CD226, also known as DNAX Accessory Molecule-1 (DNAM-1), is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is expressed on the surface of various immune cells, including T cells, natural killer (NK) cells, monocytes, and platelets . CD226 plays a crucial role in the immune response, particularly in the context of tumor immunology and autoimmune diseases .
CD226 is composed of an extracellular domain, a transmembrane domain, and a cytoplasmic tail. The extracellular domain contains two immunoglobulin-like domains, which are responsible for binding to its ligands, CD155 (PVR) and CD112 (Nectin-2) . The interaction between CD226 and its ligands promotes the activation and cytotoxicity of NK cells and T cells, enhancing their ability to target and destroy tumor cells .
CD226 has emerged as a potent driver of antitumor immunity. It competes with inhibitory receptors such as TIGIT and CD96 for binding to CD155 and CD112 . The balance between activating and inhibitory signals mediated by these receptors is critical for the regulation of immune responses against tumors. High expression levels of CD226 on tumor-infiltrating lymphocytes are associated with improved antitumor responses and better patient outcomes .
Recent studies have shown that the expression of CD226 can be downregulated in tumors, leading to reduced immune surveillance and tumor progression . Strategies to maintain or enhance CD226 expression on immune cells are being explored as potential therapeutic approaches to boost antitumor immunity .
Recombinant CD226 (Human, Sf9) refers to the human CD226 protein produced using the Sf9 insect cell expression system. This system is commonly used for the production of recombinant proteins due to its high yield and post-translational modification capabilities. The recombinant CD226 protein can be used in various research applications, including studies on immune cell activation, cancer immunotherapy, and autoimmune diseases.