Human NECL5/CD155/PVR Protein, ECD (Extracellular Domain), Fc-fusion, Recombinant

Description :
NECL5 (Nectin-like protein 5), also known as PVR (poliovirus receptor) and CD155, is a single pass type I transmembrane glycoprotein that belongs to the Nectin family of the Ig (immunoglobulin) superfamily. Most Nectin family members function as cell adhesion molecules (CAMs) located on the cell surface and involved with the binding with other cells or with the extracellular matrix (ECM). Like other Nectin members, NECL5 contains 1 Ig-like V-type domain and 2 Ig-like C2-type domains in the extracellular region that interacts either with other CAMs of the same kind (homophilic binding) or with other CAMs or the extracellular matrix (heterophilic binding) in a Ca2+-independent manner. NECL5 is predominately expressed in enterocytes and gastrointestinal lymphatic tissues. It was originally identified by the ability to mediate the cell attachment and entry of poliovirus (PV), an etiologic agent of the central nervous system disease poliomyelitis. The normal cellular function of NECL5 maybe the involvement of intercellular adhension between epithelial, endothelial, and immune cells. NECL5 interact with CD226 and CD96, which promote the adhension, migration and NK-cell killing, and thus efficiently prime cell-mediated tumor-specific immunity. Enhanced NECL5 expression in tumor cells contributes to loss of contact inhibition and increased migration. It also allows tumor cell recognition and killing by CD226­ or CD96­expressing NK cells. NECL5 also binds the inhibitory ligand TIGIT (T-cell immunoreceptor with Ig and ITIM domains) on NK and some mature T cells, antagonizing CD226 effects.