bsm-70456M

DATASHEET

Host: Mouse

Target Protein: β-Dystroglycan (Tyr-892)

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.

Modification Site: Tyr-892

Clonality: Monoclonal

Isotype: IgG1

Swiss Prot: Q14118

Source: Clone (M117) was generated from a synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 892 of human dystroglycan.

Purification: Purified by Protein A.

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

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.