Human MUSK (aa 433-783, His & GST Tag) recombinant protein

Human MUSK (aa 433-783, His & GST Tag) recombinant protein

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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 (PubMed:25537362). 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 memory formation (By similarity).

Muscle, skeletal receptor tyrosine-protein kinase

MGC117677; NSK3; MDK4; MLK; NSK2; RP23-170A3.1; NSK1; MUSK; MGC126324; MGC126323; RP11-104M22.1

O15146

MUSK

Baculovirus-Insect Cells

A DNA sequence encoding the C-terminal segment of human MUSK isoform 2 (O15146-2) (Arg 433-Val 783) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Human

The recombinant human MUSK (aa 433-783)/GST chimera consists of 588 amino acids and has a calculated molecular mass of 68 kDa. It migrates as an approximately 58 kDa band in SDS-PAGE under reducing conditions.

> 90 % as determined by SDS-PAGE

Kinase activity untested