NKG2C-CD94 Heterodimer Protein, Human (Biotinylated, HEK293, His-Avi)

NKG2C/CD159c Protein, an immune activating receptor, plays a pivotal role in self-nonself discrimination. Teaming up with KLRD1 on cytotoxic lymphocyte subsets, it recognizes non-classical major histocompatibility (MHC) class Ib HLA-E loaded with signal sequence-derived peptides from non-classical MHC class Ib HLA-G molecules. This interaction likely contributes to the generation and effector functions of adaptive natural killer (NK) cells and is implicated 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 infection. Upon binding to HLA-E-peptide complexes, NKG2C/CD159c transmits intracellular signals through the adapter protein TYROBP/DAP12, initiating the phosphorylation of proximal signaling molecules and subsequent cell activation. Forming a heterodimer with KLRD1 through disulfide linkage, the KLRD1-KLRC2 receptor complex, in association with TYROBP homodimers, is crucial for its cell surface expression. Additionally, this receptor complex can bind with low affinity to HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia. The multifaceted interactions and functions of NKG2C/CD159c underscore its essential role in immune responses and self-tolerance mechanisms.