Recombinant Mouse Nectin-2/CD112 Protein, CF

• Reactivity: Mu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Mouse Nectin-2/CD112 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse Nectin-2/CD112 is coated at 1 μg/mL (100 μL/well), the concentration of Recombinant Mouse DNAM-1 Fc Chimera (Catalog # 4436-DN) that produces 50% optimal binding response is 0.3-1.8 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse Nectin-2/CD112 protein
  Gln32-Gly351, with a C-terminal 6-His tag
• Accession #: P32507
• N-terminal Sequence: No results obtained: Gln32 predicted
• Structure / Form: Monomer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Nectin2
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 35.4 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: 45-50 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 Mouse Nectin-2/CD112 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 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 - 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.

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.

Bioinformatics

• Gene Symbol: Nectin2
• Uniprot:
  • P32507()