μm in left ( b , e ), 10 μm in right ( b and e ); Source data are provided as a Source Data file.

Article Snippet: For surface EAAT2 staining, brain slices were blocked in 10% FBS and incubated with EAAT2 antibody (1:200; Cat# 20848, CST) overnight at 4 °C followed by secondary antibodies, without a prior PBT treatment.

Techniques: Fluorescence, Expressing, Control, Virus, Construct, Two Tailed Test

Figure 6. AptB1 interacting with EAAT2, Nucleolin, and YB-1. (a) Results of AptB1-AP/MS study revealed three candidate AptB1- interacting proteins: EAAT2, YB-1, and Nucleolin. (b) AP-immunoblots verified the interaction between AptB1 and EAAT2, Nucleolin, as well as YB-1 in the PC9 cells and in the mouse brain. (c) The confocal microscopy images showed colocalization (yellow) of AptB1 (red) and Nucleolin (green, upper panel) or YB-1 (green, lower panel) in the PC9 cells. (d) AptB1-treated cells were fractionated into cytosol and nucleus fractions. GAPDH is a cytosolic marker, and Histone H3 is a nucleus marker. The AptB1 sequences were successfully amplified in both cellular fractions. (e) The Coomassie Blue stain and the immunoblots showed the purified GST and GST-YB-1 proteins. (f) The YB-1 exonuclease assay results supported the role of YB-1 as an exonuclease for AptB1. (g) Scheme illustrating the proposed mechanism of AptBCis1 as therapeutics for lung cancer with and without LM.

Journal: ACS nano

Article Title: AptBCis1, An Aptamer-Cisplatin Conjugate, Is Effective in Lung Cancer Leptomeningeal Carcinomatosis.

doi: 10.1021/acsnano.4c04680

Figure Lengend Snippet: Figure 6. AptB1 interacting with EAAT2, Nucleolin, and YB-1. (a) Results of AptB1-AP/MS study revealed three candidate AptB1- interacting proteins: EAAT2, YB-1, and Nucleolin. (b) AP-immunoblots verified the interaction between AptB1 and EAAT2, Nucleolin, as well as YB-1 in the PC9 cells and in the mouse brain. (c) The confocal microscopy images showed colocalization (yellow) of AptB1 (red) and Nucleolin (green, upper panel) or YB-1 (green, lower panel) in the PC9 cells. (d) AptB1-treated cells were fractionated into cytosol and nucleus fractions. GAPDH is a cytosolic marker, and Histone H3 is a nucleus marker. The AptB1 sequences were successfully amplified in both cellular fractions. (e) The Coomassie Blue stain and the immunoblots showed the purified GST and GST-YB-1 proteins. (f) The YB-1 exonuclease assay results supported the role of YB-1 as an exonuclease for AptB1. (g) Scheme illustrating the proposed mechanism of AptBCis1 as therapeutics for lung cancer with and without LM.

Article Snippet: Anti-luciferase antibody (sc-74548), EAAT2 siRNA (sc-35256), Nucleolin siRNA (sc-29230), YB-1 siRNA (sc38634), and GAPDH antibody (sc-32233) were purchased from Santa Cruz. γH2AX (9718), YB-1 (4202), and EAAT2 (20848) antibodies were purchased from Cell Signaling.

Techniques: Protein-Protein interactions, Western Blot, Confocal Microscopy, Marker, Amplification, Staining, Purification

Journal: iScience

Article Title: Influenza A virus selectively elevates prostaglandin E 2 formation in pro-resolving macrophages

doi: 10.1016/j.isci.2023.108775

Figure Lengend Snippet:

Article Snippet: rabbit polyclonal anti-COX-1 , Cell Signaling , Cat#4841; RRID: AB_2084807.

Techniques: Virus, Recombinant, SYBR Green Assay, Reverse Transcription, Software