Recombinant Human Nectin-1 Protein, CF

Recombinant Human Nectin-1 Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Nectin-1

Nectin-1 (designated CD111), also called PRR-1 (poliovirus receptor-related protein 1) or HVEC (herpesvirus entry mediator C), is a widely expressed 110 kDa type I transmembrane glycoprotein important in formation of adherens junctions and synapses. It is a member of the nectin family within the Ig superfamily (1, 2). The Latin word necto means “to connect”, indicating the role of nectins in Ca²⁺-independent cell-cell adhesion (2). Nectin-1 forms homodimers in cis, followed by interactions in trans with Nectin-1, -3 or -4 (2). The 517 amino acid (aa) human Nectin-1 isoform 1 contains a 30 aa signal sequence, a 325 aa extracellular domain (ECD), a 21 aa transmembrane segment (TM), and a 141 aa cytoplasmic region. Nectin ECDs contain three Ig-like domains: an N-terminal V-type that mediates ligand binding, and two C2-type (3). Nectin-1, like other nectins, has a splice form (isoform 2 or HigR, 458 aa) with alternate TM and cytoplasmic sequences. Another, isoform 3, is a 352 aa secreted protein (4). The common region of mature human Nectin-1 (aa 31 - 334) shares 93%, 94%, 96% and 96% aa identity with mouse, rat, bovine and porcine Nectin-1, respectively. Nectin-1 binds viral glycoprotein D to mediate herpesvirus (but not poxvirus) entry into vaginal mucosa, sensory neurons and fibroblasts (4 - 7). In forming adherens junctions and synapses, nectins 1 and 3 initiate cell-cell interactions, recruiting alpha _v beta ₃ integrin extracellularly and cadherins intracellularly through afadin and other junctional proteins (2, 8 - 11). These interactions organize the cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections. Nectin-1 also recognizes CD96 on NK cells (12). Deficiency of Nectin-1 can result in cleft lip/palate ectodermal dysplasia (13). Nectin-1 downregulation in epithelial cancers, mediated in part by ectodomain shedding, may contribute to invasiveness (14).

Related Research Areas

• Cell to Cell Adhesion Disassembly During EMT
• Epithelial Cell Markers and Intracellular Molecules
• Epithelial Cell Polarity
• Immunoglobulin Superfamily CAMs
• Infectious Diseases
• Nectin and Nectin-like Binding Receptors and Ligands
• Nectins
• Search Immune Checkpoint Targets
• Surface Ectodermal Cells
• Synaptic Adhesion Molecules