Recombinant Human Nectin-1 (C-6His)

Description

EnkiLife provides the Recombinant Human Nectin-1 (C-6His) protein,aslo know as Poliovirus Receptor-Related Protein 1,Herpes Virus Entry Mediator C,Herpesvirus Entry Mediator C,HveC,Herpesvirus Ig-Like Receptor,HIgR,Nectin-1,CD111,PVRL1,HVEC,PRR1, which features high purity, high activity, and high stability. It can be applied in scientific research, biopharmaceuticals, and other fields.Purity:Greater than 95% as determined by reducing SDS-PAGE;Endotoxin Level:<1 EU/µg as determined by LAL test.;Construction:Recombinant Human Poliovirus Receptor-Related Protein 1 is produced by our Mammalian expression system and the target gene encoding Gln31-Thr334 is expressed with a 6His tag at the C-terminus.Accession:Q15223. Expression Host:Human Cells.Species:Human.Predicted Molecular Mass:34.99 KDa. Background:Nectin-1 is a type I transmembrane glycoprotein belonging to the Ig superfamily. Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between Nectin-1 and Nectin-3 and between Nectin-1 and Nectin-4. Nectin ECDs contain three Ig like domains: an N terminal V type that mediates ligand binding, and two C2 type. Nectin-1 binds viral Glycoprotein D to mediate Herpesvirus (but not Poxvirus) entry into vaginal mucosa, sensory neurons and fibroblasts. In forming adherens junctions and synapses, Nectin-1 and Nectin-3 initiate cell-cell interactions, recruiting αvβ3 integrin extracellularly and cadherins intracellularly through afadin and other junctional proteins. These interactions organize the cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections. Nectin-1 and Nectin-3 have been found to localize assymetrically along the chemical synapse, with Nectin-1 primarily on the axonal side and Nectin-3 on the dendritic side. Deficiency of Nectin-1 can result in cleft lip/palate ectodermal dysplasia. Nectin-1 downregulation in epithelial cancers is mediated in part by ectodomain shedding, but it may contribute to invasiveness.