- Species ReactivityHuman
- SpecificityDetects human Nectin-2/CD112 by flow cytometry.
- SourceMonoclonal Mouse IgG1 Clone # 610603
- PurificationProtein A or G purified from hybridoma culture supernatant
- ImmunogenMouse myeloma cell line NS0-derived recombinant human Nectin-2/CD112 isoform a
Gln32-Leu360
Accession # NP_002847 - FormulationSupplied in a saline solution containing BSA and Sodium Azide.
- LabelAlexa Fluor 488
- Flow Cytometry5 µL/106 cellsSee below
- ShippingThe product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
- Stability & StorageProtect from light. Do not freeze.
- 12 months from date of receipt, 2 to 8 °C as supplied.
- Takai, Y. and H. Nakanishi, 2003, J. Cell Sci. 116:17.
- Bottino, C. et al. (2003) J. Exp. Med. 198:557.
- Pende, D. et al. (2005) Mol. Immunol. 42:463.
- Eberle, F. et al. (1995) Gene 159:267.
- Warner, M.S. et al. (1998) Virology 246:179.
- Struyf, F. et al. (2002) J. Virol. 76:12940.
- 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
Background:
Nectins are a small family of Ca++-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that organize intercellular junctions (1). The nectin family has at least four members (nectin-1-4), all of which show alternate splicing (except for Nectin-4), 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 alternately named poliovirus receptor-related proteins. They do not, however, appear to bind poliovirus (1). Nectin-2 is a 60 or 65 kDa type I TM glycoprotein that is found on a variety of cell types (2, 3). It has two splice forms (4, 5). Nectin-2δ is a 65 kDa long form and is synthesized as a 538 amino acid precursor. It contains a 31 amino acid (aa) signal sequence, a 329 aa extracellular region, a 21 aa TM segment, and a 157 aa cytoplasmic domain. The extracellular region contains one N-terminal 85 aa V-type Ig domain and two 45-55 aa C2-type Ig domains. The V-domain is believed to mediate nectin binding to its ligands (6). The short, 60 kDa isoform of Nectin-2 (Nectin-2 alpha ) has the same signal sequence and extracellular domain as nectin-2δ, but differs in the TM and cytoplasmic region (4, 5). In this case, the cytoplasmic tail is only 94 aa in length. The human extracellular region shows 72% aa sequence identity with the equivalent region in mouse. Nectin-2 is known to bind the pseudorabies virus, and herpes simplex virus-2 (HSV-2), but not HSV-1. It does not bind poliovirus. As a cell adhesion molecule, Nectin-2 will form cis-homodimers (same cell), followed by trans-dimers (across cells). Nectin-2 will not cis-dimerize with other nectins, but will cis-dimerize with its two splice forms. Notably, a Nectin-2 cis-dimer on one cell will heterodimerize with a Nectin-3 cis-dimer on another cell (1). Nectin-2 is found concentrated in adherens junctions, and exists on neurons, endothelial cells, epithelial cells and fibroblasts.
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