Recombinant Human Nectin-3 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human Nectin-3 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rhNectin-3/his at 1 µg/mL can bind rhNectin-1/his with an apparent
KD <120 nM.
Source
Mouse myeloma cell line, NS0-derived human Nectin-3 protein
Leu56-Asp400 & Gly58-Asp400, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Leu56 & Gly58
Protein/Peptide Type
Recombinant Proteins
Gene
NECTIN3
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
38.7 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
66-85 kDa, 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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human Nectin-3 Protein, CF

  • CD113 antigen
  • CD113
  • CDw113FLJ90624
  • DKFZp566B0846
  • nectin 3
  • Nectin3
  • Nectin-3
  • poliovirus receptor-related 3
  • poliovirus receptor-related protein 3
  • PPR3
  • PRR3CD113
  • PVRL3
  • PVRR3

Background

Nectins are a small family of Ca++-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions (1, 2, 3, 4). The Nectin family has at least four members (Nectin-1 - 4), all of which show alternate splicing, a transmembrane (TM) region (except for Nectin-1 gamma ), and three extracellular Ig-domains. Nectins are highly homologous to the human receptor for poliovirus, and as such, have been alternatively-named poliovirus receptor-related proteins. They do not, however, appear to bind poliovirus (1). Nectin-3 (also named PRR3, CD113 and PVRL3) is an 83 kDa, type I TM glycoprotein. Its precursor is 549 amino acids (aa) in length. It contains an extended signal sequence of 57 aa, an extracellular domain (ECD) of 347 aa, a transmembrane segment of 21 aa (aa 405 - 425), and a cytoplasmic region of 124 amino acids. The ECD shows three Ig-like domains; one N-terminal V-type and two membrane-proximal C2-type. The cytoplasmic region shows a Glu-Trp-Tyr-Val motif that binds afadin (3, 5, 6). The ECD of human Nectin-3 is 94% aa identical to mouse Nectin-3 ECD (5, 6). Nectin-3 has a diverse expression pattern. It has been found in junctions between small intestinal columnar epithelial cells (6), pigmented and nonpigmented epithelium in the ciliary body (7), spermatids and Sertoli cells in the seminiferous tubules (8), and on spinal cord motor neurons and axons, plus Schwann cells of the peripheral nervous system (9). As with mouse, human Nectin-3 has three potential isoforms. It does not appear that they are strict orthologs. In addition to the full length isoform, a second human isoform has a 31 aa substitution for the first 54 aa of the signal sequence, followed by a deletion of aa 291 - 549 (10). The third human isoform shows a 10 aa substitution for aa 357 - 549 (11). Nectin-3 is proposed to promote cell adhesion by initiating cell-to-cell adhesion, allowing for subsequent JAM and cadherin-based intercellular junction formation. It does so by first forming same cell (cis-) heterodimers with alpha v beta 3 and PDGFR (an anti-apoptotic interaction) (2, 4). This results in actin reorganization and recruitment of adherens and occludins adhesion molecules. Subsequent Nectin-3 activity adds strength to the junction through trans-interactions with a variety of molecules, including Nectin-3 itself, as well as Nectins-1 and 2 plus Necl-1, 2 and 5 (3, 4).

  1. Takai, Y. and H. Nakanishi (2003) J. Cell Sci. 116:17.
  2. Miyoshi, J. and Y. Takai (2007) Am. J. Nephrol. 27:590.
  3. Sakisaka, T. et al. (2007) Curr. Opin. Cell Biol. 19:593.
  4. Rikitake, Y. and Y. Takai (2008) Cell. Mol. Life Sci. 65:253.
  5. Reymand, N. et al. (2000) Gene 255:347.
  6. Satoh-Horikawa, K. et al. (2000) J. Biol. Chem. 275:10291.
  7. Inagaki, M. et al. (2005) Development 132:1525.
  8. Inagaki, M. et al. (2006) Genes Cells 11:1125.
  9. Zelano, J. et al. (2006) Exp. Neurol. 201:461.
  10. GenBank Accession # BAC11414.
  11. SwissProt # Q9NQS3.

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Bioinformatics

Gene Symbol NECTIN3
Uniprot