protein

Recombinant Human Muscle, skeletal receptor tyrosine-protein kinase

MBS1204143

0.05 mg (Yeast)

190 USD

Recombinant Protein

Recombinant Human Muscle, skeletal receptor tyrosine-protein kinase

Muscle, skeletal receptor tyrosine-protein kinase

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

muscle, skeletal receptor tyrosine-protein kinase isoform 2; Muscle, skeletal receptor tyrosine-protein kinase; muscle, skeletal receptor tyrosine-protein kinase; muscle, skeletal, receptor tyrosine kinase; Muscle-specific tyrosine-protein kinase receptor; MuSK; Muscle-specific kinase receptor

MUSK

MUSK; MUSK; CMS9; FADS; MuSK; Muscle-specific kinase receptor

MUSK_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

24-495; Provide the complete extracellular domain.

495

LPKAPVITTPLETVDALVEEVATFMCAVESYPQPEISWT
RNKILIKLFDTRYSIRENGQLLTILSVEDSDDGIYCCTA
NNGVGGAVESCGALQVKMKPKITRPPINVKIIEGLKAVL
PCTTMGNPKPSVSWIKGDSPLRENSRIAVLESGSLRIHN
VQKEDAGQYRCVAKNSLGTAYSKVVKLEVEEESEPEQDT
KVFARILRAPESHNVTFGSFVTLHCTATGIPVPTITWIE
NGNAVSSGSIQESVKDRVIDSRLQLFITKPGLYTCIATN
KHGEKFSTAKAAATISIAEWREYCLAVKELFCAKEWLVM
EEKTHRGLYRSEMHLLSVPECSKLPSMHWDPTACARLPH
LAFPPMTSSKPSVDIPNLPSSSSSSFSVSPTYSMTVIIS
IMSSFAIFVLLTITTLYCCRRRKQWKNKKRESAAVTLTT
LPSELLLDRLHPNPMYQRMPLLLNPKLLSLEYPRNNIEY
VRDI

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

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

Signal Transduction

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

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)

261878455

NP_001159752.1

NM_001166280.1

O15146

79.9kD

ECM Proteoglycans Pathway (1270256); Extracellular Matrix Organization Pathway (1270244)

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

0.05 mg (Yeast)

190 USD

0.05 mg (E-Coli)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750