Anti-δ1-Catenin (Tyr-228), Phosphospecific Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | O60716 |
Reactivity | Bovine |
Host | Mouse |
Clonality | Mouse Monoclonal |
Isotype | IgG1 |
Clone Names | M356 |
Calculated MW | 108170 Da |
Gene ID | 1500 |
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Other Names | pp120 Src substrate, p120 |
Target/Specificity | 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. |
Format | Protein A Purified |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Anti-δ1-Catenin (Tyr-228), Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Shipping | Blue Ice |
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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.
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