金山科研平台，产品价格货期咨询微信：jinshanbio Source:Mouse myeloma cell line, NS0-derived, Gln32-Gly351, with a C-terminal 6-His tag Accession #:P32507 N-terminal Sequence Analysis:No results obtained: Gln32 predicted Structure:Monomer Purity:>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. Predicted Molecular Mass:35.4 kDa SDS-PAGE:45-50 kDa, reducing conditions Activity:Measured by its ability to compete with biotinylated rmNectin-2 for binding to rmDNAM-1/Fc Chimera (R&D Systems, Catalog # 4436-DN). Formulation:Lyophilized from a 0.2 µm filtered solution in PBS.See Certificate of Analysis for details. Molecule Information: Nectin-2/CD112 Long Name: Poliovirus Receptor Related 2 Aliases: CD112; HVEB; MPH; PRR2; PVRL2 Entrez Gene IDs: 5819 (Human); 19294 (Mouse) Background: Nectin-1, -2, -3 Nectins are type I transmembrane glycoproteins that are calcium-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs). Homology has led to their designation as poliovirus receptor-related (PRR) proteins, but nectins do not bind poliovirus. The extracellular domains of the nectin family form cis-homodimers (same cell), followed by homophilic or heterophilic trans-dimers (across cells) that organize intercellular junctions. Nectin-1, also known as CD111, PRR1 and herpes virus entry mediator C (HVEC) has a secreted splice variant. Nectin-1, Nectin-2 (CD112, PRR2, HVEB) and Nectin-3 (PRR3) are concentrated in adherens junctions and exist on neurons, endothelial cells, epithelial cells and fibroblasts. Nectin-4 is mainly expressed in the placenta; a soluble form is generated via the action of TACE/ADAM17.