Anti-α-N-Catenin antibody produced in rabbit

α-N-Catenin antibody is suitable for microarray and western blot at a dilution of 1:1,000 by using cytosolic fraction of mouse brain.

Catenins bind directly or indirectly to the conserved cytoplasmic tail domain of the cell adhesion cadherins. 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 expression of α-N-catenin is more restricted and this form predominates in the brain and is localized at synaptic junctions.

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The catenins (α, β, γ) are cytoplasmic proteins found in varying developing and adult tissues. α- N-catenin is a cadherin-binding protein, that plays a crucial role in cadherin-mediated cell-cell adhesion. It is widely expressed in the nervous system. α-Catenin (CAP102, 102 kDa), originally described as an E-cadherin associated protein, has been shown to associate with N-cadherin and P-cadherin. Within its conserved region α-catenin shows 30% identity to vinculin. There are at least two subtypes of α-catenin: α-E-catenin and α-N-catenin (102 kDa). The predominant form is α-E-catenin. Alternative spliced forms of α-N-catenin include α-N-catenin I and α-N-catenin II. The ratio of the two isoforms changes during development: isoforms II is more abundant than isoform I in early embryonic development, whereas isoform I is predominant in the adult stage.

synthetic peptide corresponding to a region located near the N-terminus of human α-N-catenin (amino acids 171-186) conjugated to KLH. This sequence is identical in mouse and chicken α-N-catenin. It is not found in α-E-catenin, β-catenin, and γ-catenin.

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