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Recombinant Human Nectin-2/CD112 Fc Chimera Protein, CF

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When Recombinant Human Nectin‑2/CD112 Fc Chimera(Catalog # 9317-N2) is coated at 0.5 μg/mL, Recombinant HumanDNAM-1 Fc Chimera (Catalog # 666-DN) binds with an ED50 of0.04-0.2 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Nectin-2/CD112 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Nectin‑2/CD112 Fc Chimera is immobilized at 0.5 µg/mL (100 µL/well), the concentration of Recombinant Human DNAM‑1 Fc Chimera (Catalog # 666-DN) that produces 50% of the optimal binding response is 0.04-0.2 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human Nectin-2/CD112 protein
Human Nectin-2/CD112
(Gln32-Leu360)
Accession # NP_002847.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained: Gln32 predicted
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE with silver staining, under reducing conditions.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
62 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.

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 with silver staining, under reducing conditions.
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-2/CD112 Fc Chimera Protein, CF

  • CD112 antigen
  • CD112
  • Herpes virus entry mediator B
  • Herpesvirus entry mediator B
  • herpesvirus entry protein B
  • HVEB
  • HVEBpoliovirus receptor-like 2
  • MPH
  • nectin 2
  • Nectin2
  • Nectin-2
  • poliovirus receptor-related 2 (herpesvirus entry mediator B)
  • poliovirus receptor-related protein 2
  • PRR2
  • PRR2nectin-2
  • PVRL2
  • PVRR2poliovirus receptor related 2

Background

Nectins are a small family of Ca++-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions (1). They are highly homologous to the human receptor for poliovirus, and as such have been alternately named poliovirus receptor-related proteins. The 65 kDa long isoform of human Nectin-2/CD112 (Nectin-2δ) consists of a 329 amino acid (aa) extracellular region (ECD) with three immunoglobulin-like domains, a 21 aa transmembrane segment, and a 157 aa cytoplasmic domain (2). Within the ECD, human Nectin-2 shares 72% aa sequence identity with mouse Nectin-2. Alternative splicing generates a short 60 kDa isoform with a 94 aa cytoplasmic tail (2). Nectin-2 localizes to adherens junctions between neurons, endothelial cells, epithelial cells, and fibroblasts (1, 3). It forms homodimers in cis, followed by dimers in trans (between cells) (3). It does not cis-dimerize with other Nectins but forms cis-dimers between its two splice forms. Notably, a Nectin-2 cis-dimer on one cell can heterodimerize with a Nectin-3 cis-dimer on a neighboring cell (3). Nectin-2 additionally binds to DNAM-1/CD226 on NK cells and triggers NK cell cytolytic activity (4, 5). Nectin-2 is known to bind pseudorabies virus and herpes simplex virus-2 (HSV-2), but not HSV-1 or poliovirus (3, 6). Nectin-2 is a component of cardiac intercalated discs and limits fibrosis and dysfunction resulting from pressure overload (7).
  1. Samanta, D. and S.C. Almo (2015) Cell. Mol. Life Sci. 72:645.
  2. Eberle, F. et al. (1995) Gene 159:267.
  3. Struyf, F. et al. (2002) J. Virol. 76:12940.
  4. Bottino, C. et al. (2003) J. Exp. Med. 198:557.
  5. Pende, D. et al. (2005) Mol. Immunol. 42:463.
  6. Warner, M.S. et al. (1998) Virology 246:179.
  7. Satomi-Kobayashi, S. et al. (2009) Hypertension 54:825.

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