CD161 Monoclonal Antibody (10/78), PerCP-eFluor™ 710, eBioscience™, Invitrogen™

Description

Plays an inhibitory role on natural killer (NK) cells cytotoxicity. Activation results in specific acid sphingomyelinase/SMPD1 stimulation with subsequent marked elevation of intracellular ceramide. Activation also leads to AKT1/PKB and RPS6KA1/RSK1 kinases stimulation as well as markedly enhanced T-cell proliferation induced by anti-CD3. Acts as a lectin that binds to the terminal carbohydrate Gal-alpha(1,3)Gal epitope as well as to the N-acetyllactosamine epitope. Binds also to CLEC2D/LLT1 as a ligand and inhibits NK cell-mediated cytotoxicity as well as interferon-gamma secretion in target cells. {ECO:0000269; PubMed:16455998, ECO:0000269; PubMed:16925668, ECO:0000269; PubMed:8077657}.

KLRB1 (Killer cell lectin like receptor subfamily B, member 1, CD-161) protein is classified as a type II membrane protein because it has an external C terminus. KLRB1 cell surface antigen is expressed by almost all NK cells and in a small subset of CD3+ve T cells. KLRB1 is a homodimeric cell surface protein, comprising two chains with molecular weights ranging from 40-44kDa. KLRB1 plays an inhibitory role on natural killer (NK) cells. Activation of KLRB1 leads to acid sphingomyelnase/SMPD1 stimulation and an increase in intracellular ceramide. Moreover, there is also an activation of AKT1/PKB and RPS6KA1/RSK1 kinase stimulation, and T cell proliferation by anti-CD3. KLRB1 acts as a lectin that binds to the terminal carbohydrate Gal-alpha(1,3)Gal epitope and to the N-acetyllactosamine epitope. KLRB1 also binds to CLEC2D/LLT1 as a ligand, and inhibits NK cell-mediated cytotoxicity as well as interferon-gamma secretion in target cells. The KLRB1 protein contains an extracellular domain with several motifs characteristic of C-type lectins, a transmembrane domain, and a cytoplasmic domain.