Anti-Alpha Catenin, clone 1G5

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide. Recognizes a protein of 102kDa, identified as Catenin, alpha-1. Catenins comprise a large family of Ca2+-dependent, homotypic cell-cell adhesion molecules that play important roles in development, epithelial cell polarity and tumor progression. Alpha-Catenin is a key regulator of actin dynamics in cell-cell adhesion. During cell-cell adhesion, alpha-Catenin forms a heterodimer with beta-Catenin and links the cadherins to actin associated with the cytoskeleton. Alpha-Catenin also regulates the beta-Catenin signaling in various cells. It displays the tumor suppressor activity and is found to be down regulated in some forms of breast cancer. Protein function: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation. [The UniProt Consortium]