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Recombinant Human Nectin-1 His-tag Avi-tag Protein, CF

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2 μg/lane of Biotinylated Recombinant Human Nectin‑1 His-tag Avi-tag Protein (Catalog # AVI2880) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...read more
When Recombinant Human Nectin-3 Protein  (3064-N3) is immobilized at 3.0 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human Nectin‑1 His-tag Avi-tag Protein (Catalog # AVI2880) that ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Nectin-1 His-tag 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 3.0 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human Nectin‑1 His-tag Avi-tag (Catalog # AVI2880) that produces 50% of the optimal binding response is 0.10-1.00 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human Nectin-1 protein
Human Nectin-1
(Gln31-Gly346)
Accession # Q15223.3
6-His tagAvi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Gln31 inferred from enzymatic pyroglutamate treatment revealing Val32. 
Structure / Form
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
35 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
50-65 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 200 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 His-tag 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, also called poliovirus receptor-related protein-1 (PRR1), is a member of the Nectin family which are Ca++-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions. The Nectin family is comprised of 4 family members and 5 nectin-like molecules and they are structurally homologous to the poliovirus receptors (1). Mature human Nectin-1 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a single transmembrane segment, and a cytoplasmic domain that interacts with the F-actin–binding protein afadin (2). Within the ECD, human Nectin-1 shares 93% and 94% amino acid sequence identity with mouse and rat Nectin1, respectively. Two splice variants of Nectin-1 are known, one with an alternate cytoplasmic domain and a soluble form (4). 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). Nectin-1 forms homodimers in cis, followed by interactions in trans with Nectin-1, -3 or -4 (1). 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). Our Avi-tag Biotinylated 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 unchanged so there is no interference in the protein's bioactivity.
  1. Takai, Y. et al. (2008) Nat. Rev. Mol. Cell Biol. 9:603.
  2. Samanta, D. et al. (2012) PNAS 109:14836.
  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.
  15. Tampakis, A. et al. (2019) Oncology. 96:318.

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