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Recombinant Human Nectin-1 Fc Chimera Avi-tag Protein, CF

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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 ...read more
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 ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Nectin-1 Fc Chimera Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Nectin-3 Protein (Catalog # 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.
Source
Human embryonic kidney cell, HEK293-derived human Nectin-1 protein
Human Nectin-1
(Gln31-Gly346)
Accession # Q15223.3
IEGRMDHuman IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Gln31 inferred from deblocking revealing Val32
Structure / Form
Disulfide-linked homodimer, biotinylated via Avi-tag
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
64 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
85-96 kDa, under reducing conditions

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Nectin-1 Fc Chimera Avi-tag Protein, CF

  • CD111 antigen
  • CD111
  • CLPED1ectodermal dysplasia 4 (Margarita Island type)
  • ED4
  • Herpes virus entry mediator C
  • Herpesvirus entry mediator C
  • Herpesvirus Ig-like receptor
  • HIgRPVRR
  • HVEC
  • HVECpoliovirus receptor-like 1
  • MGC142031
  • Nectin1
  • Nectin-1
  • OFC7nectin 1
  • poliovirus receptor-related 1 (herpesvirus entry mediator C)
  • poliovirus receptor-related protein 1
  • PRR
  • PRR1
  • PRR1MGC16207
  • PVRL1
  • PVRR1
  • PVRR1nectin-1
  • SK-12

Background

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.

  1. Lopez, M. et al. (1995) Gene 155:261.
  2. Takai, Y. et al. (2008) Nat. Rev. Mol. Cell Biol. 9:603.
  3. Fabre, S. et al. (2002) J. Biol. Chem. 277:27006.
  4. Lopez, M. et al. (2001) J. Virol. 75:5684.
  5. Cocchi, F. et al. (1998) Proc. Natl. Acad. Sci. USA 95:15700.
  6. Linehan, M. M. et al. (2004) J. Virol. 78:2530.
  7. Simpson, S. A. et al. (2005) J. Neurovirol. 11:208.
  8. Mizoguchi, A. et al. (2002) J. Cell Biol. 156:555.
  9. Togashi, H. et al. (2006) J. Cell Biol. 174:141.
  10. Tachibana, K. et al. (2000) J. Cell Biol. 150:1161.
  11. Takai, Y. and H. Nakanishi (2003) J. Cell Science 116:17.
  12. Seth, S. et al. (2007) Biochem. Biophys. Res. Commun. 364:959.
  13. Suzuki, K. et al. (2000) Nat. Genet. 25:427.
  14. Tanaka, Y. et al. (2002) Biochem. Biophys. Res. Commun. 299:472.

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