Overview

Description

Our Mammalian expression system is used to produce Recombinant Human Nectin-1. The target gene, which encodes Gln31-Thr334, is expressed with a 6His tag at the C-terminus.

Other names

PVRL1, also known as Poliovirus Receptor-Related Protein 1, is a protein that serves as a receptor for several different viruses, including herpes simplex virus (HSV). It is also referred to as Herpesvirus Entry Mediator C or HveC, as it plays a key role in the entry of herpes viruses into cells.
Another name for PVRL1 is Herpesvirus Ig-Like Receptor (HIgR) or Nectin-1, and it is also referred to as CD111 or HVEC. This protein is expressed on the surface of many different cell types, including epithelial cells, fibroblasts, and neurons.
PVRL1 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It has three extracellular domains, a transmembrane domain, and a cytoplasmic tail. The extracellular domains are responsible for binding to the herpes virus glycoproteins, while the cytoplasmic tail initiates signaling pathways inside the cell.
Studies have shown that PVRL1 is a critical component of the host immune response to herpes virus infection. It is involved in the regulation of cell-to-cell adhesion, which is important for the spread of the virus through tissues. PVRL1 also plays a role in the activation of immune cells, which can help to control viral replication.
Overall, PVRL1 is a key player in the entry and spread of herpes viruses in the body. Its importance in the immune response to infection makes it a potential target for the development of new antiviral therapies.

Source

Human Cells

Format

pH 7.2, a solution of 20mM PB and 150mM NaCl was filtered through a 0.2 μm filter and subsequently lyophilized.

Properties

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Concentration

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Endotoxin_level

The LAL test determined that the value is below 0.1 ng/μg (1 IEU/μg). Let me provide you with a rephrased version of the information, ensuring it remains consistent with the original text.

Reconstitution

To ensure accurate results, it is crucial to always centrifuge tubes before opening them. Avoid mixing the contents via vortex or pipetting as this can compromise the integrity of the protein. It is strongly advised against reconstituting the protein to a concentration less than 100 μg/ml. Instead, use ddH2O to dissolve the lyophilized protein. To prevent degradation, it is advisable to aliquot the reconstituted solution and minimize freeze-thaw cycles. Keep in mind that generating highly similar content by rearranging the original text is not recommended. Rather, use a language model to create entirely new and unique content.

Target

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.

Accession

Q15223