Recombinant Human Agrin Protein, N-terminal, CF

R&D Systems, part of Bio-Techne | Catalog # 8909-AG

R&D Systems, part of Bio-Techne
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8909-AG-050
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Key Product Details

Source

CHO

Accession #

O00468

Conjugate

Unconjugated

Applications

Bioactivity

View all Agrin Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Agrin protein
Thr30-Arg1102, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE with silver staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Thr30

Predicted Molecular Mass

113 kDa

SDS-PAGE

138-181 kDa, reducing conditions

Activity

Measured by its ability to inhibit neurite outgrowth of E16-E18 rat embryonic cortical neurons on a Laminin  alpha4 coated plate.
Able to significantly inhibit neurite outgrowth when immobilized as a 3 μL droplet containing 50 ng of protein.

Formulation, Preparation and Storage

8909-AG
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 500 μg/mL in PBS.

Reconstitution Buffer Available:
Size / Price
Qty
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: Agrin

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 Follistatin-like/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 alternative 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). In addition, multiple proteolytic fragments of Agrin are produced by Neurotrypsin, MMP-1, -7, -12, and -14 (4, 5). This recombinant protein consists of the N-terminal region of human Agrin (up to the Neurotrypsin alpha-cleavage site upstream of the SEA domain) (4). It shares 80% amino acid sequence identity with comparable regions of mouse and rat Agrin. The N-terminal region binds to BMP-2, BMP-4, and TGF-beta, and it blocks BMP-induced signaling through BMPR1A (6). 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) (7-9). In contrast, only Z+ Agrin is effective at inducing clustering of the postsynaptic Acetylcholine Receptor (AChR) and presynaptic motoneuron differentiation (10, 11). Agrin-induced AChR clustering requires a myotube receptor complex that contains alpha-Dystroglycan, MuSK, and LRP4 (7, 12-14). 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 (15). It regulates neuronal excitability by binding and inhibiting the alpha3 subunit of the neuronal Na/K ATPase (16). It functions as an epithelial cell attachment receptor for HIV-1 through interactions with the gp41 coat protein (17). During T cell activation, Agrin contributes to formation of the immunological synapse and regulates the threshold of T cell activation (18). Agrin is up-regulated in hepocellular carcinoma, where it enhances cell proliferation and tumor progression (19).

References

  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. Reif, R. et al. (2007) FASEB J. 21:3466.
  5. Patel, T.R. et al. (2012) PLoS ONE 9:e43669.
  6. Banyai, L. et al. (2010) PLoS ONE 5:e10758.
  7. Gee, S.H. et al. (1994) Cell 77:675.
  8. Sugiyama, J. et al. (1994) Neuron 13:103.
  9. Gesemann, M. et al. (1998) J. Biol. Chem. 273:600.
  10. Burgess, R.W. et al. (1999) Neuron 23:33.
  11. Ferns, M.J. et al. (1993) Neuron 11:491.
  12. Glass, D.J. et al. (1996) Cell 85:513.
  13. Kim, N. et al. (2008) Cell 135:334.
  14. Zhang, B. et al. (2008) Neuron 60:285.
  15. Cotman, S.L. et al. (2000) Mol. Cell. Neurosci. 15:183.
  16. Hilgenberg, L.G.W. et al. (2006) Cell 125:359.
  17. Alfsen, A. et al. (2005) Mol. Biol. Cell 16:4267.
  18. Khan, A.A. et al. (2001) Science 292:1681.
  19. Chakraborty, S. et al. (2015) Nat. Comun. 6:6184.

Alternate Names

AGRN

Entrez Gene IDs

375790 (Human); 11603 (Mouse); 25592 (Rat)

Gene Symbol

AGRN

UniProt

O00468

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