Description
Recombinant Human CD111/Nectin-1 Protein (His Tag)(Active) | PKSH031065 | Gentaur US, UK & Europe Disrtribition
Synonyms: 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;ED4;HIgR;HV1S;HVEC;nectin-1;OFC7;PRR;PVRR;PVRR1;SK-12
Active Protein: Active protein
Activity: A DNA sequence encoding the human PVRL1 isoform 1 (NP_002846.3) extracellular domain (Met 1-Thr 334) was expressed, with a polyhistidine tag at the C-terminus.
Protein Construction: A DNA sequence encoding the human PVRL1 isoform 1 (NP_002846.3) extracellular domain (Met 1-Thr 334) was expressed, with a polyhistidine tag at the C-terminus.
Fusion Tag: C-His
Species: Human
Expressed Host: HEK293 Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 98 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 35.4 kDa
Formulation: Lyophilized from sterile PBS, pH 7.4
Reconstitution: Please refer to the printed manual for detailed information.
Background: Poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin-1; CD111), also known as PVRL1 is a cell adhesion molecule belonging to the immunoglobulin superfamily that can bind to virion glycoprotein D (gD) to mediate entry of herpes simplex viruses (HSV) and pseudorabies virus (PRV). CD111/Nectin-1/PVRL1 colocalizes with E-cadherin at adherens junctions in epithelial cells. The disruption of cell junctions can result in the redistribution of nectin-1. To determine whether disruption of junctions by calcium depletion influenced the susceptibility of epithelial cells to viral entry, Madin-Darby canine kidney cells expressing endogenous nectin-1 or transfected human nectin-1 were tested for the ability to bind soluble forms of viral gD and to be infected by HSV and PRV, before and after calcium depletion. It has been revealed that binding of HSV and PRV gD was localized to adherens junctions in cells maintained in normal medium but was distributed, along with nectin-1, over the entire cell surface after calcium depletion. Both the binding of gD and the fraction of cells that could be infected by HSV-1 and PRV were enhanced by calcium depletion. Taken together, CD111/Nectin-1/PVRL1 confined to adherens junctions in epithelial cells is not very accessible to virus, whereas dissociation of cell junctions releases nectin-1 to serve more efficiently as an entry recptor.
Research Area: Microbiology, Neuroscience
