Recombinant Human Agrin Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Agrin Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of U‑87 MG human glioblastoma/astrocytoma cells. The typical ED₅₀ for this effect is 0.9-3.6 μg/mL after 1 hour incubation at 37 °C.

  Optimal dilutions should be determined by each laboratory for each application.

• Source: Chinese Hamster Ovary cell line, CHO-derived human Agrin protein
  Ala1260-Pro2045, with an N-terminal 6-His tag
• Accession #: NP_940978
• N-terminal Sequence: His
• Structure / Form: Monomer
• Protein/Peptide Type: Recombinant Proteins
• Gene: AGRN
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 83.5 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 100-110 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 300 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Agrin Protein, CF

• agrin proteoglycan
• Agrin
• AGRN

Background

Agrin is a 400‑600 kDa heparan sulfate proteoglycan component of the extracellular matrix. The N-terminal half of human Agrin, which mediates ECM interactions, contains a Laminin-binding NtA domain, 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. Rat Agrin lacks the NtA domain, 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 human Agrin corresponding to the Z- isoform of rat Agrin. It shares 60%, 78%, and 80% amino acid sequence identity with comparable regions of chick, mouse, and rat 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).

1. Jury, E.C. and P.S. Kabouridis (2010) Arthritis Res. Ther. 12:205.
2. Bezakova, G. and M.A. Ruegg (2003) Nat. Rev. Mol. Cell Biol. 4:295.
3. Groffen, A.J.A. et al. (1998) Eur. J. Biochem. 254:123.
4. Gee, S.H. et al. (1994) Cell 77:675.
5. Sugiyama, J. et al. (1994) Neuron 13:103.
6. Gesemann, M. et al. (1998) J. Biol. Chem. 273:600.
7. Burgess, R.W. et al. (1999) Neuron 23:33.
8. Ferns, M.J. et al. (1993) Neuron 11:491.
9. Glass, D.J. et al. (1996) Cell 85:513.
10. Kim, N. et al. (2008) Cell 135:334.
11. Zhang, B. et al. (2008) Neuron 60:285.
12. Cotman, S.L. et al. (2000) Mol. Cell. Neurosci. 15:183.
13. Hilgenberg, L.G.W. et al. (2006) Cell 125:359.
14. Alfsen, A. et al. (2005) Mol. Biol. Cell 16:4267.
15. Khan, A.A. et al. (2001) Science 292:1681.

Publications for Agrin (6624-AG)(11)

Publications using 6624-AG

• Naniwa, S;Nishida, K;Yoshida, A;Nasu, Y;Nakahara, R;Ohtsuki, T;Hotta, Y;Shimizu, N;Ichikawa, C;Lin, D;Otsuka, N;Ozaki, T; LRP4 and Agrin Are Modulated by Cartilage Degeneration and Involved in ?-Catenin Signaling in Human Articular Chondrocytes International journal of molecular sciences 2025-01-24 [PMID: 39940775] (Bioassay, Human)
• Silvestri, B;Mochi, M;Mawrie, D;de Turris, V;Colantoni, A;Borhy, B;Medici, M;Anderson, EN;Garone, MG;Zammerilla, CP;Simula, M;Ballarino, M;Pandey, UB;Rosa, A; HuD impairs neuromuscular junctions and induces apoptosis in human iPSC and Drosophila ALS models Nature communications 2024-11-07 [PMID: 39511225] (Bioassay, Human)
• Barbeau, S;Semprez, F;Dobbertin, A;Merriadec, L;Roussange, F;Eymard, B;Sternberg, D;Fournier, E;Karasoy, H;Martinat, C;Legay, C; Molecular Analysis of a Congenital Myasthenic Syndrome Due to a Pathogenic Variant Affecting the C-Terminus of ColQ International journal of molecular sciences 2023-11-11 [PMID: 38003406] (Differentiation, Human)
• Y Yamashita, S Nakada, K Nakamura, H Sakurai, K Ohno, T Goto, Y Mabuchi, C Akazawa, N Hattori, E Arikawa-Hi Evaluation of Human-Induced Pluripotent Stem Cells Derived from a Patient with Schwartz-Jampel Syndrome Revealed Distinct Hyperexcitability in the Skeletal Muscles Biomedicines, 2023-03-07;11(3):. 2023-03-07 [PMID: 36979792] (Cell Culture, Human, Mouse)
• K Stoklund D, L Terrie, P Baatsen, A Kerstens, L De Swert, R Janky, N Corthout, P Masrori, P Van Damme, P Hyttel, M Meyer, L Thorrez, K Freude, L Van Den Bo FUS-ALS hiPSC-derived astrocytes impair human motor units through both gain-of-toxicity and loss-of-support mechanisms Molecular Neurodegeneration, 2023-01-18;18(1):5. 2023-01-18 [PMID: 36653804] (Bioassay, Human)
• M Pandya, G Gopinathan, C Tillberg, J Wang, X Luan, TGH Diekwisch The Hippo Pathway Effectors YAP/TAZ Are Essential for Mineralized Tissue Homeostasis in the Alveolar Bone/Periodontal Complex Journal of developmental biology, 2022-03-01;10(1):. 2022-03-01 [PMID: 35323233] (Cell Culture, Human)
• K Stoklund D, EN Krasnow, L Fumagalli, T Vandoorne, P Baatsen, A Kerstens, G Giacomazzi, B Pavie, E Rossaert, J Beckers, M Sampaolesi, P Van Damme, L Van Den Bo Human motor units in microfluidic devices are impaired by FUS mutations and improved by HDAC6 inhibition Stem Cell Reports, 2021-04-22;0(0):. 2021-04-22 [PMID: 33891869] (Bioassay, Human)
• CY Lin, M Yoshida, LT Li, A Ikenaka, S Oshima, K Nakagawa, H Sakurai, E Matsui, T Nakahata, MK Saito iPSC-derived functional human neuromuscular junctions model the pathophysiology of neuromuscular diseases JCI Insight, 2019-09-19;4(18):. 2019-09-19 [PMID: 31534050] (Bioassay, Human)
• N Nagy, C Barad, R Hotta, S Bhave, E Arciero, D Dora, AM Goldstein Collagen 18 and agrin are secreted by enteric neural crest cells to remodel their microenvironment and regulate their migration during ENS development Development, 2018-05-08;0(0):. 2018-05-08 [PMID: 29678817] (Bioassay, Chicken)
• ME Katt, RM Linville, LN Mayo, ZS Xu, PC Searson Functional brain-specific microvessels from iPSC-derived human brain microvascular endothelial cells: the role of matrix composition on monolayer formation Fluids Barriers CNS, 2018-02-20;15(1):7. 2018-02-20 [PMID: 29463314] (Bioassay, Human)
• The Different Binding Properties of Cultured Human Corneal Endothelial Cell Subpopulations to Descemet&#039;s Membrane Components Invest Ophthalmol Vis Sci, 2016-09-01;57(11):4599-605. 2016-09-01 [PMID: 27598865] (Bioassay, Human)

Review for Agrin (6624-AG) (1)

Average Rating: 4

(Based on 1 review)

reviewed by: Patricia Carulla Martí In vitro bioactivity in cell culture 05/30/2024

Summary

• Application: In vitro bioactivity in cell culture
• Lot: SGX0621121

Bioinformatics

• Gene Symbol: AGRN
• Uniprot:
  • NP_940978()