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MUSK Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 2
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, WB, FC, E |
|---|---|
| Primary Accession | O15146 |
| Other Accession | Q62838, Q61006 |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 97056 Da |
| Antigen Region | 35-65 aa |
| Gene ID | 4593 |
|---|---|
| Other Names | Muscle, skeletal receptor tyrosine-protein kinase, Muscle-specific tyrosine-protein kinase receptor, MuSK, Muscle-specific kinase receptor, MUSK |
| Target/Specificity | This MUSK antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 35-65 amino acids from the N-terminal region of human MUSK. |
| Dilution | WB~~1:1000 IHC-P~~1:10~50 FC~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | MUSK Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MUSK |
|---|---|
| Function | 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). |
| Cellular Location | Postsynaptic cell membrane; Single-pass type I membrane protein. Note=Colocalizes with acetylcholine receptors (AChR) to the postsynaptic cell membrane of the neuromuscular junction |
Provided below are standard protocols that you may find useful for product applications.
Background
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor, generally the g phosphate of ATP, onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. With more than 500 gene products, the protein kinase family is one of the largest families of proteins in eukaryotes. The family has been classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. The tyrosine kinase (TK) group is mainly involved in the regulation of cell-cell interactions such as differentiation, adhesion, motility and death. There are currently about 90 TK genes sequenced, 58 are of receptor protein TK (e.g. EGFR, EPH, FGFR, PDGFR, TRK, and VEGFR families), and 32 of cytosolic TK (e.g. ABL, FAK, JAK, and SRC families).
References
Blume-Jensen P, et al. Nature 2001. 411: 355.
Cantrell D, J. Cell Sci. 2001. 114: 1439.
Jhiang S Oncogene 2000. 19: 5590.
Manning G, et al. Science 2002. 298: 1912.
Moller, D, et al. Am. J. Physiol. 1994. 266: C351-C359.
Robertson, S. et al. Trends Genet. 2000. 16: 368.
Robinson D, et al. Oncogene 2000. 19: 5548.
Van der Ven, P, et al. Hum. Molec. Genet. 1993. 2: 1889.
Vanhaesebroeck, B, et al. Biochem. J. 2000. 346: 561.
Van Weering D, et al. Recent Results Cancer Res. 1998. 154: 271.
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