Recombinant Rat Agrin Protein Summary
Product Specifications
Ala1153-Pro1959 (Pro1788-Ser1798 del), with an N-terminal Met and 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
550-AG
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 500 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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550-AG/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: Agrin
Agrin is a 400‑600 kDa heparan sulfate proteoglycan component of the extracellular matrix. The N‑terminal half of rat Agrin, which mediates ECM interactions, contains nine Kazal-type protease inhibitor domains, two Laminin EGF-like domains, and one SEA domain. The C-terminal half contains four EGF-like repeats and three Laminin globular G domains. Human Agrin also contains a Laminin‑binding N-terminal Agrin domain (NtA), and mouse and chick Agrin include the NtA domain only by the use of an alternate promoter. Additional isoforms are generated by alternate splicing at sites Y and Z in the C-terminal half of rat Agrin (known as A and B, respectively in chick). Agrin isoforms that contain an insert at site Z (Z+ forms) are known as neural Agrin and are selectively produced by motoneurons. Other isoforms are known as muscle Agrin and are additionally expressed in non-neuronal tissues, particularly in basement membranes of the lung and kidney (1-3). This recombinant protein consists of the C-terminal half of rat Agrin and contains a nine amino acid (aa) insert at the Z site. It shares 59%, 80%, and 94% aa sequence identity with comparable regions of chick, human, and mouse Agrin, respectively. The C-terminal half of Z- and Z+ Agrin binds to alpha -Dystroglycan and mediates adhesion between motoneurons and myotubes at the neuromuscular junction (NMJ) (4-6). In contrast, only Z+ Agrin is effective at inducing clustering of the postsynaptic Acetylcholine Receptor (AChR) and presynaptic motoneuron differentiation (7, 8). Agrin‑induced AChR clustering requires a myotube receptor complex that contains alpha -Dystroglycan, MuSK, and LRP4 (4, 9-11). Agrin exhibits many functions in addition to NMJ development. It is enriched in senile Alzheimer’s disease plaques where it binds the A beta (1-40) peptide and promotes amyloid fibril formation (12). It regulates neuronal excitability by binding and inhibiting the alpha 3 subunit of the neuronal Na/K ATPase (13). It functions as an epithelial cell attachment receptor for HIV-1 through interactions with the gp41 coat protein (14). During T cell activation, Agrin contributes to formation of the immunological synapse and regulates the threshold of T cell activation (15).
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Citations for Recombinant Rat Agrin Protein
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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Neuronal Agrin Promotes Proliferation of Primary Human Myoblasts in an Age-Dependent Manner
Authors: K Gros, U Matkovi?, G Parato, K Miš, E Luin, A Bernareggi, M Sciancalep, T Marš, P Lorenzon, S Pirkmajer
International Journal of Molecular Sciences, 2022-10-04;23(19):.
Species: Human
Sample Types: Whole Cells
Applications: Cell Culture -
Control of CRK-RAC1 activity by the miR-1/206/133 miRNA family is essential for neuromuscular junction function
Authors: I Klockner, C Schutt, T Gerhardt, T Boettger, T Braun
Nature Communications, 2022-06-08;13(1):3180.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Differential vulnerability of hippocampal CA3-CA1 synapses to Abeta
Authors: OA Shipton, CS Tang, O Paulsen, M Vargas-Cab
Acta neuropathologica communications, 2022-04-04;10(1):45.
Species: Human
Sample Types: Whole Cells
Applications: Differentiation, Differentiation -
Involvement of neuronal and muscular Trk-fused gene (TFG) defects in the development of neurodegenerative diseases
Authors: T Yamamotoya, S Hasei, Y Akasaka, Y Ohata, Y Nakatsu, M Kanna, M Fujishiro, H Sakoda, H Ono, A Kushiyama, H Misawa, T Asano
Scientific Reports, 2022-02-04;12(1):1966.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Transport and Secretion of the Wnt3 Ligand by Motor Neuron-like Cells and Developing Motor Neurons
Authors: C Pinto, V Pérez, J Mella, M Albistur, T Caprile, FC Bronfman, JP Henríquez
Biomolecules, 2021-12-17;11(12):.
Species: Mouse
Sample Types: Transfected Whole Cells
Applications: Bioassay -
Mechanism of disease and therapeutic rescue of Dok7 congenital myasthenia
Authors: J Oury, W Zhang, N Leloup, A Koide, AD Corrado, G Ketavarapu, T Hattori, S Koide, SJ Burden
Nature, 2021-06-23;0(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Activation of skeletal muscle-resident glial cells upon nerve injury
Authors: D Proietti, L Giordani, M De Bardi, C D'Ercole, B Lozanoska-, S Amadio, C Volontè, S Marinelli, A Muchir, M Bouchè, G Borsellino, A Sacco, PL Puri, L Madaro
JCI Insight, 2021-04-08;0(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Neuronal MT1-MMP mediates ECM clearance and Lrp4 cleavage for agrin deposition and signaling in presynaptic development
Authors: MJ Oentaryo, AC Tse, CW Lee
J. Cell. Sci., 2020-08-05;0(0):.
Species: Xenopus
Sample Types: Whole Cells
Applications: Bioassay -
Phosphorylation of alpha-dystrobrevin is essential for alphakap accumulation and acetylcholine receptor stability
Authors: PJ Chen, D Zelada, DC Belhasan, M Akaaboune
J. Biol. Chem., 2020-06-12;0(0):.
Species: Mouse
Sample Types: Transfected Whole Cells
Applications: Bioassay -
A mechanism in Agrin signaling revealed by a prevalent Rapsyn mutation in congenital myasthenic syndrome
Authors: G Xing, H Jing, L Zhang, Y Cao, L Li, K Zhao, Z Dong, W Chen, H Wang, R Cao, WC Xiong, L Mei
Elife, 2019-09-24;8(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
A Role of Agrin in Maintaining the Stability of Vascular Endothelial Growth Factor Receptor-2 during Tumor Angiogenesis
Authors: K Njah, S Chakrabort, B Qiu, S Arumugam, A Raju, AV Pobbati, M Lakshmanan, V Tergaonkar, G Thibault, X Wang, W Hong
Cell Rep, 2019-07-23;28(4):949-965.e7.
Species: Human, Mouse
Sample Types: In Vivo, Whole Cells, Whole Tissue
Applications: Bioassay, In Vivo -
Characterization of pathogenic monoclonal autoantibodies derived from muscle-specific kinase myasthenia gravis patients
Authors: K Takata, P Stathopoul, M Cao, M Mané-Damas, ML Fichtner, ES Benotti, L Jacobson, P Waters, SR Irani, P Martinez-M, D Beeson, M Losen, A Vincent, RJ Nowak, KC O'Connor
JCI Insight, 2019-06-20;4(12):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Cullin-3 dependent deregulation of ACTN1 represents a new pathogenic mechanism in nemaline myopathy
Authors: J Blondelle, K Tallapaka, JT Seto, M Ghassemian, M Clark, JM Laitila, A Bournazos, JD Singer, S Lange
JCI Insight, 2019-04-16;5(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Three-Dimensional Human iPSC-Derived Artificial Skeletal Muscles Model Muscular Dystrophies and Enable Multilineage Tissue Engineering
Authors: SM Maffiolett, S Sarcar, ABH Henderson, I Mannhardt, L Pinton, LA Moyle, H Steele-Sta, O Cappellari, KE Wells, G Ferrari, JS Mitchell, GE Tyzack, VN Kotiadis, M Khedr, M Ragazzi, W Wang, MR Duchen, R Patani, PS Zammit, DJ Wells, T Eschenhage, FS Tedesco
Cell Rep, 2018-04-17;23(3):899-908.
Applications: Bioassay -
Lack of Fgf18 causes abnormal clustering of motor nerve terminals at the neuromuscular junction with reduced acetylcholine receptor clusters
Authors: K Ito, B Ohkawara, H Yagi, H Nakashima, M Tsushima, K Ota, H Konishi, A Masuda, S Imagama, H Kiyama, N Ishiguro, K Ohno
Sci Rep, 2018-01-11;8(1):434.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Cullin E3 ligase activity is required for myoblast differentiation
Authors: J Blondelle, P Shapiro, AA Domenighet, S Lange
J. Mol. Biol, 2017-02-24;0(0):.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
R-spondin 2 promotes acetylcholine receptor clustering at the neuromuscular junction via Lgr5
Authors: Hiroaki Nakashima
Sci Rep, 2016-06-22;6(0):28512.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Coronin 6 regulates acetylcholine receptor clustering through modulating receptor anchorage to actin cytoskeleton.
Authors: Chen, Yuewen, Ip, Fanny C, Shi, Lei, Zhang, Zhe, Tang, Huibin, Ng, Yu Pong, Ye, Wen-Cai, Fu, Amy K Y, Ip, Nancy Y
J Neurosci, 2014-02-12;34(7):2413-21.
Species: Rat
Sample Types: Whole Tissue
Applications: Bioassay -
LRP4 third beta-propeller domain mutations cause novel congenital myasthenia by compromising agrin-mediated MuSK signaling in a position-specific manner.
Authors: Ohkawara B, Cabrera-Serrano M, Nakata T, Milone M, Asai N, Ito K, Ito M, Masuda A, Ito Y, Engel A, Ohno K
Hum Mol Genet, 2013-11-13;23(7):1856-68.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
APP interacts with LRP4 and agrin to coordinate the development of the neuromuscular junction in mice.
Authors: Choi H, Liu Y, Tennert C, Sugiura Y, Karakatsani A, Kroger S, Johnson E, Hammer R, Lin W, Herz J
Elife, 2013-08-20;2(0):e00220.
Applications: Bioassay -
Agrin regulates growth cone turning of Xenopus spinal motoneurons.
Authors: Xu X, Fu AK, Ip FC, Wu CP, Duan S, Poo MM, Yuan XB, Ip NY
Development, 2005-09-01;132(19):4309-16.
Species: Xenopus
Sample Types: Whole Cells
Applications: Bioassay -
Postsynaptic requirement for Abl kinases in assembly of the neuromuscular junction.
Authors: Finn AJ, Feng G, Pendergast AM
Nat. Neurosci., 2003-07-01;6(7):717-23.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay
FAQs
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What is the isoform of 550-AG?
The source sequence is Ala1153-Pro1959 (Pro1788-Ser1798 del), Accession # P25304.2, with an N-terminal Met and 6-His tag. This is Isoform 4 in the NCBI database.
Reviews for Recombinant Rat Agrin Protein
Average Rating: 5 (Based on 1 Review)
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Reason for Rating: Recombinant protein performed very well. (!) Induced potent AChR clustering activity in C2C12 myotubes, (2) Bound heparin (because of KSRK splice site), and (3) Activated MuSK phosphorylation in Western blot assays.
Shown here are differentiated C2C12 mouse skeletal muscle myotubes treated with or without agrin (5 nM) in DMEM (1 hr, 37C). Subsequent staining with fluorophore-labeled-alpha bungarotoxin revealed robust AChR clusters (green) in agrin-treated myotubes.