Anti-Human CEACAM3 Antibody Pair

Product Description: CEA cell adhesion molecule 3 (CEACAM3) is a cell adhesion molecule exclusively expressed on human granulocytes that functions as a major receptor mediating recognition and efficient opsonin-independent phagocytosis of CEACAM-binding microorganisms. The protein contains a single extracellular IgV-like domain and a distinctive 71-amino-acid cytoplasmic domain featuring an immunoreceptor tyrosine-based activation motif (ITAM)-like sequence. Upon bacterial infection, CEACAM3 becomes phosphorylated by Src family protein tyrosine kinases (particularly Hck and Fgr), with the Y230 residue serving as the central hub for interactions with SH2 domain-containing proteins. This phosphorylation triggers actin-cytoskeleton-dependent engulfment of bacteria and stimulates the small GTPase Rac, a critical regulator of actin cytoskeleton dynamics and oxidative burst. CEACAM3 appears to be a specialized member of the CEACAM family that evolved specifically for innate immune control of human-specific bacterial pathogens, with no homologues found in other mammalian species and no identified endogenous ligands. Protein Function: Major granulocyte receptor mediating recognition and efficient opsonin-independent phagocytosis of CEACAM-binding microorganisms, including Neissiria, Moxarella and Haemophilus species, thus playing an important role in the clearance of pathogens by the innate immune system. Responsible for RAC1 stimulation in the course of pathogen phagocytosis [The Uniprot Consortium]