NKG2C/CD159c Protein, Mouse (HEK293, hFc)

The NKG2C/CD159c protein is an immune-activating receptor that critically differentiates self from non-self by forming a complex with KLRD1. It recognizes non-canonical MHC-E loaded with signal sequence-derived peptides from MHC-G molecules and contributes to the generation and effector function of adaptive NK cells, playing a role in maternal-fetal tolerance. NKG2C/CD159c Protein, Mouse (HEK293, hFc) is the recombinant mouse-derived NKG2C/CD159c protein, expressed by HEK293 , with C-hFc labeled tag.

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.

Mouse

HEK293

C-hFc

Q9MZK6 (I94-L231)

709790

Extracellular Domain

IPFLEQNNSFPNTRTQKVRHCGHCPEEWITYSNSCYYIGKEKRTWAESLLACTSKNSSLLSIDNEEEMKFLTAISPSTWTGVFRDSSHHPWVTINGLTFKHEIKDSDHAEYNCAMLHLDRLKSVQCGSSKRYYCKHKL

Approximately 52-60 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.