Phospho-DAG1 (pTyr892) Mouse Antibody [Clone ID: M117]

Specifications

Product Data
Clone Name	M117
Applications	WB
Recommend Dilution	WB: 1:1000
Reactivity	Human, Rat, Mouse
Host	Mouse
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.
Formulation	PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Concentration	lot specific
Purification	Protein A Purified
Conjugation	Unconjugated
Storage Condition	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.
Predicted Protein Size	43
Database Link	UniProt ID Q14118
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.
Note	Protein G purified tissue culture supernatant.
Reference Data

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