|Detection of Nectin‑2/CD112 in K562 Human Cell Line by Flow Cytometry. K562 human chronic myelogenous leukemia cell line was stained with Mouse Anti-Human Nectin‑2/CD112 Monoclonal Antibody (Catalog # MAB2229, filled histogram) or isotype control antibody (Catalog # MAB002, open histogram) followed by PE-conjugated Goat anti-mouse secondary antibody (Catalog # F0102B). View our protocol for Staining Membrane-associated Proteins.|
|Nectin‑2/CD112 in MCF‑7 Human Cell Line. Nectin‑2/CD112 was detected in immersion fixed MCF‑7 human breast cancer cell line using Mouse Anti-Human Nectin‑2/CD112 Monoclonal Antibody (Catalog # MAB2229) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm and plasma membrane. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
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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