Rat Agrin Antibody Summary
Ala1153-Pro1959 (Pro1788-Ser1798 del)
Accession # P25304
Rat Agrin Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Acetylcholine Receptor Clustering Induced by Agrin and Neutralization by Rat Agrin Antibody. Recombinant Rat Agrin (Catalog # 550-AG) induces acetylcholine receptor clustering on chick myotubes in a dose-dependent manner (orange line). Acetylcholine Receptor Clustering elicited by Recom-binant Rat Agrin (0.016 µg/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Rat Agrin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF550). The ND50 is typically 0.001-0.004 µg/mL.
Agrin in Mouse Kidney. Agrin was detected in perfusion fixed frozen sections of mouse kidney using Goat Anti-Rat Agrin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF550) at 0.1 µg/mL overnight at 4 °C. Tissue was stained using the Northern-Lights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). Specific staining was localized to basement membrane of epithelial cells in tubules and endothelial cells in glomeruli. View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Agrin, a heparan sulfate proteoglycan, is a component of the synaptic basal lamina which promotes acetylcholine receptor (AChR) clustering on cultured myotubes and in vivo. This AChR clustering activity has been shown to be mediated via a receptor complex that includes a receptor-like tyrosine kinase specific to the skeletal muscle termed muscle-specific kinase (MuSK), and an as of yet unidentified myotube-specific accessory component.
Agrin contains a number of distinct domains. The N-terminal half of the molecule, which is responsible for the tight interaction with the extracellular matrix, has nine follistatin-like repeats that share homology to Kazal-type protease inhibitor domains. The C-terminal half, which by itself is sufficient for the AChR clustering activity, has four EGF-like repeats and three laminin globular G domains. Agrin exists in several isoforms which are generated by alternative splicing at multiple splicing sites in the C-terminal half. Some of these isoforms are expressed specifically in the nervous system while other isoforms are expressed in both neural and nonneural tissues. Dramatic differences in AChR clustering activities have been observed between the different isoforms. The highest activity is found to be associated with isoforms found exclusively in neural tissues that contain the four amino acids K-S-R-K at position # 1643‑1646 and the eight amino acids E-L-T-N-E-I-P-A after Ser1779. Rat and chick Agrin share approximately 60% amino acid sequence identity. R&D Systems recombinant C-terminal half fragment of Agrin is a soluble secreted protein which has been found to have AChR clustering activity on chick myotubes.
Citations for Rat Agrin Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 3
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Evidence of a Myenteric Plexus Barrier and Its Macrophage-Dependent Degradation During Murine Colitis: Implications in Enteric Neuroinflammation
Authors: D Dora, S Ferenczi, R Stavely, VE Toth, ZV Varga, T Kovacs, I Bodi, R Hotta, KJ Kovacs, AM Goldstein, N Nagy
Cellular and Molecular Gastroenterology and Hepatology, 2021;0(0):.
Sample Types: Whole Tissue
Agrin, a novel basement membrane component in human and rat liver, accumulates in cirrhosis and hepatocellular carcinoma.
Authors: Tatrai P, Dudas J, Batmunkh E, MÃƒÂ¡thÃƒÂ© M, Zalatnai A, Schaff Z, Ramadori G, Kovalszky I
Lab. Invest., 2006;86(11):1149-60.
Sample Types: Whole Tissue
Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins.
Authors: Graf ER, Zhang X, Jin SX, Linhoff MW, Craig AM
Sample Types: Whole Cells
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