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primary antibody directed towards 20 c-terminal residues glur2  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology primary antibody directed towards 20 c-terminal residues glur2
    Primary Antibody Directed Towards 20 C Terminal Residues Glur2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primary antibody directed towards 20 c-terminal residues glur2/product/Santa Cruz Biotechnology
    Average 90 stars, based on 1 article reviews
    primary antibody directed towards 20 c-terminal residues glur2 - by Bioz Stars, 2026-03
    90/100 stars

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    Key reagents and resources used in the present study.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Neural mechanism underlies CYLD modulation of morphology and synaptic function of medium spiny neurons in dorsolateral striatum

    doi: 10.3389/fnmol.2023.1107355

    Figure Lengend Snippet: Key reagents and resources used in the present study.

    Article Snippet: C-Myc-GRIA2 , Sino Biological , MG57202-CM.

    Techniques: Recombinant, Protein Extraction, Software

    CYLD stabilizes AMPARs. (A) Representative immunoblots of total protein isolated from the DLS of Cyld +/+ and Cyld −/− littermates. (B) Quantification of immunoblots in (A) reveals that total protein expression levels remain unchanged between genotypes (GluA1, GluA2 and mGluR5: n = 4 per group; CaMKIIα, CaMKIIβ, pCaMKIIα and pCaMKIIβ: n = 6 per group). (C) Representative immunoblots of surface protein isolated from the DLS of Cyld +/+ and Cyld −/− littermates. (D) Quantification of immunoblots in (C) reveals a significant decrease in surface GluA1 and GluA2 protein levels in Cyld −/− mice (GluA1: n = 5 per group; GluA2: n = 8 per group; NMDAR1 and mGluR5: n = 3 per group; NMDAR2B: n = 11 per group). β-actin and Na, K-ATPase were used as loading controls. Data are presented as the mean ± SEM; *** p < 0.001.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Neural mechanism underlies CYLD modulation of morphology and synaptic function of medium spiny neurons in dorsolateral striatum

    doi: 10.3389/fnmol.2023.1107355

    Figure Lengend Snippet: CYLD stabilizes AMPARs. (A) Representative immunoblots of total protein isolated from the DLS of Cyld +/+ and Cyld −/− littermates. (B) Quantification of immunoblots in (A) reveals that total protein expression levels remain unchanged between genotypes (GluA1, GluA2 and mGluR5: n = 4 per group; CaMKIIα, CaMKIIβ, pCaMKIIα and pCaMKIIβ: n = 6 per group). (C) Representative immunoblots of surface protein isolated from the DLS of Cyld +/+ and Cyld −/− littermates. (D) Quantification of immunoblots in (C) reveals a significant decrease in surface GluA1 and GluA2 protein levels in Cyld −/− mice (GluA1: n = 5 per group; GluA2: n = 8 per group; NMDAR1 and mGluR5: n = 3 per group; NMDAR2B: n = 11 per group). β-actin and Na, K-ATPase were used as loading controls. Data are presented as the mean ± SEM; *** p < 0.001.

    Article Snippet: C-Myc-GRIA2 , Sino Biological , MG57202-CM.

    Techniques: Western Blot, Isolation, Expressing

    CYLD regulates GluA1 and GluA2 K63-ubiquitination. (A) HEK293 cells were cotransfected with CYLD and Myc-GluA1 or Myc-GluA2 expression vectors. The cell lysates were immunoprecipitated using anti-Myc and anti-CYLD antibodies and immunoblotted with anti-CYLD and anti-GluA2 antibodies. (B) Interaction between endogenous CYLD and GluA1 and GluA2 in the mouse brain, analyzed by immunoprecipitation. Rabbit IgG was used as a negative control in immunoprecipitation experiments. (C) HEK293 cells were cotransfected with expression vectors for various combinations of Myc-GluA1 (left) or Myc-GluA2 (right), HA-K63Ub and CYLD, followed by immunoprecipitation with anti-Myc and immunoblotting with anti-K63Ub. (D) Quantification of immunoblots in (C) shows a reduction in K63Ub conjugated to GluA1 (left) and GluA2 (right) by CYLD in HEK293 cells. (E) DLS lysates from Cyld +/+ and Cyld −/− littermates were immunoprecipitated with anti-GluA1 (left) or anti-GluA2 (right) antibodies and immunoblotted with anti-K63Ub. Rabbit IgG was used as a negative control in immunoprecipitation experiments. (F) Quantification of immunoblots in (E) reveals increased GluA1 and GluA2 K63 ubiquitination in Cyld −/− mice ( n = 4 Cyld +/+ mice, n = 4 Cyld −/− mice). (G) In vitro deubiquitination assays showing that CYLD removes GluA1 (left) and GluA2 (right) K63Ub chains. Data are presented as the mean ± SEM; * p <0.05.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Neural mechanism underlies CYLD modulation of morphology and synaptic function of medium spiny neurons in dorsolateral striatum

    doi: 10.3389/fnmol.2023.1107355

    Figure Lengend Snippet: CYLD regulates GluA1 and GluA2 K63-ubiquitination. (A) HEK293 cells were cotransfected with CYLD and Myc-GluA1 or Myc-GluA2 expression vectors. The cell lysates were immunoprecipitated using anti-Myc and anti-CYLD antibodies and immunoblotted with anti-CYLD and anti-GluA2 antibodies. (B) Interaction between endogenous CYLD and GluA1 and GluA2 in the mouse brain, analyzed by immunoprecipitation. Rabbit IgG was used as a negative control in immunoprecipitation experiments. (C) HEK293 cells were cotransfected with expression vectors for various combinations of Myc-GluA1 (left) or Myc-GluA2 (right), HA-K63Ub and CYLD, followed by immunoprecipitation with anti-Myc and immunoblotting with anti-K63Ub. (D) Quantification of immunoblots in (C) shows a reduction in K63Ub conjugated to GluA1 (left) and GluA2 (right) by CYLD in HEK293 cells. (E) DLS lysates from Cyld +/+ and Cyld −/− littermates were immunoprecipitated with anti-GluA1 (left) or anti-GluA2 (right) antibodies and immunoblotted with anti-K63Ub. Rabbit IgG was used as a negative control in immunoprecipitation experiments. (F) Quantification of immunoblots in (E) reveals increased GluA1 and GluA2 K63 ubiquitination in Cyld −/− mice ( n = 4 Cyld +/+ mice, n = 4 Cyld −/− mice). (G) In vitro deubiquitination assays showing that CYLD removes GluA1 (left) and GluA2 (right) K63Ub chains. Data are presented as the mean ± SEM; * p <0.05.

    Article Snippet: C-Myc-GRIA2 , Sino Biological , MG57202-CM.

    Techniques: Expressing, Immunoprecipitation, Negative Control, Western Blot, In Vitro

    Key reagents and resources used in the present study.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Neural mechanism underlies CYLD modulation of morphology and synaptic function of medium spiny neurons in dorsolateral striatum

    doi: 10.3389/fnmol.2023.1107355

    Figure Lengend Snippet: Key reagents and resources used in the present study.

    Article Snippet: C-Myc-GRIA2 , Sino Biological , MG57202-CM.

    Techniques: Recombinant, Protein Extraction, Software

    List of primary antibodies used for immunohistochemistry and in Western blotting.

    Journal: Frontiers in Neuroscience

    Article Title: Evidence of Synaptic and Neurochemical Remodeling in the Retina of Aging Degus

    doi: 10.3389/fnins.2020.00161

    Figure Lengend Snippet: List of primary antibodies used for immunohistochemistry and in Western blotting.

    Article Snippet: GluA2 , Ms , IgG1 , Fusion protein amino acids 834–883 cytoplasmic C-terminus of rat GluA2/GluR2 , Immunoblot of membranes from adult rat brain and adult GluA2/GluR2 knockout and wild-type mouse hippocampi , 1:1000 , Clone L21/32; UC Davis/NIH NeuroMab , .

    Techniques: Immunohistochemistry, Western Blot, Recombinant, Membrane, Knock-Out