1. Measured by its binding ability in a functional ELISA. Immobilized PVRL3 at 1 μg/ml (100 μl/well) can bind biotinylated recombinant human PVRL1 / Nectin-1 with a linear range of 6.4-800 ng/ml. 2. Immobilized Nectin 3 Protein, Human, Recombinant (ECD, hFc Tag) at 2 μg/ml (100 μl/well) can bind PVRL1/NECTIN1 Protein, Human, Recombinant (His Tag), the EC50 of PVRL1/NECTIN1 Protein, Human, Recombinant (His Tag)is 150-700 ng/mL.

PVRL1/NECTIN1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 35.4 kDa and the accession number is Q15223-1.

Human

HEK293 Cells

SK-12,PVRR1,PVRR,PRR1,PRR,poliovirus receptor-related 1 (herpesvirus entry mediator C),OFC7,nectin-1,HVEC,HV1S,HIgR,ED4,CLPED1,CD111

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. Predicted N terminal: Gln 31

> 98 % as determined by SDS-PAGE

A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.

It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

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.