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neural agrin  (R&D Systems)


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    R&D Systems neural agrin
    Neural Agrin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/neural+agrin/Recombinant+Rat+Agrin+Protein/bio_rxiv__64898__2026__03__17__709302-71-6-9
    Average 95 stars, based on 83 article reviews
    neural agrin - by Bioz Stars, 2026-10
    95/100 stars

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    Related Articles

    other:

    Article Title: Caloric Restriction Mimetics Slow Aging of Neuromuscular Synapses and Muscle Fibers
    Article Snippet: Induction of Postsynaptic Sites on C2C12-Derived Myotubes Using Neural-Agrin The active region of neural-agrin ( 30 ) was purchased from R&D Systems (550-AG).

    Article Title: MuSK antibodies differently affect the MuSK signaling cascade depending on valency and epitope specificity
    Article Snippet: All mAbs were used at 7.7nM, neural agrin (550-AG-100, R&D systems) at 0.1nM, neuregulin (396-HB-050, R&D systems) at 4.9nM, EGF at 200ng/mL (236-EG-200, R&D systems), unless otherwise specified.

    Article Title: Caloric Restriction Mimetics Slow Aging of Neuromuscular Synapses and Muscle Fibers
    Article Snippet: The active region of neural-agrin ( 30 ) was purchased from R&D Systems (550-AG).

    Control:

    Article Title: Wnt signaling promotes AChR aggregation at the neuromuscular synapse in collaboration with agrin
    Article Snippet: .. After 3 days, myotubes were treated with control EGFP or Wnt3-HA conditioned medium obtained from transfected QT6 cells with or without 200 pM neural agrin (R&D Systems) for the indicated times at 37 °C. ..

    Transfection:

    Article Title: Wnt signaling promotes AChR aggregation at the neuromuscular synapse in collaboration with agrin
    Article Snippet: .. After 3 days, myotubes were treated with control EGFP or Wnt3-HA conditioned medium obtained from transfected QT6 cells with or without 200 pM neural agrin (R&D Systems) for the indicated times at 37 °C. ..

    Staining:

    Article Title: Transport and Secretion of the Wnt3 Ligand by Motor Neuron-like Cells and Developing Motor Neurons
    Article Snippet: .. Co-cultured cells were treated with 200 pM neural agrin (R&D Systems) for 12–18 h at 37 °C and then stained with Alexa488-conjugated α-BTX (1 μg/mL) (Molecular Probes; 1:500) for 1 h at 37 °C, washed, and fixed in 4% paraformaldehyde for 20 min at 4 °C. .. Acetylcholine receptor aggregates were imaged through z -stacks series, which were collected using a Zeiss LSM700 confocal laser-scanning microscope (CMA Bio-Bio, Universidad de Concepcion).

    In Vitro:

    Article Title: The extracellular matrix protein agrin promotes heart regeneration in mice
    Article Snippet: Isolation of cardiac cells Primary cardiac cells were isolated from P1 and P7 ICR mice using a neonatal dissociation kit (gentleMACS, Miltenyi Biotec) according to the manufacturer’s instructions, and cultured in gelatin-coated wells (0.02%, G1393, Sigma-Aldrich) with DMEM/F12 medium supplemented with L-glutamine, Na-pyruvate, non-essential amino acids, penicillin, streptomycin, 5% horse serum and 10% fetal bovine serum (FBS) at 37 °C and 5% CO 2 . .. In experiments involving administration of either neural agrin (R&D Systems, dose range 10–1,000 ng ml −1 in vitro ), ECM fragments, MMP inhibitors (marimastat, Sigma-Aldrich), MEK inhibitor (PD0325901), 10 μM Yap inhibitor (verteporfin, Tocris) 28 , 29 or Dag1 inhibitory antibody (05-593, Millipore) the cells were allowed to adhere for 48 h before treatment. ..



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    Figure 7. Domains of LRP4 interacting with ColQ. A, schematic representation of ectoLRP4-AP and its deletion mutants. B, plate-binding assays. Same concentrations of ectoLRP4-AP and of the indicated deletion mutants were added to ColQ-coated or CT wells. Bound proteins were quantified by measuring AP activity. Results are expressed as the mean ± SEM percentage of the control value set as 100% (ectoLRP4-AP bound to CT wells). n ≥6; **p < 0.01; ****p < 0.0001, using two-way ANOVA followed by Tukey’s multiple comparison post hoc test. For interaction factor: F = 18.07, p < 0.0001; for CT versus ColQ: F = 162, p < 0.0001; for the comparison of the different ectoLRP4 mutants: F = 21.01, p < 0.0001. The N-terminal region of LRP4 plays a crucial role in ColQ–LRP4 interaction as its deletion (ectoLRP4Δ1-AP) compromised binding to ColQ. Conversely, the N-terminal region alone (ectoLRP4Δ234-AP) bound to ColQ at the same level as ectoLRP4-AP. C, ColQ-coated wells were incubated with 25 nM of ectoLRP4-AP in the presence or not of 500 nM purified re- combinant neural agrin. Results are the mean ± SEM percentage of ectoLRP4-AP bound to ColQ wells in the absence of agrin (set as 100%; n = 9, ***p < 0.001, using one-sample t test). The binding of ecto-LRP4 to ColQ was reduced by more than 50% in the presence of agrin. D, pull-down assay where ColQ- coated beads were incubated with 500 nM of His-tagged <t>recombinant</t> neural agrin. Agrin signals were analyzed by Western immunoblot using antibodies against His-tag. No agrin was coprecipitated with ColQ. AP, alkaline phosphatase; ColQ, collagen Q; LRP4, low-density lipoprotein receptor–related protein 2; ns, not significant.
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    Figure 7. Domains of LRP4 interacting with ColQ. A, schematic representation of ectoLRP4-AP and its deletion mutants. B, plate-binding assays. Same concentrations of ectoLRP4-AP and of the indicated deletion mutants were added to ColQ-coated or CT wells. Bound proteins were quantified by measuring AP activity. Results are expressed as the mean ± SEM percentage of the control value set as 100% (ectoLRP4-AP bound to CT wells). n ≥6; **p < 0.01; ****p < 0.0001, using two-way ANOVA followed by Tukey’s multiple comparison post hoc test. For interaction factor: F = 18.07, p < 0.0001; for CT versus ColQ: F = 162, p < 0.0001; for the comparison of the different ectoLRP4 mutants: F = 21.01, p < 0.0001. The N-terminal region of LRP4 plays a crucial role in ColQ–LRP4 interaction as its deletion (ectoLRP4Δ1-AP) compromised binding to ColQ. Conversely, the N-terminal region alone (ectoLRP4Δ234-AP) bound to ColQ at the same level as ectoLRP4-AP. C, ColQ-coated wells were incubated with 25 nM of ectoLRP4-AP in the presence or not of 500 nM purified re- combinant neural agrin. Results are the mean ± SEM percentage of ectoLRP4-AP bound to ColQ wells in the absence of agrin (set as 100%; n = 9, ***p < 0.001, using one-sample t test). The binding of ecto-LRP4 to ColQ was reduced by more than 50% in the presence of agrin. D, pull-down assay where ColQ- coated beads were incubated with 500 nM of His-tagged recombinant neural agrin. Agrin signals were analyzed by Western immunoblot using antibodies against His-tag. No agrin was coprecipitated with ColQ. AP, alkaline phosphatase; ColQ, collagen Q; LRP4, low-density lipoprotein receptor–related protein 2; ns, not significant.

    Journal: The Journal of biological chemistry

    Article Title: The collagen ColQ binds to LRP4 and regulates the activation of the Muscle-Specific Kinase-LRP4 receptor complex by agrin at the neuromuscular junction.

    doi: 10.1016/j.jbc.2023.104962

    Figure Lengend Snippet: Figure 7. Domains of LRP4 interacting with ColQ. A, schematic representation of ectoLRP4-AP and its deletion mutants. B, plate-binding assays. Same concentrations of ectoLRP4-AP and of the indicated deletion mutants were added to ColQ-coated or CT wells. Bound proteins were quantified by measuring AP activity. Results are expressed as the mean ± SEM percentage of the control value set as 100% (ectoLRP4-AP bound to CT wells). n ≥6; **p < 0.01; ****p < 0.0001, using two-way ANOVA followed by Tukey’s multiple comparison post hoc test. For interaction factor: F = 18.07, p < 0.0001; for CT versus ColQ: F = 162, p < 0.0001; for the comparison of the different ectoLRP4 mutants: F = 21.01, p < 0.0001. The N-terminal region of LRP4 plays a crucial role in ColQ–LRP4 interaction as its deletion (ectoLRP4Δ1-AP) compromised binding to ColQ. Conversely, the N-terminal region alone (ectoLRP4Δ234-AP) bound to ColQ at the same level as ectoLRP4-AP. C, ColQ-coated wells were incubated with 25 nM of ectoLRP4-AP in the presence or not of 500 nM purified re- combinant neural agrin. Results are the mean ± SEM percentage of ectoLRP4-AP bound to ColQ wells in the absence of agrin (set as 100%; n = 9, ***p < 0.001, using one-sample t test). The binding of ecto-LRP4 to ColQ was reduced by more than 50% in the presence of agrin. D, pull-down assay where ColQ- coated beads were incubated with 500 nM of His-tagged recombinant neural agrin. Agrin signals were analyzed by Western immunoblot using antibodies against His-tag. No agrin was coprecipitated with ColQ. AP, alkaline phosphatase; ColQ, collagen Q; LRP4, low-density lipoprotein receptor–related protein 2; ns, not significant.

    Article Snippet: After 5 days of differentiation, WT and ColQ-deficient myotubes were stimulated or not with 5 nM of recombinant rat neural agrin (R&D Systems) for 16 h. Muscle cells were fixed in 4% paraformaldehyde and incubated with Alexa Fluor 594– conjugated α-bungarotoxin (1:1000 dilution) for 1 h. Images were collected using a microscope (Olympus BX61) equipped with a Fast 1394 Digital CCD FireWire camera (model Retiga 2000R; Qimaging) and a 40× oil immersion objective (numerical aperture: 1.0; Olympus).

    Techniques: Binding Assay, Activity Assay, Control, Comparison, Incubation, Pull Down Assay, Recombinant, Western Blot