Rat Agrin Antibody Summary
Ala1153-Pro1959 (Pro1788-Ser1798 del)
Accession # P25304
Applications
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.
Scientific Data
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.
Reconstitution Calculator
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.
Background: Agrin
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.
Product Datasheets
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.
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Citations: Showing 1 - 10
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A matrisome RNA signature from early-pregnancy mouse mammary fibroblasts predicts distant metastasis-free breast cancer survival in humans
Authors: Ayman M. Ibrahim, Alan Bilsland, Steffen Rickelt, Joanna S. Morris, Torsten Stein
Breast Cancer Research
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Inhibiting Matrix Metalloproteinases Protects Evoked Electromyography Amplitudes and Muscle Tension in the Orbicularis Oris Muscle in a Rat Model of Facial Nerve Injury
Authors: Shuang Wu, Lijun Song, Meirong Yu, Chao Gong, Lianhua Chen
Journal of Neuropathology & Experimental Neurology
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Glomerular basement membrane deposition of collagen ?1(III) in Alport glomeruli by mesangial filopodia injures podocytes via aberrant signaling through DDR1 and integrin ?2?1
Authors: Madison J, Wilhelm K, Meehan DT et al.
The Journal of Pathology
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Amelioration of Muscle and Nerve Pathology in LAMA2 Muscular Dystrophy by AAV9-Mini-Agrin
Authors: Chunping Qiao, Yi Dai, Viktoriya D. Nikolova, Quan Jin, Jianbin Li, Bin Xiao et al.
Molecular Therapy - Methods & Clinical Development
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Nerve pathology is prevented by linker proteins in mouse models for LAMA2-related muscular dystrophy
Authors: Judith R Reinhard, Emanuela Porrello, Shuo Lin, Pawel Pelczar, Stefano C Previtali, Markus A Rüegg
PNAS Nexus
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Nephronectin Regulates Mesangial Cell Adhesion and Behavior in Glomeruli
Authors: Susan E. Zimmerman, Chitkale Hiremath, Jun Tsunezumi, Zhufeng Yang, Bronwyn Finney, Denise K. Marciano
Journal of the American Society of Nephrology
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Glomerular basement membrane deposition of collagen ?1(III) in Alport glomeruli by mesangial filopodia injures podocytes via aberrant signaling through DDR1 and integrin ?2?1
Authors: Madison J, Wilhelm K, Meehan DT et al.
The Journal of Pathology
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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, 2021-07-08;0(0):.
Species: Mouse
Sample Types: Whole Tissue
Applications: IHC -
Agrin, a novel basement membrane component in human and rat liver, accumulates in cirrhosis and hepatocellular carcinoma.
Authors: Tatrai P, Dudas J, Batmunkh E, Máthé M, Zalatnai A, Schaff Z, Ramadori G, Kovalszky I
Lab. Invest., 2006-09-18;86(11):1149-60.
Species: Rat
Sample Types: Whole Tissue
Applications: IHC-Fr -
Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins.
Authors: Graf ER, Zhang X, Jin SX, Linhoff MW, Craig AM
Cell, 2004-12-29;119(7):1013-26.
Species: Rat
Sample Types: Whole Cells
Applications: ICC
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