Cell Signaling Technology

Product Pathways - Adhesion

Catenin δ-1 Antibody #4989

Applications Reactivity MW (kDa) Source
W F H M R 100 Rabbit

Applications Key:  W=Western Blotting  F=Flow Cytometry
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Catenin δ-1 Antibody detects endogenous levels of total catenin δ-1 protein.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to the sequence of human catenin δ-1. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from MDA-MB-231 and NIH/3T3 cells using Catenin δ-1 Antibody.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of NIH/3T3 cells, using Catenin δ-1 Antibody (blue) compared to a nonspecifc negative control antibody (red).

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).

  1. Reynolds, A.B. and Roczniak-Ferguson, A. (2004) Oncogene 23, 7947-7956.
  2. Davis, M. A. et al. (2003) J. Cell Biol. 163, 525-534.
  3. Thoreson, M.A. and Reynolds, A.B. (2002) Differentiation 70, 583-589.
  4. Anastasiadis, P.Z. and Reynolds, A.B. (2000) J. Cell Sci. 113, 1319-1334.

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