CD64 is a 72 kD single chain type I glycoprotein also known as FcγRI and FcRI. CD64 is a member of the immunoglobulin superfamily and is expressed on monocytes/macrophages, dendritic cells, and mast cells. The expression can be upregulated by IFN-γ stimulation. CD64 binds IgG immune complex. It plays a role in antigen capture, phagocytosis of IgG/antigen complexes, and antibody-dependent cellular cytotoxicity (ADCC).
CD66a, known as CEACAM1a, carcinoembryonic antigen-related cell adhesion molecule 1a, is a glycoprotein of the immunoglobulin superfamily and the carcinoembryonic antigen family. Isoforms expressing either two or four alternatively spliced Ig-like domains in mice have been found in a number of epithelial, endothelial, or hematopoietic tissues. CEACAM1a functions as an intercellular adhesion molecule, an angiogenic factor, and a tumor cell growth inhibitor. It also serves as a signal regulatory protein influencing B cell receptor complex-mediated activation. The mouse and human CEACAM1a proteins are targets of viral or bacterial pathogens, respectively. It was reported that targeted disruption of the CEACAM1a gene resulting in a partial ablation of the protein in mice led to reduced susceptibility to virus infection. The antibody recognizes the N-terminal domain of murine CEACAM1a, it does not recognize murine CEACAM1b, an allele in SJL mice.
CD69 is a 60 kD type II membrane protein composed of a 27/33 kD disulfide-linked homodimer, also known as Very Early Activation Antigen (VEA), AIM, EA1, MLR3, and gp34/28. It is expressed on a subset of thymocytes and platelets. CD69 is rapidly induced on activated T and B cells, neutrophils, and NK cells. It is a C-type lectin, closely related to the NKR-P1 and Ly-49 NK cell activation molecules. CD69 is involved in the early events of cell activation and thymocyte positive selection.
CD6, a 100 kD monomeric T cell surface glycoprotein, is a member of the scavenger receptor cysteine-rich protein superfamily. It is expressed on mouse thymocytes and splenic T cells and neurons, but not on splenic B cells. CD6 has a long cytoplasmic tail in mice, with two proline-rich domains that interact with the -SH3 domain binding sequence. CD6 binding to its ligand, CD166 (ALCAM), serves as a costimulatory molecule through its interaction with SLP-76. CD6 mediated signaling may contribute to thymocyte survival and functional avidity in mice and men.
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