Anti mglur5

Manufactured by Abcam

Sourced in United Kingdom

Anti-mGluR5 is a laboratory antibody product. It recognizes the metabotropic glutamate receptor 5 (mGluR5), which is a G protein-coupled receptor involved in various cellular processes. This antibody can be used for the detection and analysis of mGluR5 in experimental settings.

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Lab products found in correlation

Anti β actin, by Cell Signaling Technology (2 mentions) Anti nr2b, by Cell Signaling Technology (2 mentions) Anti homer1, by Abcam (2 mentions) Anti erk1 2, by Cell Signaling Technology (1 mentions) Anti nr2a, by Cell Signaling Technology (1 mentions) Anti psd95, by Abcam (1 mentions) Quantity one software, by Bio-Rad (1 mentions) Pvdf membrane, by GE Healthcare (1 mentions) Anti tyrosine hydroxylase, by Merck Group (1 mentions) Anti glun2a, by Merck Group (1 mentions) Anti gapdh, by Santa Cruz Biotechnology (1 mentions) Anti glun1, by Cell Signaling Technology (1 mentions) Anti glun2b, by Cell Signaling Technology (1 mentions) Anti α tubulin, by Merck Group (1 mentions) Anti β actin, by Merck Group (1 mentions) Semi dry transfer system, by Bio-Rad (1 mentions) Syn per reagent, by Thermo Fisher Scientific (1 mentions) Horseradish peroxidase, by Jackson ImmunoResearch (1 mentions)

Spelling variants of this product

MGluR5 (6 citations) Rabbit anti-mGluR5 (2 citations)

4 protocols using anti mglur5

Quantitative Analysis of Synaptic Proteins in mGluR5 Knockout Mice

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The experimental process is as described in the previous study (19 (link)). PFC and hippocampal tissues of mGluR5^−/− mice and wild-type littermates (group three) were collected and lysed in 100–300 μl of Radio Immunopreciptation Assay (RIPA) lysis buffer (10 mM Tris, 1 mM EDTA, 0.5% NP-40, 150 mM NaCl, and 1% Triton X-100 at pH 7.4). The RIPA lysis buffer contained a 1:100 (v/v) ratio of a protease inhibitor cocktail and a phosphatase inhibitor cocktail (Roche). The BCA protein assay (Pierce) was used to quantify the total protein samples (20–40 μg), and then the samples were resolved via sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to PVDF membranes. The primary antibodies were as follows: anti-β-actin (1:1,000, Cell Signaling Technology); anti-mGluR5 (1:1,000, Abcam); anti-NR2A (1:1,000, Cell Signaling Technology); anti-NR2B (1:1,000, Cell Signaling Technology); anti-PSD95 (1:1,000, Abcam); anti-homer1 (1:1,000, Abcam); and anti-Erk1/2 (1:1,000, Cell Signaling Technology). The enhanced chemiluminescence (ECL) detection method (Advansta) was used to visualize all Western blots. Image J software (version 1.47) was used to quantify the scanned images.

Cai G., Zhu Y., Chen J., Zhao S., Wang L., Wang M., Huang J, & Wu S. (2020). Analysis of the Gut Microbiota and Inflammatory Factors in mGluR5-Knockout Mice. Frontiers in Psychiatry, 11, 335.

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Shank3 Deficiency Proteome Analysis

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Brains were removed from Shank3B^−/− mice and WT mice and sectioned into 1-mm-thick coronal sections at the end of the study. The tissues of each brain area were extracted from the sections according to the mouse atlas (The Mouse Brain in Stereotaxic Coordinates, second edition, by George Paxinos and Keith B.J. Franklin). The collected tissues were lysed in 100–300 μL of RIPA lysis buffer (10 mM Tris, 150 mM NaCl, 1% Triton X-100, 0.5% NP-40, and 1 mM EDTA at pH 7.4) containing a 1:100 (v/v) ratio of a protease inhibitor cocktail and a phosphatase inhibitor cocktail (Roche). We used the bicinchoninic acid protein assay (Pierce) to quantify total protein samples (20–40 μg). Then, the samples were resolved via sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to polyvinylidene fluoride membranes. The primary antibodies were as follows: anti-β-actin (1:1,000, Cell Signaling Technology); anti-Shank3 (1:1,000, Abcam); anti-mGluR5 (1:1,000, Abcam); anti-NR2b (1:1,000, Cell Signaling Technology); and anti-homer1 (1:1,000, Abcam). All western blots were visualized using the enhanced chemiluminescence detection method (Advansta). The scanned images were quantified using ImageJ software (version 1.47).

Cai G., Wang M., Wang S., Liu Y., Zhao Y., Zhu Y., Zhao S., Zhang M., Guo B., Yao H., Wang W., Wang J, & Wu S. (2019). Brain mGluR5 in Shank3B−/− Mice Studied With in vivo [18F]FPEB PET Imaging and ex vivo Immunoblotting. Frontiers in Psychiatry, 10, 38.

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Proteomic Analysis of Postmortem Brain

Cited 1 time

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Preparation and immunoblotting were performed as previously described^{78 (link)}. Frozen, powdered samples from post-mortem brains were sonicated in 1% SDS and boiled for 10 min. Proteins were separated by SDS-PAGE and electroblotted onto PVDF membranes (GE-Healthcare). Immunodetections were accomplished by using the following antibodies: anti-SR (1:500, Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti-DAAO (1:1000, Everest Biotech Ltd, Oxfordshire, UK), anti-GluN1 (1:1000, Cell Signaling Technology, Beverly, MA, USA), anti-GluN2A (1:1000, Sigma, St. Louis, MO, USA), anti-GluN2B (1:1000, Cell Signaling Technology), anti-GluR1, anti-GluR2/3 (1:1000, Merck Millipore, Darmstadt, Germany), anti-mGluR2/3 (1:1000, Merck Millipore), anti-mGluR5 (1:1000, Abcam, Cambridge, UK), anti-α-tubulin (1:50000, Sigma), anti-tyrosine hydroxylase (1:2000, Merck Millipore), anti-GAPDH (1:1000, Santa Cruz Biotechnology). Blots were then incubated in horseradish peroxidase-conjugated secondary antibodies. Immunoreactivity was detected by enhanced chemiluminescence (ECL) (GE-Healthcare) and quantified by Quantity One software (Bio-Rad). Optical density values were normalized to α-tubulin or GAPDH for variations in loading and transfer. Statistical analyses were performed by one-way ANOVA, followed by Fisher’s post-hoc comparison, when required.

Nuzzo T., Punzo D., Devoto P., Rosini E., Paciotti S., Sacchi S., Li Q., Thiolat M.L., Véga C., Carella M., Carta M., Gardoni F., Calabresi P., Pollegioni L., Bezard E., Parnetti L., Errico F, & Usiello A. (2019). The levels of the NMDA receptor co-agonist D-serine are reduced in the substantia nigra of MPTP-lesioned macaques and in the cerebrospinal fluid of Parkinson’s disease patients. Scientific Reports, 9, 8898.

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TMEV-Induced Synaptic Protein Analysis

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Brains were obtained from TMEV-infected and mock-infected (PBS-injected) mice for 1–2 DPI, and for 3–14 DPI time points brains were obtained from mock-infected and TMEV-infected mice displaying seizures. Hippocampi were dissected, weighed, and then homogenize on ice in Syn-PER reagent (ThermoFisher Scientific, Waltham, MA). In order to obtain a synaptosomal fraction, the homogenized samples were centrifuged at 1200 × g for 10 minutes. The supernatants were collected and centrifuged at 15,000 × g for 20 minutes. The supernatants were discarded and the final pellets were resuspended in 100 μL Syn-PER reagent. Gel electrophoresis of the synaptosomal samples was performed using Criterion TGX 4–15% precast polyacrylamide gels (BioRad, Hercules, CA), and transfer of proteins to nitrocellulose was carried out using a semi-dry transfer system (BioRad). Nitrocellulose membranes were then stained using anti-mGluR5 (ABCAM, Cambridge, MA) and anti-β actin (SigmaAldrich, St. Louis, MO), and secondary antibodies conjugated with horseradish peroxidase (Jackson ImmunoResearch Laboratories Inc., West Grove, PA) were used to identify protein bands with chemiluminescence reagents. Analyses of western blots were performed using ImageJ software, normalizing all samples to β-actin as a loading control. Samples were eliminated if there were clear and visible artifacts, loading, or transfer errors.

Hanak T.J., Libbey J.E., Doty D.J., Sim J.T., DePaula-Silva A.B, & Fujinami R.S. (2018). Positive Modulation of mGluR5 Attenuates Seizures and Reduces TNF-α+ Macrophages and Microglia in the Brain in a Murine Model of Virus-Induced Temporal Lobe Epilepsy. Experimental neurology, 311, 194-204.

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