NKG2C/CD159c Protein, Mouse (HEK293, hFc)

NKG2C/CD159c protein operates as an immune activating receptor crucial for self-nonself discrimination. When forming a complex with KLRD1 on cytotoxic lymphocyte subsets, it recognizes non-classical major histocompatibility complex MHC-E loaded with signal sequence-derived peptides from non-classical MHC-G molecules. This recognition likely contributes to the generation and effector functions of adaptive natural killer (NK) cells and plays a role in maternal-fetal tolerance during pregnancy. NKG2C/CD159c also regulates the effector functions of terminally differentiated cytotoxic lymphocyte subsets, particularly in the adaptive NK cell response to viral infections. Upon MHC-E-peptide binding, it transmits intracellular signals via the adapter protein TYROBP/DAP12, leading to the phosphorylation of proximal signaling molecules and cell activation. NKG2C/CD159c forms a heterodimer with KLRD1, and this complex, disulfide-linked, interacts with TYROBP/DAP12 homodimer, an interaction crucial for the expression of NKG2C/CD159c on the cell surface. This intricate mechanism underscores the significant role of NKG2C/CD159c in immune responses, particularly in recognizing and responding to specific MHC-E-peptide complexes and modulating the functions of cytotoxic lymphocytes.