nmda receptor 2b glun2b d15b3 rabbit mab  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc nmda receptor 2b glun2b d15b3 rabbit mab
    Western blot analysis of the N-methyl-D-aspartate <t>receptor</t> <t>(NMDA-R)</t> subunit <t>2B</t> <t>(GluN2B)</t> in the inferior colliculus (IC). (A) The expression of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein among the four groups. (B) The expression of the GluN2B protein was significantly higher in the SS group compared to the control group. In addition, GluN2B protein expression was significantly lower in the EGb+SS group, as compared to the SS group. (C) Relative protein expression of GluN2B in the IC. The expression of GluN2B protein was significantly higher in the SS group and EGb+SS group compared to the control and EGb groups. Notably, the expression of GluN2B protein was significantly decreased in EGb+SS group following EGb pretreatment compared to that in SS group. SS, sodium salicylate; EGb, EGb 761 Ginkgo biloba extract. *P
    Nmda Receptor 2b Glun2b D15b3 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Effect of Ginkgo Biloba Extract on N-Methyl-D-Aspartic Acid Receptor Subunit 2B Expression in a Salicylate-Induced Ototoxicity Model"

    Article Title: Effect of Ginkgo Biloba Extract on N-Methyl-D-Aspartic Acid Receptor Subunit 2B Expression in a Salicylate-Induced Ototoxicity Model

    Journal: Clinical and Experimental Otorhinolaryngology

    doi: 10.21053/ceo.2018.00983

    Western blot analysis of the N-methyl-D-aspartate receptor (NMDA-R) subunit 2B (GluN2B) in the inferior colliculus (IC). (A) The expression of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein among the four groups. (B) The expression of the GluN2B protein was significantly higher in the SS group compared to the control group. In addition, GluN2B protein expression was significantly lower in the EGb+SS group, as compared to the SS group. (C) Relative protein expression of GluN2B in the IC. The expression of GluN2B protein was significantly higher in the SS group and EGb+SS group compared to the control and EGb groups. Notably, the expression of GluN2B protein was significantly decreased in EGb+SS group following EGb pretreatment compared to that in SS group. SS, sodium salicylate; EGb, EGb 761 Ginkgo biloba extract. *P
    Figure Legend Snippet: Western blot analysis of the N-methyl-D-aspartate receptor (NMDA-R) subunit 2B (GluN2B) in the inferior colliculus (IC). (A) The expression of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein among the four groups. (B) The expression of the GluN2B protein was significantly higher in the SS group compared to the control group. In addition, GluN2B protein expression was significantly lower in the EGb+SS group, as compared to the SS group. (C) Relative protein expression of GluN2B in the IC. The expression of GluN2B protein was significantly higher in the SS group and EGb+SS group compared to the control and EGb groups. Notably, the expression of GluN2B protein was significantly decreased in EGb+SS group following EGb pretreatment compared to that in SS group. SS, sodium salicylate; EGb, EGb 761 Ginkgo biloba extract. *P

    Techniques Used: Western Blot, Expressing

    The N-methyl-D-aspartate receptor (NMDA-R) subunit 2B (GluN2B) immunohistochemistry in the inferior colliculus (×200 magnification). (A) The control group showed no GluN2B immunoreactivity. (B) Brain samples from the EGb-treated group also showed negative GluN2B staining. (C) In the SS-treated group, strong immunoreactivity was detected in neuronal cells (arrow) along with some scattered glial cell immunoreactivity (arrowhead). (D) GluN2B staining vanished in the EGb+SS group, with only weak focal immunoreactivity. EGb, EGb 761 Ginkgo biloba extract; SS, sodium salicylate.
    Figure Legend Snippet: The N-methyl-D-aspartate receptor (NMDA-R) subunit 2B (GluN2B) immunohistochemistry in the inferior colliculus (×200 magnification). (A) The control group showed no GluN2B immunoreactivity. (B) Brain samples from the EGb-treated group also showed negative GluN2B staining. (C) In the SS-treated group, strong immunoreactivity was detected in neuronal cells (arrow) along with some scattered glial cell immunoreactivity (arrowhead). (D) GluN2B staining vanished in the EGb+SS group, with only weak focal immunoreactivity. EGb, EGb 761 Ginkgo biloba extract; SS, sodium salicylate.

    Techniques Used: Immunohistochemistry, Staining

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    Cell Signaling Technology Inc monoclonal anti nr1 antibody
    Immunocytochemistry demonstrating nuclear colocalization of <t>NR1-1a</t> and NR3B in melanoma cells. Confocal microscopic analysis demonstrated that NR1-1a (red) shows similar nuclear colocalization in melanoma cells with NR3B (green) as NR1. Nuclei of NHEM showed very weak signals of NR1-1a. NR1-1a was present in the cytoplasmic region of NHEM but unequivocal colocalization with NR3B was not detected at any cellular compartment. As an example, two extra arrows are used in the insert that shows M35/01 cells: the dashed arrow points at an area where the immunofluorescent signal of NR1-1a (red) colocalizes with DAPI (blue), resulting in purple tone whereas the spotted arrow points at an area where NR1-1a colocalizes with DAPI and NR3B (green), resulting in orange colour. Photomicrographs of 1 μm thick optical sections passing through the majority of nuclei in the area of the interest are shown. One representative cell pointed by white arrow with numerous (nuclear) colocalizing signals was selected on each picture and presented in the insert. Scale bar: 20 μm. Positive controls for the secondary <t>antibodies</t> and special controls for the primary antibodies were also performed (See Supplementary Information Figure S8A,B ).
    Monoclonal Anti Nr1 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Immunocytochemistry demonstrating nuclear colocalization of NR1-1a and NR3B in melanoma cells. Confocal microscopic analysis demonstrated that NR1-1a (red) shows similar nuclear colocalization in melanoma cells with NR3B (green) as NR1. Nuclei of NHEM showed very weak signals of NR1-1a. NR1-1a was present in the cytoplasmic region of NHEM but unequivocal colocalization with NR3B was not detected at any cellular compartment. As an example, two extra arrows are used in the insert that shows M35/01 cells: the dashed arrow points at an area where the immunofluorescent signal of NR1-1a (red) colocalizes with DAPI (blue), resulting in purple tone whereas the spotted arrow points at an area where NR1-1a colocalizes with DAPI and NR3B (green), resulting in orange colour. Photomicrographs of 1 μm thick optical sections passing through the majority of nuclei in the area of the interest are shown. One representative cell pointed by white arrow with numerous (nuclear) colocalizing signals was selected on each picture and presented in the insert. Scale bar: 20 μm. Positive controls for the secondary antibodies and special controls for the primary antibodies were also performed (See Supplementary Information Figure S8A,B ).

    Journal: International Journal of Molecular Sciences

    Article Title: NR1 and NR3B Composed Intranuclear N-methyl-d-aspartate Receptor Complexes in Human Melanoma Cells

    doi: 10.3390/ijms19071929

    Figure Lengend Snippet: Immunocytochemistry demonstrating nuclear colocalization of NR1-1a and NR3B in melanoma cells. Confocal microscopic analysis demonstrated that NR1-1a (red) shows similar nuclear colocalization in melanoma cells with NR3B (green) as NR1. Nuclei of NHEM showed very weak signals of NR1-1a. NR1-1a was present in the cytoplasmic region of NHEM but unequivocal colocalization with NR3B was not detected at any cellular compartment. As an example, two extra arrows are used in the insert that shows M35/01 cells: the dashed arrow points at an area where the immunofluorescent signal of NR1-1a (red) colocalizes with DAPI (blue), resulting in purple tone whereas the spotted arrow points at an area where NR1-1a colocalizes with DAPI and NR3B (green), resulting in orange colour. Photomicrographs of 1 μm thick optical sections passing through the majority of nuclei in the area of the interest are shown. One representative cell pointed by white arrow with numerous (nuclear) colocalizing signals was selected on each picture and presented in the insert. Scale bar: 20 μm. Positive controls for the secondary antibodies and special controls for the primary antibodies were also performed (See Supplementary Information Figure S8A,B ).

    Article Snippet: On the following day after washing three times with PBS, biotinylated goat anti-rabbit antibodies were added onto the samples (Vector Laboratories, Burlingame, CA, USA), at a dilution of 1:1000 in PBST, at room temperature for 2 h. After washing, cultures were incubated with monoclonal anti-NR1 antibody (Cell Signaling Technology, Danvers, MA, USA) or polyclonal anti-NR1-1a antibody (Merck-Millipore, Billerica, MA, USA), both produced in rabbit, at a dilution of 1:50 at 4 °C overnight.

    Techniques: Immunocytochemistry

    Immunocytochemistry demonstrating colocalization of NR1 and NR3B in the nuclei of melanoma cells, but not in the cell membrane in melanocytes. Confocal microscopic evaluation revealed that NR1 (red) was present in the cytosol of every melanoma cell line, while NR3B (green) showed weaker and less diffuse signals in the cytoplasm. Unambiguous plasma membrane immunofluorescent signals were not visible, but NR1 and NR3B colocalized inside the nuclei of melanoma cells. NR1 and NR3B colocalization was absent or undetected in the nuclei of NHEM. That 1-μm thick optical section was selected for presentation which specifically went through the majority of nuclei to show that all nuclei were immunopositive. One representative cell pointed by white arrow was selected for the inserts at each part of the panel. Scale bar: 20 μm. Positive controls for the secondary antibodies and special controls for the primary antibodies were also performed (see Supplementary Information Figure S8A,B ).

    Journal: International Journal of Molecular Sciences

    Article Title: NR1 and NR3B Composed Intranuclear N-methyl-d-aspartate Receptor Complexes in Human Melanoma Cells

    doi: 10.3390/ijms19071929

    Figure Lengend Snippet: Immunocytochemistry demonstrating colocalization of NR1 and NR3B in the nuclei of melanoma cells, but not in the cell membrane in melanocytes. Confocal microscopic evaluation revealed that NR1 (red) was present in the cytosol of every melanoma cell line, while NR3B (green) showed weaker and less diffuse signals in the cytoplasm. Unambiguous plasma membrane immunofluorescent signals were not visible, but NR1 and NR3B colocalized inside the nuclei of melanoma cells. NR1 and NR3B colocalization was absent or undetected in the nuclei of NHEM. That 1-μm thick optical section was selected for presentation which specifically went through the majority of nuclei to show that all nuclei were immunopositive. One representative cell pointed by white arrow was selected for the inserts at each part of the panel. Scale bar: 20 μm. Positive controls for the secondary antibodies and special controls for the primary antibodies were also performed (see Supplementary Information Figure S8A,B ).

    Article Snippet: On the following day after washing three times with PBS, biotinylated goat anti-rabbit antibodies were added onto the samples (Vector Laboratories, Burlingame, CA, USA), at a dilution of 1:1000 in PBST, at room temperature for 2 h. After washing, cultures were incubated with monoclonal anti-NR1 antibody (Cell Signaling Technology, Danvers, MA, USA) or polyclonal anti-NR1-1a antibody (Merck-Millipore, Billerica, MA, USA), both produced in rabbit, at a dilution of 1:50 at 4 °C overnight.

    Techniques: Immunocytochemistry

    Western blot analysis gave detailed picture on NMDAR subunit protein expression. NR1-1a and NR2A subunits were expressed in melanocytes, while other subunits were undetectable by western blots ( A ). Fractionated melanoma samples revealed that NR1 and NR3B subunits are expressed in every cellular compartment ( B ). In each melanoma cell line NR2A and NR3A were present in the cytosol and membranes, but in the nucleus ( B ). NR2B was undetectable in each compartment ( B ). Immunoblot signals of NR1-1a were detected in the cytosol and membranes, but more importantly also in the nuclei of melanoma cells ( B ). Controls used in the experiments: MITF (microphthalmia associated transcription factor) for melanocyte differentiation control; GAPDH as an internal control for melanocyte whole cell lysates; actin as internal controls for the comparison of the cellular fractions; TATABP (TATA box binding protein) expression as internal control for nuclear fraction analysis. The positive control for detection of NMDAR subunit protein expression was human brain tissue lysate (see Supplementary Information Figure S3 ). Whole membrane pictures of western blots are presented as Supplementary Figure S4 . Normalization of the relative optical density parameters of the protein subunit expressions to the respective control is shown in a graphical format in the Supplementary Information Figures S5–S7 . (C = cytosolic, M = membrane, N = nuclear fractions of melanoma cells).

    Journal: International Journal of Molecular Sciences

    Article Title: NR1 and NR3B Composed Intranuclear N-methyl-d-aspartate Receptor Complexes in Human Melanoma Cells

    doi: 10.3390/ijms19071929

    Figure Lengend Snippet: Western blot analysis gave detailed picture on NMDAR subunit protein expression. NR1-1a and NR2A subunits were expressed in melanocytes, while other subunits were undetectable by western blots ( A ). Fractionated melanoma samples revealed that NR1 and NR3B subunits are expressed in every cellular compartment ( B ). In each melanoma cell line NR2A and NR3A were present in the cytosol and membranes, but in the nucleus ( B ). NR2B was undetectable in each compartment ( B ). Immunoblot signals of NR1-1a were detected in the cytosol and membranes, but more importantly also in the nuclei of melanoma cells ( B ). Controls used in the experiments: MITF (microphthalmia associated transcription factor) for melanocyte differentiation control; GAPDH as an internal control for melanocyte whole cell lysates; actin as internal controls for the comparison of the cellular fractions; TATABP (TATA box binding protein) expression as internal control for nuclear fraction analysis. The positive control for detection of NMDAR subunit protein expression was human brain tissue lysate (see Supplementary Information Figure S3 ). Whole membrane pictures of western blots are presented as Supplementary Figure S4 . Normalization of the relative optical density parameters of the protein subunit expressions to the respective control is shown in a graphical format in the Supplementary Information Figures S5–S7 . (C = cytosolic, M = membrane, N = nuclear fractions of melanoma cells).

    Article Snippet: On the following day after washing three times with PBS, biotinylated goat anti-rabbit antibodies were added onto the samples (Vector Laboratories, Burlingame, CA, USA), at a dilution of 1:1000 in PBST, at room temperature for 2 h. After washing, cultures were incubated with monoclonal anti-NR1 antibody (Cell Signaling Technology, Danvers, MA, USA) or polyclonal anti-NR1-1a antibody (Merck-Millipore, Billerica, MA, USA), both produced in rabbit, at a dilution of 1:50 at 4 °C overnight.

    Techniques: Western Blot, Expressing, Binding Assay, Positive Control

    RT-PCR (reverse transcription followed by polymerase chain reaction) detection of NMDAR ( N -methyl- d -aspartate receptor) subunit mRNA expression in melanoma cells and melanocytes. RT-PCRs proved the presence of the essential NR1, the widely expressed NR2 and also the rare NR3 subunits in A2058, HT169M1, HT199, M35/01 and WM35 melanoma cell lines, as well as in NHEMs (normal human epidermal melanocytes). GAPDH (Glycerol aldehyde phosphate dehydrogenase) mRNA expression served as internal control to the reaction. The positive control for NMDAR subunit detection was human brain tissue sample (see Supplementary Information Figure S1 ). Normalization of the relative optical density parameters of the subunit mRNA expressions to GAPDH is shown in a graphical format in the Supplementary Information Figure S2 .

    Journal: International Journal of Molecular Sciences

    Article Title: NR1 and NR3B Composed Intranuclear N-methyl-d-aspartate Receptor Complexes in Human Melanoma Cells

    doi: 10.3390/ijms19071929

    Figure Lengend Snippet: RT-PCR (reverse transcription followed by polymerase chain reaction) detection of NMDAR ( N -methyl- d -aspartate receptor) subunit mRNA expression in melanoma cells and melanocytes. RT-PCRs proved the presence of the essential NR1, the widely expressed NR2 and also the rare NR3 subunits in A2058, HT169M1, HT199, M35/01 and WM35 melanoma cell lines, as well as in NHEMs (normal human epidermal melanocytes). GAPDH (Glycerol aldehyde phosphate dehydrogenase) mRNA expression served as internal control to the reaction. The positive control for NMDAR subunit detection was human brain tissue sample (see Supplementary Information Figure S1 ). Normalization of the relative optical density parameters of the subunit mRNA expressions to GAPDH is shown in a graphical format in the Supplementary Information Figure S2 .

    Article Snippet: On the following day after washing three times with PBS, biotinylated goat anti-rabbit antibodies were added onto the samples (Vector Laboratories, Burlingame, CA, USA), at a dilution of 1:1000 in PBST, at room temperature for 2 h. After washing, cultures were incubated with monoclonal anti-NR1 antibody (Cell Signaling Technology, Danvers, MA, USA) or polyclonal anti-NR1-1a antibody (Merck-Millipore, Billerica, MA, USA), both produced in rabbit, at a dilution of 1:50 at 4 °C overnight.

    Techniques: Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Expressing, Positive Control

    Western blots of the NMDAR1 subunit of the NMDA receptor and β-actin from WT and Mecp2-null (null) mice at 1, 2 and 7 weeks of age are shown in A. Mean densities of NMDA1 protein (percent WT; mean ± s.e.m.) show a significant increase

    Journal: Anatomical record (Hoboken, N.J. : 2007)

    Article Title: Temporal and regional alterations in NMDA receptor expression in Mecp2-null mice

    doi: 10.1002/ar.21380

    Figure Lengend Snippet: Western blots of the NMDAR1 subunit of the NMDA receptor and β-actin from WT and Mecp2-null (null) mice at 1, 2 and 7 weeks of age are shown in A. Mean densities of NMDA1 protein (percent WT; mean ± s.e.m.) show a significant increase

    Article Snippet: After determination of protein concentration, 30 μg of protein homogenate was resolved by sodium dodecylsulfate polyacrylamide gel electrophoresis on a 4–20% gradient gel (Invitrogen), followed by transfer onto nitrocellulose membranes, and incubation with primary antibodies to the NMDAR1 subunit of the NMDA receptor (#4204, Cell Signaling, 1:1000) and β-actin (#A5316, Sigma, 1:5000) (as described ( ; ).

    Techniques: Western Blot, Mouse Assay

    The crucial role of NR2B-containing NMDARs in the magnesium-induced restoration. a The protein expression levels of NR2A (Ctl, 11 mice; Mg, 13 mice) and NR2B (Ctl, 12 mice; Mg, 13 mice) in V1b of control and magnesium-treated mice. Using two-tailed Student’s t test, P = 0.0002 for NR2A, P = 0.00002 for NR2B. Error bars, SEM. b Schematic of the experimental procedure (top) and a summary of the CBIs in each group with a local infusion of NR2B antagonist (Ro, Ro 25-6981), NR2A antagonists (PPPA/TCN; PPPA, light green; TCN 201, dark green) or vehicle (bottom). The drugs were locally infused to V1b of magnesium-treated mice using an osmotic minipump one day prior to MD. P

    Journal: Molecular Brain

    Article Title: The distinct role of NR2B subunit in the enhancement of visual plasticity in adulthood

    doi: 10.1186/s13041-015-0141-y

    Figure Lengend Snippet: The crucial role of NR2B-containing NMDARs in the magnesium-induced restoration. a The protein expression levels of NR2A (Ctl, 11 mice; Mg, 13 mice) and NR2B (Ctl, 12 mice; Mg, 13 mice) in V1b of control and magnesium-treated mice. Using two-tailed Student’s t test, P = 0.0002 for NR2A, P = 0.00002 for NR2B. Error bars, SEM. b Schematic of the experimental procedure (top) and a summary of the CBIs in each group with a local infusion of NR2B antagonist (Ro, Ro 25-6981), NR2A antagonists (PPPA/TCN; PPPA, light green; TCN 201, dark green) or vehicle (bottom). The drugs were locally infused to V1b of magnesium-treated mice using an osmotic minipump one day prior to MD. P

    Article Snippet: After blocking in 5 % nonfat dry milk (wt/vol, in 20 mM TBST), the membrane was incubated with rabbit anti-NR2A (1:1000, Abcam, ab77980), rabbit anti-NR2B (1:1000, Cell Signaling Technology, 4212S), rabbit anti-GAD65 (1:2000, Proteintech, 20746-1-AP), mouse anti-GAD67 (1:1000; Abcam, ab26116), and mouse anti-β-actin (1:15,000; Abcam, ab6276) antibodies, followed by the respective HRP-conjugated secondary antibodies (1:2500-1:10,000; Promega).

    Techniques: Expressing, CTL Assay, Mouse Assay, Two Tailed Test

    The distinct mechanism underlying the restoration induced by magnesium or reduced cortical inhibition. a The protein expression levels of GAD65 (Ctl, 17 mice; Mg, 15 mice) and GAD67 (Ctl, 12 mice; Mg, 11 mice) in V1b of control and magnesium-treated mice. Using two-tailed Student’s t test, P = 0.13 for GAD65, P = 0.73 for GAD67. b The density of cells surrounded by WFA-positive nets (green) in layers 2/3/4 and layers 5/6 of V1b in control (6 mice) and magnesium-treated (6 mice) mice. The DNA-binding dye Hoechst 33342 (Hoechst, blue) was used to identify the different layers. Scale bar, 100 μm. Using two-tailed Student’s t test, P = 0.65 for layers 2/3/4, P = 0.92 for layers 5/6. c Schematic of the experimental procedure (top) and a summary of the CBIs in adult MPA-treated mice with (Ro25-6981, Ro) or without (Vehicle, V) NR2B antagonist administration (bottom). The drugs were locally infused using an osmotic minipump one day prior to and concurrent with 4 days of MD. The horizontal bar represents the mean value; each symbol represents one animal. P = 0.26 using two-tailed Student’s t test. Error bar, SEM

    Journal: Molecular Brain

    Article Title: The distinct role of NR2B subunit in the enhancement of visual plasticity in adulthood

    doi: 10.1186/s13041-015-0141-y

    Figure Lengend Snippet: The distinct mechanism underlying the restoration induced by magnesium or reduced cortical inhibition. a The protein expression levels of GAD65 (Ctl, 17 mice; Mg, 15 mice) and GAD67 (Ctl, 12 mice; Mg, 11 mice) in V1b of control and magnesium-treated mice. Using two-tailed Student’s t test, P = 0.13 for GAD65, P = 0.73 for GAD67. b The density of cells surrounded by WFA-positive nets (green) in layers 2/3/4 and layers 5/6 of V1b in control (6 mice) and magnesium-treated (6 mice) mice. The DNA-binding dye Hoechst 33342 (Hoechst, blue) was used to identify the different layers. Scale bar, 100 μm. Using two-tailed Student’s t test, P = 0.65 for layers 2/3/4, P = 0.92 for layers 5/6. c Schematic of the experimental procedure (top) and a summary of the CBIs in adult MPA-treated mice with (Ro25-6981, Ro) or without (Vehicle, V) NR2B antagonist administration (bottom). The drugs were locally infused using an osmotic minipump one day prior to and concurrent with 4 days of MD. The horizontal bar represents the mean value; each symbol represents one animal. P = 0.26 using two-tailed Student’s t test. Error bar, SEM

    Article Snippet: After blocking in 5 % nonfat dry milk (wt/vol, in 20 mM TBST), the membrane was incubated with rabbit anti-NR2A (1:1000, Abcam, ab77980), rabbit anti-NR2B (1:1000, Cell Signaling Technology, 4212S), rabbit anti-GAD65 (1:2000, Proteintech, 20746-1-AP), mouse anti-GAD67 (1:1000; Abcam, ab26116), and mouse anti-β-actin (1:15,000; Abcam, ab6276) antibodies, followed by the respective HRP-conjugated secondary antibodies (1:2500-1:10,000; Promega).

    Techniques: Inhibition, Expressing, CTL Assay, Mouse Assay, Two Tailed Test, Binding Assay

    GluN2A currents are reduced in Prmt8 cKO mice. Traces ( A ) and quantification ( B ) of GluN2A-mediated currents from control and Prmt8 cKO mice ( N = 8 and N = 7, respectively). C , Quantification of decay time for GluN2A-mediated currents from control and Prmt8 cKO mice ( N = 8 and N = 7, respectively). ** p

    Journal: The Journal of Neuroscience

    Article Title: Loss of Protein Arginine Methyltransferase 8 Alters Synapse Composition and Function, Resulting in Behavioral Defects

    doi: 10.1523/JNEUROSCI.0591-17.2017

    Figure Lengend Snippet: GluN2A currents are reduced in Prmt8 cKO mice. Traces ( A ) and quantification ( B ) of GluN2A-mediated currents from control and Prmt8 cKO mice ( N = 8 and N = 7, respectively). C , Quantification of decay time for GluN2A-mediated currents from control and Prmt8 cKO mice ( N = 8 and N = 7, respectively). ** p

    Article Snippet: Antibodies used included the following: mouse-PSD95 (NeuroMAB), mouse-HDAC2 (Abcam), rabbit-HA (Santa Cruz Biotechnology), mouse-Svp38 (Sigma), rabbit-Cacna1C (Novus), mouse-Syn1 (Synaptic Systems), rabbit-Nsf-1 (Thermo Fisher), rabbit-Syn2 (Abcam), rabbit-Syn3 (Synaptic Systems), rabbit-Syt7 (Abcam), mouse-Syt12 (NeuroMAB), rabbit-Cplx1 (Proteintech), mouse-β-actin (Sigma), rabbit-NR2A (Cell Signaling Technology), rabbit-NR2B (Cell Signaling Technology), mouse-NR1 (Millipore), mouse-GluA1 (Millipore), rabbit-GluA2 (Cell Signaling Technology), mouse-CaMKIIA (Millipore Bioscience Research Reagents), mouse-Shank1 (NeuroMAB), mouse-α-tubulin (Sigma), rabbit-Homer (GeneTex), rabbit-eIF4G1 (Cell Signaling Technology), rabbit-eIF4H (Cell Signaling Technology), rabbit-eIF4E (Cell Signaling Technology), and rabbit-FMRP (Cell Signaling Technology).

    Techniques: Mouse Assay