Muscle-specific tyrosine-protein kinase receptor; MuSK; Muscle-specific kinase receptor

For Research Use Only. Not for use in diagnostic procedures.

E Coli or Yeast or Baculovirus or Mammalian Cell

Greater than 90% as determined by SDS-PAGE. (lot specific)

Liquid containing glycerol

This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.

Sterile filter available upon request.

Low endotoxin available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of MUSK recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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 mory formation. 1 Publication

Signal Transduction

(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)

79.9kD

muscle, skeletal, receptor tyrosine kinase

muscle, skeletal receptor tyrosine-protein kinase

Muscle, skeletal receptor tyrosine-protein kinase

MuSK; Muscle-specific kinase receptor??[Similar Products]

MUSK_HUMAN

This gene encodes a muscle-specific tyrosine kinase receptor. The encoded protein may play a role in clustering of the acetylcholine receptor in the postsynaptic neuromuscular junction. Mutations in this gene have been associated with congenital myasthenic syndrome. Alternatively spliced transcript variants have been described.[provided by RefSeq, Oct 2009]

MUSK: a receptor tyrosine kinase that is essential for the establishment and maintenance of the neuromuscular junction (NMJ). Its activation by agrin, a neuronally derived heparan-sulfate proteoglycan, and the agrin receptor (LRP4), leads to clustering of acetylcholine receptors on the postsynaptic side of the NMJ. Its activation by agrin requires Dok7, which interacts with the cytoplasmic portion of MuSK and activates its tyrosine kinase activity.

Protein type: Protein kinase, tyrosine (receptor); Protein kinase, TK; EC 2.7.10.1; Kinase, protein; Membrane protein, integral; TK group; Musk family

Chromosomal Location of Human Ortholog: 9q31.3-q32

Cellular Component: cell junction; integral to plasma membrane; neuromuscular junction; postsynaptic membrane; receptor complex

Molecular Function: ATP binding; metal ion binding; protein binding; protein-tyrosine kinase activity; transmembrane receptor protein tyrosine kinase activity

Biological Process: cell differentiation; extracellular matrix organization and biogenesis; memory; multicellular organismal development; neuromuscular junction development; peptidyl-tyrosine phosphorylation; positive regulation of neuron apoptosis; positive regulation of protein amino acid phosphorylation; protein amino acid autophosphorylation; regulation of synaptic growth at neuromuscular junction; regulation of transcription, DNA-dependent; transmembrane receptor protein tyrosine kinase signaling pathway

Disease: Fetal Akinesia Deformation Sequence; Myasthenic Syndrome, Congenital, 9, Associated With Acetylcholine Receptor Deficiency

Receptor tyrosine kinase specific for the skeletal muscle lineage expression in embryonic muscle, at the neuromuscular junction, and after injury.Valenzuela D.M., Stitt T.N., DiStefano P.S., Rojas E., Mattsson K., Compton D.L., Nunez L., Park J.S., Stark J.L., Gies D.R., Thomas S., LeBeau M.M., Fernald A.A., Copeland N.G., Jenkins N.A., Burden S.J., Glass D.J., Yancopoulos G.D.Neuron 15:573-584(1995) DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004) The cytoplasmic adaptor protein Dok7 activates the receptor tyrosine kinase MuSK via dimerization.Bergamin E., Hallock P.T., Burden S.J., Hubbard S.R.Mol. Cell 39:100-109(2010) Development and validation of a method for profiling post-translational modification activities using protein microarrays.Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.PLoS ONE 5:E11332-E11332(2010) MUSK, a new target for mutations causing congenital myasthenic syndrome.Chevessier F., Faraut B., Ravel-Chapuis A., Richard P., Gaudon K., Bauche S., Prioleau C., Herbst R., Goillot E., Ioos C., Azulay J.-P., Attarian S., Leroy J.-P., Fournier E., Legay C., Schaeffer L., Koenig J., Fardeau M., Eymard B., Pouget J., Hantai D.Hum. Mol. Genet. 13:3229-3240(2004) Patterns of somatic mutation in human cancer genomes.Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.Nature 446:153-158(2007) Refinement of the clinical phenotype in musk-related congenital myasthenic syndromes.Mihaylova V., Salih M.A., Mukhtar M.M., Abuzeid H.A., El-Sadig S.M., von der Hagen M., Huebner A., Nurnberg G., Abicht A., Muller J.S., Lochmuller H., Guergueltcheva V.Neurology 73:1926-1928(2009) Mutations in MUSK causing congenital myasthenic syndrome impair MuSK-Dok-7 interaction.Maselli R.A., Arredondo J., Cagney O., Ng J.J., Anderson J.A., Williams C., Gerke B.J., Soliven B., Wollmann R.L.Hum. Mol. Genet. 19:2370-2379(2010) A mutation causes MuSK reduced sensitivity to agrin and congenital myasthenia.Ben Ammar A., Soltanzadeh P., Bauche S., Richard P., Goillot E., Herbst R., Gaudon K., Huze C., Schaeffer L., Yamanashi Y., Higuchi O., Taly A., Koenig J., Leroy J.P., Hentati F., Najmabadi H., Kahrizi K., Ilkhani M., Fardeau M., Eymard B., Hantai D.PLoS ONE 8:E53826-E53826(2013) Identification of a Dutch founder mutation in MUSK causing fetal akinesia deformation sequence.Tan-Sindhunata M.B., Mathijssen I.B., Smit M., Baas F., de Vries J.I., van der Voorn J.P., Kluijt I., Hagen M.A., Blom E.W., Sistermans E., Meijers-Heijboer H., Waisfisz Q., Weiss M.M., Groffen A.J.Eur. J. Hum. Genet. 0:0-0(2014) Salbutamol-responsive limb-girdle congenital myasthenic syndrome due to a novel missense mutation and heteroallelic deletion in MUSK.Gallenmuller C., Muller-Felber W., Dusl M., Stucka R., Guergueltcheva V., Blaschek A., von der Hagen M., Huebner A., Muller J.S., Lochmuller H., Abicht A.Neuromuscul. Disord. 24:31-35(2014) MuSK a new target for lethal fetal akinesia deformation sequence (FADS) .Wilbe M., Ekvall S., Eurenius K., Ericson K., Casar-Borota O., Klar J., Dahl N., Ameur A., Anneren G., Bondeson M.L.J. Med. Genet. 52:195-202(2015)

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.