Muscle, skeletal receptor tyrosine-protein kinase (MUSK) Recombinant Protein | MUSK recombinant protein

Recombinant Human Muscle, skeletal receptor tyrosine-protein kinase (MUSK), partial

Cat. Num. AAA18672

• Gene Names: MUSK; CMS9; FADS
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Muscle; skeletal receptor tyrosine-protein kinase (MUSK); Recombinant Human Muscle; partial; Muscle-specific tyrosine-protein kinase receptor; MuSK; Muscle-specific kinase receptor; MUSK recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 24-495. Partial
• Sequence: LPKAPVITTPLETVDALVEEVATFMCAVESYPQPEISWTRNKILIKLFDTRYSIRENGQLLTILSVEDSDDGIYCCTANNGVGGAVESCGALQVKMKPKITRPPINVKIIEGLKAVLPCTTMGNPKPSVSWIKGDSPLRENSRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGTAYSKVVKLEVEEESEPEQDTKVFARILRAPESHNVTFGSFVTLHCTATGIPVPTITWIENGNAVSSGSIQESVKDRVIDSRLQLFITKPGLYTCIATNKHGEKFSTAKAAATISIAEWREYCLAVKELFCAKEWLVMEEKTHRGLYRSEMHLLSVPECSKLPSMHWDPTACARLPHLAFPPMTSSKPSVDIPNLPSSSSSSFSVSPTYSMTVIISIMSSFAIFVLLTITTLYCCRRRKQWKNKKRESAAVTLTTLPSELLLDRLHPNPMYQRMPLLLNPKLLSLEYPRNNIEYVRDI

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for MUSK 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

Product Categories/Family for MUSK recombinant protein

Signal Transduction

References

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)

NCBI and Uniprot Product Information

• NCBI GI #: 261878455
• NCBI GeneID: 4593
• NCBI Accession #: NP_001159752.1
• NCBI GenBank Nucleotide #: NM_001166280.1
• UniProt Accession #: O15146; Q32MJ8; Q32MJ9; Q5VZW7; Q5VZW8
• Molecular Weight: 53.8 kDa
• NCBI Official Full Name: muscle, skeletal receptor tyrosine-protein kinase isoform 2
• NCBI Official Synonym Full Names: muscle, skeletal, receptor tyrosine kinase
• NCBI Official Symbol: MUSK
• NCBI Official Synonym Symbols: CMS9; FADS
• NCBI Protein Information: muscle, skeletal receptor tyrosine-protein kinase
• UniProt Protein Name: Muscle, skeletal receptor tyrosine-protein kinase
• UniProt Gene Name: MUSK
• UniProt Synonym Gene Names: MuSK; Muscle-specific kinase receptor
• UniProt Entry Name: MUSK_HUMAN