CD226 Extracellular Domain (mouse, recombinant; His-tagged)

CD226, also known as DNAM-1, is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily.¹ It is composed of an N-terminal signal peptide, an extracellular domain containing two immunoglobulin-like (Ig-like) domains and two paired cysteine residues, a transmembrane domain, and a C-terminal cytoplasmic region containing at least two phosphorylation sites important for ligand binding.^1,2 It is expressed on certain T cells, natural killer (NK) cells, monocytes, and B cells and mediates cell adhesion between these and other immune cells.¹ CD226 is an adhesion protein that binds to its ligands, PVR/CD155 or nectin-2/CD112, expressed on immature dendritic cells, as well as infected or transformed cells, to induce NK-mediated killing and cell lysis.² CD226 also associates with lymphocyte function-associated antigen 1 (LFA1) on activated NK cells, which is essential for its signaling.³ A variant of Cd226 generated through alternative splicing in mice lacks the first Ig-like domain and does not interact with CD155.² In addition, mouse Cd226 interacts with mouse, but not human, CD155.⁴ CD226 is involved in immunological synapse formation and acts as a co-stimulatory molecule on NK cells to promote antigen presenting cell-induced cytokine release that, in turn, induces IFN-γ secretion from NK cells.² It is also involved in NK cell-mediated immunosurveillance, reducing tumor growth in mouse models of cancer while Cd226^-/- mice are more susceptible to NK cell-dependent tumor initiation.^2,5 A glycine-to-serine mutation at position 307 of CD226 is associated with autoimmune diseases, such as rheumatoid arthritis, systemic lupus erythematosus (SLE), and multiple sclerosis.^2,6 Cayman’s CD226 Extracellular Domain (mouse, recombinant; His-tagged) protein can be used for binding assay and ELISA applications. This protein consists of 247 amino acids, has a calculated molecular weight of 28.2 kDa, and a predicted N-terminus of Glu19 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 43 kDa due to glycosylation.

WARNING This product is not for human or veterinary use.

1. Shibuya, A., Campbell, D., Hannum, C., et al. DNAM-1, a novel adhesion molecule involved in the cytolytic function of T lymphocytes. Immunity 4(6), 573-581 (1996).

2. Martinet, L., and Smyth, M.J. Balancing natural killer cell activation through paired receptors. Nat. Rev. Immunol. 15(4), 243-254 (2015).

3. Shibuya, K., Lanier, L.L., Phillips, J.H., et al. Physical and functional association of LFA-1 with DNAM-1 adhesion molecule. Immunity 11(5), 615-623 (1999).

4. Stanietsky, N., Rovis, T.L., Glasner, A., et al. Mouse TIGIT inhibits NK-cell cytotoxicity upon interaction with PVR. Eur. J. Immunol. 43(8), 2138-2150 (2013).

5. Lakshmikanth, T., Burke, S.E., Ali, T.H., et al. NCRs and DNAM-1 mediate NK cell recognition and lysis of human and mouse melanoma cell lines in vitro and in vivo. J. Clin. Invest. 119(5), 1251-1263 (2009).

6. Hafler, J.P., Maier, L.M., Cooper, J.D., et al. CD226 Gly307Ser association with multiple autoimmune diseases. Genes Immun. 10(1), 5-10 (2008).