This purified rabbit anti-β-catenin polyclonal antibody is specific to human, mouse, rat, chicken and Xenopus β-catenin. Anti-β-catenin recognizes the expressed product of the CTNNB1 gene, also known as Ctnnb1. β-catenin is a 92 kDa protein which shares 70% amino acid identity with both plakoglobin (γ-catenin) and the product of the Drosophila segment polarity gene armadillo. This rabbit anti-β-catenin polyclonal antibody is validated for use in western Blotting, immunoassay (ELISA), immunocytochemistry, immunofluorescence, and immunoprecipitation.

Antibody Specifications:

• Applications: Validated applications for rabbit anti-β-catenin polyclonal antibody are western blotting, immunoassay (ELISA), immunocytochemistry, immunofluorescence, and immunoprecipitation.
• Host Species: The host species of anti-β-catenin polyclonal antibody is rabbit.
• Reactivity: Reacts with Human, chicken, mouse, rat and Xenopus β-catenin.
• Product Size: Rabbit anti-β-catenin polyclonal antibody is available in a 100 µg size.

Adherens junctions (AJ) (also referred to as zonula adherens) are required for both the establishment and maintenance of epithelial layers. In addition, these junctions have been identified in several other cell types including cardiac myocytes and fibroblasts. AJ subserve several important functions including: mediating intercellular adhesion, sensing the presence of neighboring cells, and anchoring the actin cytoskeleton. AJ are multiprotein complexes that are assembled around cell adhesion molecules called cadherins. Cadherins are a multifunctional family of Ca2+-dependent, transmembrane, glycoproteins which promote cell-cell adhesion. The cadherin extracellular domain mediates homophilic interactions between like cadherin molecules on neighboring cells, while the intracellular domain interacts with several cytoplasmic proteins which include: α-catenin, β-catenin, γ-catenin (plakoglobin), and the tyrosine kinase substrate p120cas. Cadherin-catenin interactions are required for complete cadherin activity and regulate the interaction between cadherins and the actin-based cytoskeleton. In fact, deletion of the cadherin cytoplasmic domain produces an adhesion-defective molecule that is unable to interact with the cytoskeleton. β-catenin is a 92 kDa protein which shares 70% amino acid identity with both plakoglobin (γ-catenin) and the product of the Drosophila segment polarity gene armadillo. The Armadillo protein is part of a multiprotein junctional complex and is a required component of the Drosophilia wingless (vertebrate Wnt-1) signal transduction pathway. β-catenin, plakoglobin (γ-catenin), and p120cas are homologous but distinct proteins which contain between 10-13 copies of a 42-44 amino acid motif first identified in the Armadillo protein and referred to as armadillo repeats. These armadillo repeats mediate the interaction between β and γ-catenin and the cadherin cytoplasmic domain. In addition they mediate β-catenin’s interaction with the tumor suppressor protein APC (Adenomatous Polyposis Coli). Interestingly, the interaction between APC and β-catenin has been speculated to "regulate the transmission of the contact inhibition signal to the cell". Taken together these findings suggest that β-catenin likely plays a central role in signal transduction pathways regulated by cell-cell adhesion.