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.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & 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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
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