Recombinant Mouse MUSK Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-9969P

Recombinant Mouse MUSK Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-9969P
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Product Overview

Host Species Mouse
Accession Q61006
Synonym CMS9 FADS MDK 4 MDK4 MGC126323 MGC126324 Muscle Muscle associated receptor tyrosine kinase Muscle skeletal receptor tyrosine kinase Muscle skeletal receptor tyrosine protein kinase Muscle specific kinase receptor Muscle specific tyrosine kinase receptor Muscle specific tyrosine protein kinase receptor Muscle-specific kinase receptor Muscle-specific tyrosine-protein kinase receptor MuSK MUSK_HUMAN Neural fold somite kinase 1 Neural fold somite kinase 2 Neural fold somite kinase 3 Neural fold somite kinase1 Neural fold somite kinase2 Neural fold somite kinase3 Nsk 1 Nsk 2 Nsk 3 Nsk1 Nsk2 Nsk3 Receptor tyrosine kinase MuSK Skeletal muscle receptor tyrosine kinase skeletal receptor tyrosine-protein kinase
Description Recombinant Mouse MUSK Protein (Tagged) was expressed in E.coli. It is a Protein fragment
Source E.coli
Molecular Weight 69 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle. Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation.
Subcellular Location Cell junction, synapse, postsynaptic cell membrane; Single-pass type I membrane protein. Note=Localizes to the postsynaptic cell membrane of the neuromuscular junction.
Protein Families Protein kinase superfamily, Tyr protein kinase family
Database References
Tissue Specificity Expressed preferentially in skeletal muscle.

Gene Functions References

  1. Gene expression profiling showed that MuSK was required for the BMP4-induced expression of a subset of genes in myoblasts, including regulator of G protein signaling 4 (Rgs4). PMID: 27601729
  2. These mice showed only marginal activation of MuSK and died by 3 weeks of age apparently due to an abnormally small number and size of neuromuscular junction (NMJs). PMID: 28069867
  3. data reveal that muscle skeletal receptor tyrosine kinase cysteine-rich domain is critical for neuromuscular junction formation and plays an unsuspected role in NMJ maintenance in adulthood. PMID: 25810523
  4. Forced expression of Dok-7 in muscle enhanced MuSK activation in mice lacking agrin or Lrp4 and restored midmuscle NMJ formation in agrin-deficient mice, but not in Lrp4-deficient mice. PMID: 25368159
  5. pathogenic IgG4 antibodies to MuSK bind to a structural epitope in the first Ig-like domain of MuSK, prevent binding between MuSK and Lrp4, and inhibit Agrin-stimulated MuSK phosphorylation. PMID: 24297891
  6. MuSK colocalizes with actin and Arf6 at the cell surface and during endosomal trafficking. PMID: 23621612
  7. Increasing MuSK activity delays denervation and improves motor function in ALS mice. PMID: 22939980
  8. Two classic synaptic signalling systems (neuregulin-1 and neural agrin) converge upon MuSK to regulate postsynaptic differentiation. PMID: 22328506
  9. Biglycan binding to MuSK rescues the unstable acetylcholine receptor clusters that are involved in neuromuscular junction formation and postsynaptic differentiation. PMID: 22396407
  10. Data suggest that adult skeletal muscles harbour different endogenous levels of MuSK and that these levels determine the ability to form ectopic AChR clusters upon overexpression of agrin or MuSK. PMID: 21255125
  11. Depletion of MuSK at the neuromuscular junction leads to disassembly of muscle-specific kinase and muscle weakness of myasthenia gravis in mice. PMID: 20603331
  12. Data show that expression of a chimeric receptor containing the juxtamembrane region of Musk and the kinase domain of TrkA restores presynaptic and postsynaptic differentiation in Musk-deficient mice. PMID: 12403715
  13. Activation of a musk promoter reporter construct in muscle fibers in vivo and in cultured myotubes, using transfection of multiple combinations of expression vectors for potential signaling components PMID: 12756238
  14. analysis of regulation of MuSK expression by a novel signaling pathway PMID: 12885777
  15. Our results suggest that muscle tyrosine phosphatases tightly regulate MuSK activation and signaling and support a novel role of Shp2 in MuSK-dependent AChR clustering. PMID: 15737732
  16. Musk expression was inhibited by CREB interacting with a CRE-like element with MyoD. PMID: 15964791
  17. Our findings demonstrate that MuSK kinase activity is required throughout postnatal development to hold up MuSK and AChR levels at endplates. PMID: 16337809
  18. A low-molecular weight isoform of muscle-specific receptor tyrosine kinase in mouse sperm localized in the flagellar mid-piece region of human sperm. PMID: 16487930
  19. These results demonstrate a novel pathway linking the NO-soluble guanylyl cyclase-cGMP pathway, SR Ca2+ release, PLB, and CaM kinase II to relaxation in gastric fundus smooth muscles. PMID: 16510846
  20. Dok-7 is essential for neuromuscular synaptogenesis through its interaction with MuSK PMID: 16794080
  21. muscle-specific receptor tyrosine kinase activation and binding to dystroglycan are regulated by alternative mRNA splicing of agrin PMID: 17012237
  22. A new member of the Shc family of docking proteins is characterised, which may mediate a specific aspect of signaling downstream of the MuSK receptor. PMID: 17452444
  23. MuSK controls where motor axons grow and form synapses. PMID: 18084289
  24. the COOH-terminal NES and Src homology 2 target motifs play key roles in Dok-7/MuSK signaling for neuromuscular synaptogenesis. PMID: 18165682
  25. The IGg1/2 domain of MuSK is involved in acetylcholine receptor clustering by binding to the muscle surface. PMID: 18253062
  26. Our study reveals a potentially novel mechanism that regulates agrin/MuSK signaling cascade. PMID: 18272689
  27. adult musk(V789M/-) mice show severe muscle weakness; diaphragm exhibits pronounced changes in endplate architecture, distribution & innervation; missense mutation V789M in MuSK acts as a hypomorphic mutation & leads to insufficiency in MuSK function PMID: 18718936
  28. These experiments indicate that Lrp4 is the long-sought and elusive receptor for Agrin and has a critical role in activating MuSK and stimulating neuromuscular synapse formation. PMID: 18848351


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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