Nectin-2 Extracellular Domain (mouse, recombinant)

CD112|Herpesvirus Entry Mediator B|HveB|Nectin Cell Adhesion Molecule 2|Poliovirus Receptor-related Protein 2|PRR2

Nectin-2, also known as CD112, is a member of the nectin family of adhesion molecules that mediates the formation of adherens junctions and regulates immune cell activation.{56107} It contains an N-terminal extracellular domain with three immunoglobulin-like (Ig-like) loops, C1-like and C2 domains that mediate dimerization, a transmembrane segment, and a C-terminal cytoplasmic tail that binds to the actin filament-binding protein afadin.{56107,56108} Nectin-2 is expressed by a variety of cell types, including epithelial cells, neurons, fibroblasts, Sertoli cells, and cancer cells, and is upregulated by TGF-β1 (Item No. 30606) or IFN-β stimulation.{56108,56109,56107} It localizes to the cell surface where it forms cis-homodimers that associate by trans-interactions with cis-homodimers of other nectins and nectin-like molecules (Necls) expressed on adjacent cells, resulting in cell-cell adhesion.{53805,56107} Nectin-2 binds the co-stimulatory receptor CD226/DNAM-1, which is widely expressed by most immune cells, including T cells, B cells, natural killer (NK) cells, and monocytes, and the inhibitory receptors TIGIT and CD96, which are expressed by NK cells and T cells, thus regulating both the activation or inhibition of immune cells in a receptor-specific manner.{56107} It is also the receptor for herpesvirus entry into cells. Sperm isolated from Nectin2-/- mice have decreased motility and maturation and fail to fuse with oocytes, resulting in male-specific infertility.{56110} Neutralization of nectin-2 with a monoclonal antibody decreases tumor growth and reduces metastasis in OV-90 or MDA-MB-231 mouse xenograft models, respectively.{56108} Cayman's Nectin-2 Extracellular Domain (mouse, recombinant) protein can be used for binding assay applications. This protein consists of 331 amino acids, has a calculated molecular weight of 36 kDa, and a predicted N-terminus of Gln32 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 40 to 45 kDa due to glycosylation.

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Lyophilized from sterile PBS, pH 7.4

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≥98% estimated by SDS-PAGE