Anti-β-Dystroglycan (Tyr-892), Phosphospecific Antibody

Dystroglycans are essential elements of the neuromuscular junction (NMJ) . The gene for dystroglycan is expressed as a precursor protein that is post-translationally cleaved into a 156 kDa extracellular peripheral membrane protein called α-dystroglycan and a 43 kDa transmembrane protein, β-Dystroglycan. The latter protein contains a PPxY motif that promotes binding to WW domain-containing proteins, such as utrophin and dystrophin. Phosphorylation at tyrosine 892 within the PPxY motif may regulate c-Src interactions with β-Dystroglycan, as well as inhibit interactions with WW domain proteins. In skeletal muscle, β-Dystroglycan is normally localized to the plasma membrane, however phosphorylation of Tyr-892 leads to localization of β-Dystroglycan to endosomal compartments along with c-Src. Thus, phosphorylation at Tyr-892 may have important roles in altering the localization of β-Dystroglycan during NMJ formation.

Our β-Dystroglycan (Tyr-892) mouse monoclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat β-Dystroglycan (Tyr-892) and is Protein A purified. It is great for use in WB.

Clone (M117) was generated from a synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 892 of human dystroglycan. This peptide sequence has high homology to the conserved tyrosine site in rat and mouse dystroglycan.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.