Immunofluorescent analysis of muscle-specific kinase (MuSK) (green) in C2C12 mouse myoblast cells. The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.1% Triton X-100 in TBS for 10 minutes, and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were stained without (left panel) or with a MuSK polyclonal antibody (Product # PA1-1741, right panel), at a dilution of 1:20 in blocking buffer for at least 1 hour at room temperature, and then incubated with a DyLight 488 goat anti-rabbit IgG secondary antibody (Product # 35552) for 45 minutes at room temperature (green). F-Actin (both panels, red) was stained with DyLight 554 Phalloidin (Product # 21834) and nuclei (both panels, blue) were stained with DAPI. Images were taken at 60X magnification.
|Tested species reactivity||Human, Mouse, Rat|
|Published species reactivity||Rat, Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Recombinant protein containing residues 210-304 from the extracellular domain of rat MuSK|
|Storage buffer||PBS with 1mg/ml BSA, 30% glycerol|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1:20-1:100|
|Immunoprecipitation (IP)||Assay dependent|
|Western Blot (WB)||1:500-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
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.
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. These types of receptors play a role critical in the growth and differentiation of different cell types.
A muscle specific kinase recently identified, termed MuSK for muscle-specific kinase, and has been shown to be specifically expressed in the muscle cells within the neuromuscular junction. 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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
The Agrin/MuSK signaling pathway is spatially segregated from the neuregulin/ErbB receptor signaling pathway at the neuromuscular junction.
PA1-1741 was used in immunohistochemistry to investigate the distribution of protein components of the neuregulin/erbB receptor and agrin/MuSK pathways at NMJs of adult rat gastrocnemius muscle
|Trinidad JC,Fischbach GD,Cohen JB||The Journal of neuroscience : the official journal of the Society for Neuroscience (20:8762)||2000|
Dimerization of the muscle-specific kinase induces tyrosine phosphorylation of acetylcholine receptors and their aggregation on the surface of myotubes.
PA1-1741 was used in western blot to investigate the effect of MuSK dimerization on acetylcholine receptor's tyrosine phosphorylation and aggregation
|Hopf C,Hoch W||The Journal of biological chemistry (273:6467)||1998|
Laminin and alpha-dystroglycan mediate acetylcholine receptor aggregation via a MuSK-independent pathway.
PA1-1741 was used in immunoprecipitation to investigate the regulation of AChR aggregation by laminin and alpha-dystroglycan
|Montanaro F,Gee SH,Jacobson C,Lindenbaum MH,Froehner SC,Carbonetto S||The Journal of neuroscience : the official journal of the Society for Neuroscience (18:1250)||1998|