人 CEACAM3 抗体对
01AB01058
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.
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技术参数
- 靶点基因名
- CEACAM3
- 基因别名
- CD66D; CGM1
- 蛋白别名
- CEA cell adhesion molecule 3; CEACAM3
- UniProt
- P40198
- 物种
- Human
产品详情
- 靶点名称
- CEACAM3
- 蛋白名称
- CEA cell adhesion molecule 3
- 蛋白别名
- Carcinoembryonic antigen-related cell adhesion molecule 3; Carcinoembryonic antigen CGM1; CD antigen CD66d
- 靶点基因名
- CEACAM3
- 基因别名
- CD66D; CGM1
- UniProt
- P40198
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
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.