Recombinant Human Cadherin-12 (CAD-12) Fc Chimera, CF

The cadherin superfamily is a large family of membrane-associated glycoproteins that engage in homotypic, calcium-dependent, cell-cell adhesion events. The superfamily can be divided into at least four subfamilies based on its member’s extracellular (EC) regions and cytoplasmic domains (1, 2). These include classical cadherins, desmosomal cadherins, protocadherins, and cadherin-like molecules that contain a variable number of EC and transmembrane (TM) domains (1). Cadherin-12, also known as brain‑cadherin and N-cadherin 2, is a 150 kDa classical cadherin. Classical family molecules are modular in their extracellular region, mediating calcium‑dependent cell-cell adhesion through their five EC Ca⁺⁺-binding repeats (2). Cadherin-12 can be further identified as a type II classical cadherin, due to the absence of a His-Ala-Val motif in its most N-terminal cadherin repeat (3). Human Cadherin-12 is synthesized as a 794 amino acid (aa) type I transmembrane preproprotein that contains a 23 aa signal peptide, a 31 aa prosequence, a 555 aa extracellular region, a 28 aa transmembrane segment, and a 157 aa cytoplasmic domain (4, 5). The five EC cadherin domains are approximately 110 aa in length and generate two beta -sheets that are oriented like bread in a sandwich. Human Cadherin‑12 EC region is 96% aa identical to mouse Cadherin-12 EC region. Cadherin-12 is expressed specifically in CNS neurons. The bulk of its expression is postnatal, and it is proposed to be involved in synaptogenesis (4). As a classic cadherin, Cadherin-12 will form homodimers and promote intercellular adhesion with itself and, possibly, cadherins-8 and -14 (6).