>95%, by SDS-PAGE with silver staining, under reducing conditions.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Human Nectin‑2/CD112 Fc Chimera is immobilized at 0.5 µg/mL (100 µL/well), the
Human DNAM‑1 Fc Chimera (Catalog # 666-DN)
that produces 50% of the
optimal binding response is 0.04-0.2 μg/mL.
Human embryonic kidney cell, HEK293-derived human Nectin-2/CD112 protein
Human Nectin-2/CD112 (Gln32-Leu360) Accession # Q92692-2
When Recombinant Human Nectin‑2/CD112 Fc Chimera(Catalog # 9317-N2) is coated at 0.5 μg/mL, Recombinant Human DNAM-1 Fc Chimera (Catalog # 666-DN) binds with an ED50 of 0.04-0.2 μg/mL.
Nectins are a small family of Ca++-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions (1). They are highly homologous to the human receptor for poliovirus, and as such have been alternately named poliovirus receptor-related proteins. The 65 kDa long isoform of human Nectin-2/CD112 (Nectin-2δ) consists of a 329 amino acid (aa) extracellular region (ECD) with three immunoglobulin-like domains, a 21 aa transmembrane segment, and a 157 aa cytoplasmic domain (2). Within the ECD, human Nectin-2 shares 72% aa sequence identity with mouse Nectin-2. Alternative splicing generates a short 60 kDa isoform with a 94 aa cytoplasmic tail (2). Nectin-2 localizes to adherens junctions between neurons, endothelial cells, epithelial cells, and fibroblasts (1, 3). It forms homodimers in cis, followed by dimers in trans (between cells) (3). It does not cis-dimerize with other Nectins but forms cis-dimers between its two splice forms. Notably, a Nectin-2 cis-dimer on one cell can heterodimerize with a Nectin-3 cis-dimer on a neighboring cell (3). Nectin-2 additionally binds to DNAM-1/CD226 on NK cells and triggers NK cell cytolytic activity (4, 5). Nectin-2 is known to bind pseudorabies virus and herpes simplex virus-2 (HSV-2), but not HSV-1 or poliovirus (3, 6). Nectin-2 is a component of cardiac intercalated discs and limits fibrosis and dysfunction resulting from pressure overload (7).
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