Nectin 2 Background Information Nectin is a Ca2+-independent homophilic cell adhesion molecule that belongs to the immunoglobulin superfamily. Human nectin is identical to the poliovirus receptor-related protein (PRR) and has been identified as the a-herpesvirus entry mediator. Nectin constitutes a family consisting of at least Nectin 1, 2, 3 and 4. Nectin 2, also designated PRR2/HveB, is ubquitously expressed, with the highest levels of expression in some human neuronal cell lines, fibroblastic cells, keratinocytes and primary activated T lymphocytes. Nectin 2 has two splicing variants, Nectin 2a (short form) and 2d (long form). Both Nectin 2a and 2d have a C-terminal conserved motif (E/A-X-Y-V). This motif interacts with the PDZ domain of the F-Actin-binding protein afadin, through which it is linked to the Actin cytoskel-eton. The extracellular regions of the splicing variants are identical, but their transmembrane regions and cytoplasmic regions are unique. Nectin 2 mediates the entry of three mutant herpes simplex virus type 1 (HSV-1) strains that do not use HveA as co-receptor, but not wildtype HSV-1 strains. Nectin 2 also mediates the entry of HSV-2 and pseu-dorabies virus, but not cow herpes virus type 1. Nectin 2d is tyrosine phosphorylated in response to cell-cell adhesion.
Nectin 2 (B-C12)
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Nectin 2 (B-C12): sc-65333. Indirect FCM analysis of Jurkat cells stained with Nectin 2 (B-C12), followed by PE-conjugated goat anti-mouse IgG: sc-3738. Black line histogram represents the isotype control, normal mouse IgG2b: sc-3879.