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PA1-1741 detects a predominant band at ~98kD. Other lower MW nonspecific bands of unknown identity were also detected and are likely to be proteolytic fragments.
MUSK plays an important and selective role in many aspects of skeletal muscle development and function through the initial step of postsynaptic differentiation and formation of end-plate bands in cooperation with Rapsyn. Communication between cells is often mediated by receptors on the surface of the target cell that are triggered by specific ligands released by other cells. Receptor tyrosine kinase activity is strictly regulated by the binding of the appropriate ligand to the extracellular active site of the receptor. MuSK has been shown to be part of the agrin signaling complex and plays an important role in the development and architectural maintenance of the neuromuscular junction.
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Protein Aliases: MGC126323; MGC126324; muscle localized kinase 2; muscle specific kinase (neural fold/somite kinase 1); Muscle, skeletal receptor tyrosine protein kinase; Muscle, skeletal receptor tyrosine-protein kinase; muscle, skeletal, receptor tyrosine kinase; muscle-specific kinase receptor; muscle-specific protein kinase secretory isoform; muscle-specific tyrosine kinase receptor MuSK; Muscle-specific tyrosine protein kinase receptor; Muscle-specific tyrosine-protein kinase receptor; MuSK; RP23-170A3.1
Gene Aliases: CMS9; FADS; Mdk4; Mlk; MUSK; Nsk1; Nsk2; Nsk3
UniProt ID: (Human) O15146, (Mouse) Q61006, (Rat) Q62838
Entrez Gene ID: (Human) 4593, (Mouse) 18198, (Rat) 81725
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