CD226 Extracellular Domain (human, recombinant)

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 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.^2,4 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.^2,5 Cayman’s CD226 Extracellular Domain (human, recombinant) protein can be used for binding assay applications. This protein consists of 240 amino acids, has a calculated molecular weight of 27.6 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 approximately 40 to 50 kDa due to glycosylation.

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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. 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).

5. 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).