Phospho-Catenin δ-1 (Tyr228) Antibody #2911
- WB
- IF
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 95, 100 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunofluorescence (Immunocytochemistry) | 1:100 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Catenin δ-1 (Tyr228) Antibody detects endogenous levels of catenin δ-1 protein only when phosphorylated at Tyr228. The antibody might cross react with another overexpressed phospho-tyrosine protein.
Species Reactivity:
Human
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Tyr228 of human/mouse catenin δ-1. Antibodies are purified by peptide affinity chromatography.
Background
Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).
Catenin δ-1 is phosphorylated at multiple tyrosine sites along its sequence both in vivo and in vitro (5). High levels of catenin δ-1 phosphorylated at Tyr228 are commonly seen in several carcinoma cell lines. EGFR signaling induces catenin δ-1 phosphorylation at Tyr228, with the phosphorylated protein becoming localized at adherens junctions although phosphorylation is not essential in junction formation (6).
- Reynolds, A.B. and Roczniak-Ferguson, A. (2004) Oncogene 23, 7947-7956.
- Davis, M. A. et al. (2003) J. Cell Biol. 163, 525-534.
- Thoreson, M.A. and Reynolds, A.B. (2002) Differentiation 70, 583-589.
- Anastasiadis, P.Z. and Reynolds, A.B. (2000) J. Cell Sci. 113, 1319-1334.
- Mariner, D.J. et al. (2001) J. Biol. Chem. 276, 28006-28013.
- Mariner, D.J. et al. (2004) J. Cell Sci. 117, 1339-1350.
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