Mouse Nectin-2/CD112 APC-conjugated Antibody

  • Species Reactivity
  • Specificity
    Detects mouse Nectin-2/CD112 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human Nectin-2/CD112 or recombinant mouse CD155/PVR is observed.
  • Source
    Monoclonal Rat IgG2A Clone # 829038
  • Purification
    Protein A or G purified from hybridoma culture supernatant
  • Immunogen
    Mouse myeloma cell line NS0-derived recombinant mouse Nectin-2/CD112
    Gln32-Gly351 (predicted)
    Accession # P32507
  • Formulation
    Supplied in a saline solution containing BSA and Sodium Azide.
  • Label
  • Flow Cytometry
    10 µL/106 cells
    See below
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Data Examples
Detection of Nectin‑2/CD112 in C2C12 Mouse Cell Line by Flow Cytometry. C2C12 mouse myoblast cell line was stained with Rat Anti-Mouse Nectin‑2/CD112 APC‑conjugated Monoclonal Antibody (Catalog # FAB3869A, filled histogram) or isotype control antibody (Catalog # IC006A, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
  • Shipping
    The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
  • Stability & Storage
    Protect from light. Do not freeze.
    • 12 months from date of receipt, 2 to 8 °C as supplied.
Background: Nectin-2/CD112

Nectins are a small family of Ca++-independent immunoglobulin (Ig)-like Cell Adhesion Molecules (CAMs) that control cell adhesion, proliferation, and migration (1, 2, 3). The name Nectin derives from the Latin word necto, which means “to connect”. The Nectin family contains four members (Nectin-1 to -4), all of which show alternate splicing, a transmembrane (TM) region (except for Nectin-1 gamma  which is secreted), and three extracellular Ig-domains. Nectins are highly homologous to the human receptor for poliovirus, and as such have been given the alternate name of poliovirus receptor-related proteins. They do not, however, appear to bind poliovirus (1). Mouse Nectin-2 is a 70 to 78 kDa type I TM glycoprotein that is found on a variety of cell types (4, 5). It has two splice forms (4, 6, 7). Nectin-2 alpha /PRR2 is a 65 kDa short form and is synthesized as a 467 amino acid precursor. It contains a 31 aa signal sequence, a 315 aa extracellular domain (ECD), a 28 aa TM segment, and a 93 aa cytoplasmic region. The ECD contains one N-terminal V-type Ig domain and two 85-95 aa C2-type Ig-like domains (aa 153-337) (8). The V-domain is believed to mediate Nectin binding to its ligands (9). A long, 78 kDa, 530 aa isoform of mouse Nectin-2 (Nectin-2δ) also exists. It has the same signal sequence and extracellular domain as Nectin-2 alpha  (aa 1-338), but differs in the TM segment (21 aa in length) and cytoplasmic region (159 aa in length) (4, 6, 7). Mouse Nectin-2 ECD (aa 32-338) shares 72%, 77% and 95% aa identity with the ECD in human, canine and rat Nectin-2, respectively. Nectin-2 is known to bind pseudorabies virus, and Herpes Simplex Virus-2 (HSV-2). It also binds select HSV-1 strains. It does not bind poliovirus (1, 10, 11). As a cell adhesion molecule, Nectin-2 will form cis‑homodimers (same cell) and trans-homodimers (across cells). Nectin-2 will not cis-dimerize with other Nectins, but will trans-heterodimerize with Nectin-3 and CD266/DNAM-1 (1, 3, 11, 12, 13). Nectin-2 is found concentrated at cell-to-cell interfaces, and is presumed to contribute to tight and adherens junction formation (14). Through its interaction with NK and T cell expressed DNAM-1, it also promotes lymphocyte cytotoxicity and cytokine secretion against both tumors and Dendritic Cells (DC) expressing Nectin-2 (15, 16). In the case of DC, this may be a mechanism whereby the immune system eliminates DC that are inefficient at antigen presentation. Nectin-2 is expressed on epithelium, endothelial cells, Sertoli cells, monocytes, dendritic cells, granulosa cells, mast cells, eosinophils and fibroblasts.

  • References:
    1. Takai, Y. and H. Nakanishi (2003) J. Cell Sci. 116:17.
    2. Rikitake, Y. and Y. Takai (2008) Cell. Mol. Life Sci. 65:253.
    3. Sasisaka, T. et al. (2007) Curr. Opin. Cell Biol. 19:1.
    4. Aoki, J. et al. (1994) J. Biol. Chem. 269:8431.
    5. Takahashi, K. et al. (1999) J. Cell Biol. 145:539.
    6. Aoki, J. et al. (1997) Exp. Cell Res. 235:374.
    7. Lopez, M. et al. (1998) Blood 92:4602.
    8. Morrison, M.E. and V.R. Racaniello (1992) J. Virol. 66:2807.
    9. Struyf, F. et al. (2002) J. Virol. 76:12940.
    10. Delboy, M.G. et al. (2006) Virology J. 3:105.
    11. Irie, K. et al. (2004) Semin. Cell Dev. Biol. 15:643.
    12. Tahara-Hanaoka, S. et al. (2004) Int. Immunol. 16:533.
    13. Satoh-Horikawa, K. et al. (2000) J. Biol. Chem. 275:10291.
    14. Nakanishi, H. and Y. Takai (2004) Biol. Chem. 385:885.
    15. Tahara-Hanaoka, S. et al. (2006) Blood 107:1491.
    16. Pende, D. et al. (2006) Blood 107:2030.
  • 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
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