Product Specifications for Recombinant Human Nectin-1 Protein, CF
Mouse myeloma cell line, NS0-derived human Nectin-1 protein Gln31-Thr334 with a C-terminal 6-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
No results obtained: Gln31 predicted
Predicted Molecular Mass
50-65 kDa, reducing conditions
Measured by its binding ability in a functional ELISA. When rhNectin-3 is coated at 1 μg/mL, rhNectin-1 binds with an apparent KD <25 nM.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
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.
What formulation is right for me?
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
Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitute at 300 μg/mL in PBS.
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.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
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).
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