Cayman 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.

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