Human DNAM-1/CD226 Fluorescein-conjugated Antibody

DNAX accessory molecule-1 (DNAM-1), also known as CD226, is a 65 kDa type I transmembrane glycoprotein in the immunoglobulin superfamily (1). Mature human DNAM-1 contains a 236 amino acid (aa) extracellular domain (ECD) with two Ig-like C2-set domains and a 61 aa cytoplasmic region that contains motifs for binding PDZ domains and band 4.1 family proteins (1, 2). Within the ECD, human DNAM-1 shares 50% and 52% aa sequence identity with mouse and rat DNAM-1, respectively. DNAM-1 is expressed on multiple lymphoid and myeloid cells and interacts with CD155/PVR and Nectin-2/CD112 (3, 4). Ligation of DNAM-1 promotes the activation of NK cells, CD8⁺ T cells, and mast cells (2‑6), dendritic cell maturation, megakaryocyte and activated platelet adhesion to vascular endothelial cells, and monocyte extravasation; it inhibits the forrmation of osteoclasts (7‑10). Platelet-endothelium interactions mediated by DNAM-1 enable the metastasis of tumor cells to the lung (11). In activated, but not in resting NK, T, and mast cells, the cis association of DNAM-1 with CD18 contributes to the tyrosine and serine phosphorylation of DNAM-1 during activation (6, 9, 12‑14).