Search :
Sign in or Register  
Welcome Sign in or Don't have an account?Register

Mouse Anti-AGRN Monoclonal Antibody (V2-5182) (CBMAB-0930-YC)

Online Inquiry

Summary

Host Animal
Mouse
Specificity
Rat, Mouse
Clone
V2-5182
Antibody Isotype
IgG1
Application
ICC, WB

Basic Information

Immunogen
Recombinant rat agrin, C-terminal construct
Host Species
Mouse
Specificity
Rat, Mouse
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
IHC10 μg/ml

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 50% glycerol
Preservative
0.09% sodium azide
Concentration
Batch dependent
Purity
>95%, as determined by SDS-PAGE analysis
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Agrin
Introduction
Agrin is one of several proteins that are critical in the development of the neuromuscular junction (NMJ), as identified in mouse knock-out studies. Agrin contains several laminin G, Kazal type serine protease inhibitor, and epidermal growth factor domains. Mutation in this gene may associate with congenital myasthenic syndrome affecting limb-girdle muscles.
Entrez Gene ID
Mouse11603
Rat25592
UniProt ID
MouseA2ASQ1
RatP25304
Alternative Names
AGR
Function
Isoform 1: Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha3-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain.
Isoform 2: Transmembrane form that is the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.
Isoform 1, isoform 4 and isoform 5: Neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.
Isoform 3 and isoform 6: Lack any 'z' insert, are muscle-specific and may be involved in endothelial cell differentiation.
Agrin N-terminal 110 kDa subunit: Is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity).
Agrin C-terminal 22 kDa fragment: This released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.
Biological Process
Animal organ morphogenesis
Clustering of voltage-gated sodium channels
Extracellular matrix organization
Glycosaminoglycan biosynthetic process
Glycosaminoglycan catabolic process
G protein-coupled acetylcholine receptor signaling pathway
Neuromuscular junction development
Positive regulation of filopodium assembly
Positive regulation of GTPase activity
Positive regulation of synaptic growth at neuromuscular junction
Positive regulation of transcription by RNA polymerase II
Receptor clustering
Retinoid metabolic process
Signal transduction
Synapse organization
Tissue development
Cellular Location
Isoform 1: Extracellular matrix. Synaptic basal lamina at the neuromuscular junction.
Isoform 2: Cell membrane; Synapse
Involvement in disease
Myasthenic syndrome, congenital, 8 (CMS8): A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS8 is an autosomal recessive disease characterized by prominent defects of both the pre- and postsynaptic regions. Affected individuals have onset of muscle weakness in early childhood; the severity of the weakness and muscles affected is variable.
PTM
Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. Heparin and heparin sulfate binding in the G3 domain is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions (By similarity).
At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ).
More Infomation

Wang, Z. Q., Sun, X. L., Wang, Y. L., & Miao, Y. L. (2021). Agrin promotes the proliferation, invasion and migration of rectal cancer cells via the WNT signaling pathway to contribute to rectal cancer progression. Journal of Receptors and Signal Transduction, 41(4), 363-370.

Pratt, J., De Vito, G., Narici, M., Segurado, R., Pessanha, L., Dolan, J., ... & Boreham, C. (2021). Plasma C-Terminal Agrin Fragment as an Early Biomarker for Sarcopenia: Results from the Genofit Study. The Journals of Gerontology: Series A.

Rickelt, S., Condon, C., Mana, M., Whittaker, C., Pfirschke, C., Roper, J., ... & Hynes, R. O. (2020). Agrin in the Muscularis mucosa serves as a biomarker distinguishing hyperplastic polyps from sessile serrated lesions. Clinical Cancer Research, 26(6), 1277-1287.

Wang, A., Xiao, Y., Huang, P., Liu, L., Xiong, J., Li, J., ... & Liu, L. (2020). Novel NtA and LG1 Mutations in Agrin in a Single Patient Causes Congenital Myasthenic Syndrome. Frontiers in neurology, 11, 239.

Ohkawara, B., Shen, X., Selcen, D., Nazim, M., Bril, V., Tarnopolsky, M. A., ... & Engel, A. G. (2020). Congenital myasthenic syndrome–associated agrin variants affect clustering of acetylcholine receptors in a domain-specific manner. JCI insight, 5(7).

Topaloudi, A., Zagoriti, Z., Flint, A. C., Martinez, M. B., Yang, Z., Tsetsos, F., ... & Paschou, P. (2020). A Myasthenia Gravis genomewide association study of three cohorts identifies Agrin as a novel risk locus. medRxiv.

Eldridge, S. E., Barawi, A., Wang, H., Roelofs, A. J., Kaneva, M., Guan, Z., ... & Dell’Accio, F. (2020). Agrin induces long-term osteochondral regeneration by supporting repair morphogenesis. Science translational medicine, 12(559).

Zhang, H., Sathyamurthy, A., Liu, F., Li, L., Zhang, L., Dong, Z., ... & Mei, L. (2019). Agrin-Lrp4-Ror2 signaling regulates adult hippocampal neurogenesis in mice. Elife, 8, e45303.

Bassat, E., Mutlak, Y. E., Genzelinakh, A., Shadrin, I. Y., Umansky, K. B., Yifa, O., ... & Tzahor, E. (2017). The extracellular matrix protein agrin promotes heart regeneration in mice. Nature, 547(7662), 179-184.

Xi, J., Yan, C., Liu, W. W., Qiao, K., Lin, J., Tian, X., ... & Zhao, C. (2017). Novel SEA and LG2 Agrin mutations causing congenital Myasthenic syndrome. Orphanet journal of rare diseases, 12(1), 1-7.

Ask a question We look forward to hearing from you.
0 reviews or Q&As
Loading...
Have you used Mouse Anti-AGRN Monoclonal Antibody (V2-5182)?
Submit a review and get a Coupon or an Amazon gift card. 20% off Coupon $30 eGift Card
Submit a review
Loading...
For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

Learn more

Documents

Online Inquiry