Recombinant Human P-Cadherin Fc Chimera Avi-tag Protein, CF

Placental (P) - Cadherin (PCAD) is a member of the Cadherin family of cell adhesion molecules. Cadherins are calcium-dependent transmembrane proteins, which bind to one another in a homophilic manner. On their cytoplasmic side, they associate with the three catenins, alpha, beta, and gamma (plakoglobin). This association links the cadherin protein to the cytoskeleton. Without association with the catenins, the cadherins are non-adhesive. Cadherins play a role in development, specifically in tissue formation. They may also help to maintain tissue architecture in the adult. P-Cadherin is a classical cadherin molecule. Classical cadherins consist of a large extracellular domain which contains DXD and DXNDN repeats responsible for mediating calcium-dependent adhesion, a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. Human P-Cadherin is an 829 amino acid (aa) protein with a 26 aa signal sequence and an 803 aa propeptide. The mature protein begins at aa 108 and has a 548 aa extracellular region, a 23 aa transmembrane region, and a 151 aa cytoplasmic region. The human and mouse mature PCAD proteins share 87% homology. Our Avi-tag Biotinylated human P-Cadherin Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.