General description

α-E-Catenin is a predominant subtype of α-catenin. It is widely expressed but at low levels in the nervous system. Alternative spliced variants of α-E-Catenin include α1- and α2-E-catenin.

The catenins (α, β, γ) are cytoplasmic proteins found in varying abundance in many developing and adult tissues.

Immunogen

synthetic peptide corresponding to a region located near the C-terminus of human α-E-catenin (amino acids 873-887). This sequence is identical in mouse and Xenopus α-E-catenin. It is not found in α-N-catenin, β-catenin, and γ-catenin.

Application

Anti-α-E-Catenin antibody produced in rabbit has been used in western blotting and immunocytochemistry.

Biochem/physiol Actions

Catenins bind directly or indirectly to the conserved cytoplasmic tail domain of the cell adhesion adherins. The association of catenins to cadherins produces a complex, which is linked to the actin filament network. Catenins/cadherin complexes play an important role in mediating cell adhesion, transduction of cell-cell contact positional signals to the cell interior, and may play a crucial role in cell differentiation. The linkage of the epithelial cadherin /uvomorulin to actin is essential for the cell binding function of this cadherin. α-Catenin (CAP102, 102 kDa), originally described as an E-cadherin associated protein, has been shown to associate with other members of the cadherin family members, N-cadherin and P-cadherin. Within its conserved region α-catenin shows 30% identity to vinculin.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

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