Recombinant Human Cadherin-8 (CAD-8) Fc Chimera Protein, CF

Cadherin-8 is a member of the type II, also called atypical, subfamily of classic cadherin cell adhesion molecules. Cadherins are transmembrane calcium-dependent cell adhesion proteins. On their cytoplasmic side, they associate with the three catenins, alpha, beta and gamma (plakoglobin). This association links the cadherin protein to the cytoskeleton. Type I cadherins consist of a large extracellular domain with an N-terminal propeptide sequence that is proteolytically cleaved intracellularly, five cadherin repeats and four calcium-binding pockets between the cadherin repeats a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. Within the N-terminal cadherin domain, a conserved HAV motif involved in homophilic interaction is present. In contrast, the type II cadherins do not contain the HAV motif in the N-terminal cadherin domain and display weak or no cell adhesive properties. There also appears to be more diversity in the cytoplasmic domains of the type II cadherins as compared to the type I cadherins. Cadherin-8 is most highly expressed in neuronal tissues. The rat Cadherin-8 protein has been suggested to play a role in long-term potentiation. Human Cadherin-8 is a 799 amino acid (aa) residue protein with a putative 29 aa signal sequence, and a 32 aa propeptide, a 560 aa mature extracellular domain, a 21 aa transmembrane domain and a 157 aa cytoplasmic domain. The human, mouse and rat proteins share approximately 98% homology.