Nectin-1/CD111
Nectin-1 (CD111, PVRL1) is a calcium-independent cell adhesion molecule of the nectin family, characterized by three extracellular Ig-like domains (one V-set and two C1-set), a single transmembrane segment and a cytoplasmic tail linked to the actin cytoskeleton through afadin. Nectin-1 forms cis-homodimers and trans-homophilic interactions with nectin-1 on adjacent cells, and trans-heterophilic interactions with nectin-3 and nectin-4, establishing adherence junctions in epithelia, endothelia and neuronal synapses and coordinating cadherin-based junction formation. In the nervous system, nectin-1 is critical for synapse formation, hippocampal plasticity and memory, and optic nerve development; mutations in PVRL1 cause cleft lip/palate-ectodermal dysplasia syndrome (CLPED1, Margarita Island ectodermal dysplasia). Nectin-1 serves as the entry receptor for herpes simplex viruses 1 and 2 (glycoprotein D binding) and pseudorabies virus, and acts as an immune ligand: engagement of CD96 and TIGIT by nectin-1 contributes to NK and T-cell inhibitory signaling, linking this adhesion molecule to tumor immune evasion.
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Nectin-1/CD111 Recombinant Proteins (8)
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Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
- Formula: Human
- Molecular Weight: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
