Phospho-CTNND1 (pTyr228) Mouse Antibody [Clone ID: M356]

Specifications

Product Data
Clone Name	M356
Applications	ICC, WB
Recommend Dilution	WB: 1:1000 ICC: 1:100
Reactivity	Human, Rat, Mouse
Host	Mouse
Immunogen	Clone M356 was generated from a phospho-δ1-Catenin (Tyr-228) synthetic peptide containing amino acid residues around tyrosine 228 of human δ1-Catenin. This peptide sequence is highly conserved in rat and mouse δ1-Catenin.
Specificity	The antibody detects a 110 kDa* protein corresponding to the molecular mass of δ1-Catenin on SDS-PAGE immunoblots of human A431 and HUVEC cells treated with pervanadate. This antibody does not detect this band after alkaline phosphatase treatment.
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	110
Database Link	UniProt ID O60716
Background	Catenins have emerged as molecular sensors that integrate cell-cell junctions and cytoskeletal dynamics with signaling pathways that control morphogenesis and cell to cell communication. δ1-Catenin (p120 catenin) is a catenin family member which contains an N-terminal coiled-coil domain, a regulatory domain containing multiple phosphorylation sites, and a central Armadillo repeat domain. δ1-Catenin regulates E-cadherin turnover, and has both positive and negative effects on cadherin-mediated adhesion. Actin dynamics are also regulated by δ1-Catenin, which can modulate RhoA, Rac and cdc42 activity. δ1-Catenin is phosphorylated at multiple tyrosine, serine and threonine sites both in vitro and in vivo. High levels of δ1-Catenin phosphorylated at Tyr-228 are commonly seen in several carcinoma cell lines and after EGFR activation. Many other tyrosine sites are also phosphorylated in the N-terminal region including Tyr-96, Tyr-112, Tyr-280, and Tyr-302. In addition, Thr-310 and Thr-916 are constituitively phosphorylated in many cell types, however this phosphorylation may occur only in δ1-Catenin associated with the plasma membrane.
Note	Protein G purified tissue culture supernatant.
Reference Data

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