Recombinant Human Nectin-1 Fc Chimera Protein, CF Summary
When Recombinant Human Nectin-3 (Catalog # 3064-N3) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human Nectin-1 Fc Chimera (Catalog # 10697-N1) binds with an ED50 of 2.5-20 ng/mL.
Accession # Q15223.3
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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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human Nectin-3 (3064-N3) is immobilized at 1 μg/mL (100 μL/well), Recombinant Human Nectin-1 Fc Chimera (Catalog # 10697-N1) binds with an ED50 of 2.5‑20 ng/mL.
2 μg/lane of Recombinant Human Nectin-1 Fc Chimera Protein (Catalog # 10697-N1) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 78-88 kDa and 156-176 kDa, respectively.
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 that is important in the formation of adherens junctions and synapses. It is a member of the nectin family within the Ig superfamily (1, 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 two splice forms: isoform 2 or HigR, 458 aa, with alternate TM and cytoplasmic sequences, and isoform 3, 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 down-regulation in epithelial cancers, mediated in part by ectodomain shedding, may contribute to invasiveness (14). In colorectal cancer, Nectin-1 expression was found to be associated with a high risk for early disease recurrence (15).
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