Recombinant Mouse Agrin His-tag Protein, CF

Measured by its binding ability in a functional ELISA. Recombinant Mouse Agrin His-tag Protein (Catalog # 11573-AG) binds to Recombinant Mouse LRP-4 His-tag Protein (10229-LR) with an ED50 of 30.0‑300 ng/mL.

2 μg/lane of Recombinant Mouse Agrin His-tag Protein (Catalog # 11573-AG) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 114-128 kDa under reducing conditions.

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

Recombinant Mouse Agrin His-tag Protein, CF Summary

• Accession #: A2ASQ1.1
• N-terminal Sequence: His (of 6-His tag)
• Protein/Peptide Type: Recombinant Proteins

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 105 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: 114-128 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Reconstitution Instructions: Reconstitute at 1.00 mg/mL in PBS.

Notes

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

Alternate Names for Recombinant Mouse Agrin His-tag 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 mouse 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 mouse Agrin. It shares 59%, 82%, and 94% aa sequence identity with comparable regions of chick, human, 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. Rupp, F. et al. (1991) Neuron 6:811.
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.

Bioinformatics

• Uniprot:
  • A2ASQ1.1()