Beta-Dystroglycan (Tyr-892), phospho-specific (clone M117), anti-human, mouse, rat

Background:
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.

Immunogen: 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.

Specificity: The antibody detects a 43 kDa* protein on SDS-PAGE immunoblots of human HepG2 or HeLa cells treated with pervanadate, but not in control cells.

Buffer/Storage:
Mouse monoclonal antibody purified with protein A chromatography is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.