Recombinant Human Nectin-2/CD112 Fc Chimera Protein, CF 9317-N2-050: R&D Systems

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

  
  • Purity
    >95%, by SDS-PAGE with silver staining, under reducing conditions.
  • Endotoxin Level
    <0.10 EU per 1 μg of the protein by the LAL method.
  • Activity
    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
    (Gln32-Leu360)
    Accession # Q92692-2
    IEGRMD Human IgG1
    (Pro100-Lys330)
    N-terminus C-terminus
  • Accession #
  • N-terminal Sequence
    Analysis
    No results obtained: Gln32 predicted
  • Structure / Form
    Disulfide-linked homodimer
  • Predicted Molecular Mass
    62 kDa
9317-N2
 
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
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.
  • 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.
Data Images
When Recombinant Human Nectin‑2/CD112 Fc Chimera(Catalog # 9317-N2) is coated at 0.5 μg/mL, Recombinant Human
DNAM-1 Fc Chimera (Catalog # 666-DN) binds with an ED50 of
0.04-0.2 μg/mL.
Background: Nectin-2/CD112
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).
  • References:
    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.
  • Long Name:
    Poliovirus Receptor Related 2
  • Entrez Gene IDs:
    5819 (Human); 19294 (Mouse)
  • Alternate Names:
    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
Related Research Areas

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