Glun1

Manufactured by Thermo Fisher Scientific

Sourced in United States

The GluN1 is a laboratory equipment product that serves as a core component in various biological and chemical research applications. It functions as a fundamental building block for specialized experiments and analyses. The details of its intended use and specific applications are not included in this factual and unbiased description.

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Lab products found in correlation

Synaptophysin, by Santa Cruz Biotechnology (2 mentions) Slitrk1, by Abcam (2 mentions) Slitrk3, by Abcam (2 mentions) α tubulin, by Merck Group (2 mentions) Synapsin 1, by Merck Group (2 mentions) Glua1, by Santa Cruz Biotechnology (2 mentions) Glua2, by Santa Cruz Biotechnology (2 mentions) Il 1racp, by Merck Group (2 mentions) Glun2a, by Zymo Research (2 mentions) Glua1, by Abcam (2 mentions) Neuro 2a cells, by American Type Culture Collection (2 mentions) Dock4, by Abcam (2 mentions) Glua2, by Merck Group (2 mentions) Glun2a, by Merck Group (2 mentions) Glun2b, by Merck Group (2 mentions) Dock4, by Thermo Fisher Scientific (2 mentions) Anti rb igg hrp, by Cell Signaling Technology (2 mentions) Nsc23766, by Selleck Chemicals (2 mentions) Psd95, by Abcam (2 mentions) Flag tag (flag), by Merck Group (2 mentions)

6 protocols using glun1

Generation and Characterization of Antibodies

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SALM3 (1929) guinea pig polyclonal antibodies were generated using a synthetic peptide as immunogen (aa 594–608 of mouse SALM3; CYGYARRLGGAWARR). Peptides mimicking the last 30 aa of mouse SALM1, SALM2, and SALM4 were used to generate guinea pig polyclonal antibodies (2022, 2058, and 2026, respectively). The following antibodies have been described: PSD-95 (1690) (Han et al., 2010 (link)), NGL-3 (2020) (Lee et al., 2014 (link)), SALM3 (1816), and SALM5 (1907) (Mah et al., 2010 (link)). The following antibodies were purchased: α-tubulin, synapsin I (Sigma), synaptophysin, GluA1, GluA2 (Santa Cruz), slitrk1, slitrk3 (Abcam), GluN1 (Invitrogen), GluN2A (Zymed), GluN2B (NeuroMab), PTPσ (17G7.2, mouse, Medimabs), and IL-1RAcP (Millipore). IL1RAPL1 antibody was a kind gift from Dr. Carlo Sala.

Li Y., Zhang P., Choi T.Y., Park S.K., Park H., Lee E.J., Lee D., Roh J.D., Mah W., Kim R., Kim Y., Kwon H., Bae Y.C., Choi S.Y., Craig A.M, & Kim E. (2015). Splicing-Dependent Trans-synaptic SALM3–LAR-RPTP Interactions Regulate Excitatory Synapse Development and Locomotion. Cell reports, 12(10), 1618-1630.

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Western Blot Analysis of Synaptic Proteins

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The primary antibodies used in Western blot analysis were purchased from the following commercial suppliers: Dock4 (ab85723, 1:1000) and PSD95 (ab2723, 1:1000) were from Abcam; GluA1 (PC246, 1:1000), GluA2 (MAB397, 1:1000), GluN2A (AB1555P, 1:1000), GluN2B (AB1557P and 06-000, 1:1000), Rac1 (05-389, 1:2000), and puromycin (MABE343, 1:10000) were from Merck Millipore; GluN1 (32-0500, 1:1000) was from Invitrogen; Dock4 (WH0009732M1, 1:1000), ɑ-tubulin (T6199, 1:5000), and Flag (F1804, 1:1000) were from Sigma; GAPDH (A01020, 1:5000) was from Abbkine. The secondary antibodies for Western blot were purchased from Cell Signaling Technology (anti-mouse IgG-HRP, 7076s; anti-Rb IgG-HRP, 7074s). Pharmacological inhibitors MG132 and NSC23766 were purchased from Selleck. puromycin was purchased from Merck Millipore. cDNAs of Dock4 and Rac1 and their mutants, and Dock4 shRNA were described previously [27 (link), 32 (link)]. Neuro-2a cells were purchased from ATCC and were routinely tested for mycoplasma contamination-free before use.

Guo D., Peng Y., Wang L., Sun X., Wang X., Liang C., Yang X., Li S., Xu J., Ye W.C., Jiang B, & Shi L. (2019). Autism-like social deficit generated by Dock4 deficiency is rescued by restoration of Rac1 activity and NMDA receptor function. Molecular Psychiatry, 26(5), 1505-1519.

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Comprehensive Antibody Validation for Western Blot

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The primary antibodies used in Western blot analysis were purchased from the following commercial suppliers: Dock4 (ab85723, 1:1000) and PSD95 (ab2723, 1:1000) were from Abcam; GluA1 (PC246, 1:1000), GluA2 (MAB397, 1:1000), GluN2A (AB1555P, 1:1000), GluN2B (AB1557P and 06-000, 1:1000), Rac1 (05-389, 1:2000), and puromycin (MABE343, 1:10000) were from Merck Millipore; GluN1 (32-0500, 1:1000) was from Invitrogen; Dock4 (WH0009732M1, 1:1000), ɑ-tubulin (T6199, 1:5000), and Flag (F1804, 1:1000) were from Sigma; GAPDH (A01020, 1:5000) was from Abbkine. The secondary antibodies for Western blot were purchased from Cell Signaling Technology (anti-mouse IgG-HRP, 7076s; anti-Rb IgG-HRP, 7074s). Pharmacological inhibitors MG132 and NSC23766 were purchased from Selleck. puromycin was purchased from Merck Millipore. cDNAs of Dock4 and Rac1 and their mutants, and Dock4 shRNA were described previously ^{27 (link), 32}. Neuro-2a cells were purchased from ATCC and were routinely tested for mycoplasma contamination-free before use.

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Western Blot Analysis of Synaptic Proteins

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After determination of the protein concentration, protein samples were separated by SDS-PAGE and subsequently transferred to PVDF membranes (Bio-Rad, Hercules, CA, USA). Membranes were blocked by 5% non-fat milk in TBST, then incubated at 4 °C overnight with the following primary antibodies: EphB2 (1:1000; R&D Systems, Minneapolis, MN, USA), GluN1 (1:1000; Invitrogen), GluN2A (1:800; Santa Cruz, Dallas, TX, USA), GluN2B (1:1000; Santa Cruz), P-GluN2B (Y1472) (1:1000; Millipore, Bedford, MA, USA), P-EphB2 (Y594) (1:1000; Abcam, Cambridge, MA, USA), β-actin (1:2000; Santa Cruz), GAPDH (1:1000) and His-tag (1:1000; Zhongshan Goldenbridge Biotechnology, Beijing, China). After rinses with TBST, membranes were incubated with horseradish peroxidase-conjugated secondary antibodies (1:1000; Beyotime Institute of Biotechnology, Haimen, China). Protein bands were visualized with an ECL detection system (Beyotime Institute of Biotechnology) and quantified densitometrically with ImageJ software (NIH).

Hu R., Wei P., Jin L., Zheng T., Chen W.Y., Liu X.Y., Shi X.D., Hao J.R., Sun N, & Gao C. (2017). Overexpression of EphB2 in hippocampus rescues impaired NMDA receptors trafficking and cognitive dysfunction in Alzheimer model. Cell Death & Disease, 8(3), e2717-.

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Generation and Characterization of Antibodies

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Quantifying Synaptic Protein Levels

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Total RNA was extracted, and samples were processed for real-time polymerase chain reaction (PCR) by a TaqMan qRT-PCR instrument (CFX384 real-time system, Bio-Rad Laboratories S.r.l.), as previously described (Calabrese et al. 2013) (link) CGTCTGTTCACTCGAGATTCTG.
Protein extraction and western blot analysis.
The protein levels of GluN1, PSD95 CDC42 and SEPT7 were investigated in the crude synaptosomal fraction, extracted from the rats prefrontal cortex as previously reported (Calabrese et al. 2013) (link). 10 µg of proteins was run on 10% SDS-polyacrylamide gels and transferred onto nitrocellulose membranes. Blots were blocked and incubated at room temperature with the primary antibodies (Genetex; GluN1: 1:1000, Invitrogen; PSD95: 1:4000, Cell Signaling; CDC42: 1:1000, Cell Signaling; SEPT7: 1:500) and then for 1 h at room temperature with the corresponding secondary antibody (GluN1: 1:3000, anti-mouse; PSD95:
1:8000, anti-rabbit; CDC42: 1:1000, anti-rabbit; SEPT7: 1:2000, anti-rabbit). Immunocomplexes were visualized using the Western Lightning Plus ECL (PerkinElmer) and Chemidoc MP imaging system (Bio-Rad Laboratories).

Brivio P., Homberg J.R., Riva M.A, & Calabrese F. (2019). Alterations of Glutamatergic Markers in the Prefrontal Cortex of Serotonin Transporter Knockout Rats: A Developmental Timeline. Cellular and molecular neurobiology, 39(5).

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