| Overview |
| bsm-70456m |
| _-Dystroglycan (Tyr-892), Phosphospecific Antibody |
| WB |
| 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. |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Mouse |
| Clone (M117) was generated from a synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 892 of human dystroglycan. |
| Tyr-892 |
| Monoclonal |
| M117 |
| IgG1 |
| Purified by Protein A. |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C. |
| Target |
| Q14118 |
| 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 _-dystroglycan and a 43 kDa transmembrane protein, _-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 _-Dystroglycan, as well as inhibit interactions with WW domain proteins. In skeletal muscle, _-Dystroglycan is normally localized to the plasma membrane, however phosphorylation of Tyr-892 leads to localization of _-Dystroglycan to endosomal compartments along with c-Src. Thus, phosphorylation at Tyr-892 may have important roles in altering the localization of _-Dystroglycan during NMJ formation. |
| Application Dilution |
| WB |
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