Muscle, Skeletal Receptor Tyrosine-Protein Kinase (MUSK) Human Recombinant Protein

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)

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.

MBS1204143 is a recombinant protein targeting MUSK. Also known as Recombinant Human Muscle, skeletal receptor tyrosine-protein kinase (MUSK), partial. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.