Recombinant Mouse MuSK Fc Chimera Protein, CF

In the presence of Recombinant Mouse Agrin, immobilized Recombinant Mouse MuSK Fc Chimera (2 μg/mL at 100 μL/well) binds Recombinant Mouse LRP-4 (10229-LR) with an ED50 of 150-900 ng/mL.

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

Recombinant Mouse MuSK Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. In the presence of Recombinant Mouse Agrin, immobilized Recombinant Mouse MuSK Fc Chimera (2 µg/mL at 100 µL/well) binds Recombinant Mouse LRP-4 (Catalog # 10229-LR) with an ED₅₀ of 150‑900 ng/mL
• Source: Mouse myeloma cell line, NS0-derived mouse MuSK protein
  

  Mouse MuSK (Glu22-Thr494) Accession # Q61006.1	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: Q61006.1
• N-terminal Sequence: Glu22
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 79 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: 175-200, under non-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.
  • 2 weeks, 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 500 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 Mouse MuSK Fc Chimera Protein, CF

• EC 2.7.10
• EC 2.7.10.1
• MGC126323
• MGC126324
• muscle, skeletal, receptor tyrosine kinase
• MuSK
• skeletal receptor tyrosine-protein kinase

Background

MuSK (muscle-specific kinase) is a 100-kDa type I transmembrane (TM) protein belonging to the receptor tyrosine kinase family (1). It is found in the postsynaptic membrane of skeletal muscle motor endplates (2). MuSK contains a 473 aa extracellular domain (ECD), a 21 aa transmembrane domain, and a 353 cytoplasmic domain. Human MuSK has multiple isoforms. One contains deletions at residues 307-­394 and 454­-461, while a second is a short soluble form that contains residues 120­-209 plus a unique 24 aa C­terminal tail (3). Within the ECD, mouse MuSK shares 91% and 96% aa sequence identity with human and rat MuSK, respectively. MuSK is a crucial signaling molecule in the formation of the neuromuscular junction(NMJ). Defects in MuSK causes muscle weakness in congenital myathenic syndromes (4). MuSK binds the heparin sulfate proteoglycan agrin to promote acetylcholine receptor clustering. It has also been found to bind with low-density lipoprotein receptor-related protein 4 (LRP4) (5), Wnt ligands (6), Biglycan (7), ColQ (8) and BMPs(10). Recent studies have showed that MuSK does not bind agrin directly, but enhanced the MuSK-LRP4 interaction (8, 9). When agrin binds to the N-terminal region of LRP4, this promotes the association of LRP4 and MuSK, which then stimulates MuSK kinase activity (11, 12).

1. Valenzuela, D.M. et al. (1995) Neuron 15:573.
2. Finn, A.J. et al. (2003) Nat. Neurosci. 6:717.
3. Nasrin, F. et al. (2014) Sci. Rep. 4:6841.
4. DeChiara, T. et al. (1996) Cell 85:501.
5. Kim, N. et al. (2008) Cell 135:334.
6. Banerjee, S. et al. (2011) Development 138:3287.
7. Amenta, A.R. et al. (2012) J. Neurosci. 32:2324.
8. Otsuka, K. et al. (2015) Scientific Reports 5:13928.
9. Zhang, B. et al. (2008) Neuron 60:285.
10. Yilmaz, A. et al. (2016) Science Signaling 9:ra87.
11. Zhang, W. et al. (2011) J. Biol. Chem. 286:40624.
12. Burden, S.J. et al. (2017) CSH Perspectives Biol. 5:a009167.

Bioinformatics

• Uniprot:
  • Q61006.1()