Recombinant Human Nectin-1 Fc Chimera Avi-tag Protein, CF
Recombinant Human Nectin-1 Fc Chimera Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
| Human Nectin-1 (Gln31-Gly346) Accession # Q15223.3 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag |
| N-terminus | C-terminus | ||
Analysis
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.
AVI10697
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| 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.
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Scientific Data
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When Recombinant Human Nectin-3 Protein (3064-N3) is immobilized at 0.5 μg/mL, 100 μL/well, the concentration of Biotinylated Recombinant Human Nectin‑1 Fc Chimera Avi-tag (Catalog # AVI10697) that produces 50% of the optimal binding response is approximately 6.0-40 ng/mL.
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2 μg/lane of Biotinylated Human Nectin-1 Fc Chimera Avi-tag (Catalog # AVI10697) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 85-96 kDa and 160-190 kDa.
Reconstitution Calculator
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 down-regulation in epithelial cancers, mediated in part by ectodomain shedding, may contribute to invasiveness (14). Our Avi-tag Biotinylated Human Nectin-1 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is uncharged so there is no interference in the protein's bioactivity.
- Lopez, M. et al. (1995) Gene 155:261.
- Takai, Y. et al. (2008) Nat. Rev. Mol. Cell Biol. 9:603.
- Fabre, S. et al. (2002) J. Biol. Chem. 277:27006.
- Lopez, M. et al. (2001) J. Virol. 75:5684.
- Cocchi, F. et al. (1998) Proc. Natl. Acad. Sci. USA 95:15700.
- Linehan, M. M. et al. (2004) J. Virol. 78:2530.
- Simpson, S. A. et al. (2005) J. Neurovirol. 11:208.
- Mizoguchi, A. et al. (2002) J. Cell Biol. 156:555.
- Togashi, H. et al. (2006) J. Cell Biol. 174:141.
- Tachibana, K. et al. (2000) J. Cell Biol. 150:1161.
- Takai, Y. and H. Nakanishi (2003) J. Cell Science 116:17.
- Seth, S. et al. (2007) Biochem. Biophys. Res. Commun. 364:959.
- Suzuki, K. et al. (2000) Nat. Genet. 25:427.
- Tanaka, Y. et al. (2002) Biochem. Biophys. Res. Commun. 299:472.
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