Recombinant Human Cadherin-20 (CAD-20) Protein, CF

Cadherin-20 is an 82 kDa (predicted) type II classical cadherin from the cadherin superfamily and one of three Cadherin 7-like genes located in a cluster on chromosome 18 (1, 4). Cadherins are calcium-dependent intercellular glycoproteins containing five extracellular cadherin repeats of about 110 amino acids (aa) with typical conserved sequences (1 - 2). The extracellular cadherin domains bind Ca²⁺ in order for correct protein folding and normal functioning to take place (1). Human Cadherin-20 is synthesized as a precursor that contains a 34 aa signal sequence, a 25 aa propeptide, a 560 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 161 aa cytoplasmic region (SwissProt # Q9HBT6). The ECD contains five cadherin domains, two calcium-binding sites, and four potential sites for N-linked glycosylation. Mature human Caderin-20 is 98% and 97% aa identical to mature mouse and rat Cadherin-20, respectively. Cadherin-20 is expressed in placenta, adult brain, and fetal brain (1). In mice, during embryogenesis, Cadherin-20 was found to be synthesized by the forebrain, anterior neural ridge, developing visual system, primitive external granular layer of the cerebellum and a subset of neural crest cells likely to develop into melanoblasts (3). Cadherin-20 is a cell adhesion protein that preferentially interacts with itself in a homophilic manner in connecting cells (1). It thus may contribute to the sorting of heterogeneous cell types (3). In addition, since disturbance of cellular adhesion is a prerequisite for invasion and metastasis of tumor cells, cadherins are considered prime candidates for tumor suppressor genes (1).