Recombinant Cynomolgus Monkey Nectin-2/CD112 His Protein, CF

Nectins are a small family of Ca⁺⁺-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions (1). The nectin family has at least four members (nectin-1-4), all of which show alternate splicing (except for Nectin-4), a transmembrane (TM) region (except for Nectin-1 gamma), and three extracellular Ig-domains. Nectins are highly homologous to the human receptor for poliovirus, and as such have been alternately named poliovirus receptor-related proteins. They do not, however, appear to bind poliovirus (1). Nectin-2 is a type I TM glycoprotein that is found on a variety of cell types (2, 3). Cynomolgus Nectin-2 is synthesized as a 538 amino acid precursor. It contains a 31 amino acid (aa) signal sequence, a 329 aa extracellular domain (ECD), a 22 aa TM segment, and a 156 aa cytoplasmic domain. The ECD contains one N-terminal V-type Ig domain and two C2-type Ig domains. The V-domain is believed to mediate nectin binding to its ligands (4).  The ECD of cynomolgus Nectin-2 shows 96% aa sequence identity with the ECD of human Nectin-2. Nectin-2 is known to bind the pseudorabies virus, and herpes simplex virus-2 (HSV-2), but not HSV-1. It does not bind poliovirus. As a cell adhesion molecule, Nectin-2 will form cis-homodimers (same cell), followed by trans-dimers (across cells). Nectin-2 will not cis-dimerize with other nectins, but will cis-dimerize with its two splice forms. Notably, a Nectin-2 cis-dimer on one cell will heterodimerize with a Nectin-3 cis-dimer on another cell (1). Nectin-2 is found concentrated in adherens junctions, and exists on neurons, endothelial cells, epithelial cells and fibroblasts.