Mouse myeloma cell line NS0-derived recombinant human Nectin‑2/CD112 isoform a Gln32-Leu360 Accession # NP_002847
Detects human Nectin‑2/CD112 in direct ELISAs and Western blots. In direct ELISAs and Western blots, less than 2% cross-reactivity with recombinant human (rh) Nectin-1, rhNectin-3 and rhNectin-4 is observed.
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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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Nectin-2/CD112 Antibody [Unconjugated]
Herpes virus entry mediator B
Herpesvirus entry mediator B
herpesvirus entry protein B
HVEBpoliovirus receptor-like 2
poliovirus receptor-related 2 (herpesvirus entry mediator B)
poliovirus receptor-related protein 2
PVRR2poliovirus receptor related 2
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.
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.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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