人 FCGR3B 抗体对
01AB01485
Fc gamma receptor IIIb (FCGR3B), also known as CD16b, is a glycosylphosphatidylinositol (GPI)-anchored membrane protein uniquely expressed on human neutrophils and eosinophils. Unlike other Fc gamma receptors, FCGR3B lacks a cytoplasmic signaling domain and instead acts primarily as a decoy receptor, modulating immune responses by binding to the Fc portion of immunoglobulin G (IgG) and facilitating the clearance of immune complexes. Structurally, it contains two extracellular immunoglobulin-like domains and exists in two main allotypic forms, NA1 and NA2, which differ in their affinity for IgG1 and IgG3; the NA1 variant is more efficient at mediating the ingestion of opsonized particles. Functionally, FCGR3B is involved in actin polymerization, β1 integrin activation, and the formation of neutrophil extracellular traps (NETs), but does not promote phagocytosis or L-selectin expression like its counterpart FCGR2A. Clinically, genetic variations or deficiencies in FCGR3B are associated with increased susceptibility to autoimmune diseases such as systemic lupus erythematosus and certain neutrophil-mediated disorders.
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技术参数
- 靶点基因名
- FCGR3B
- 基因别名
- CD16B; FCG3; FCGR3; IGFR3
- 蛋白别名
- Fc gamma receptor IIIb; FCGR3B
- UniProt
- O75015
- 物种
- Human
产品详情
- 靶点名称
- FCGR3B
- 蛋白名称
- Fc gamma receptor IIIb
- 蛋白别名
- Low affinity immunoglobulin gamma Fc region receptor III-B; Fc-gamma RIII-beta; CD16-I; Fc-gamma RIII; Fc-gamma RIIIb; FcRIII; FcRIIIb; FcR-10; IgG Fc receptor III-1; CD antigen CD16b
- 靶点基因名
- FCGR3B
- 基因别名
- CD16B; FCG3; FCGR3; IGFR3
- UniProt
- O75015
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Fc gamma receptor IIIb (FCGR3B), also known as CD16b, is a glycosylphosphatidylinositol (GPI)-anchored membrane protein uniquely expressed on human neutrophils and eosinophils. Unlike other Fc gamma receptors, FCGR3B lacks a cytoplasmic signaling domain and instead acts primarily as a decoy receptor, modulating immune responses by binding to the Fc portion of immunoglobulin G (IgG) and facilitating the clearance of immune complexes. Structurally, it contains two extracellular immunoglobulin-like domains and exists in two main allotypic forms, NA1 and NA2, which differ in their affinity for IgG1 and IgG3; the NA1 variant is more efficient at mediating the ingestion of opsonized particles. Functionally, FCGR3B is involved in actin polymerization, β1 integrin activation, and the formation of neutrophil extracellular traps (NETs), but does not promote phagocytosis or L-selectin expression like its counterpart FCGR2A. Clinically, genetic variations or deficiencies in FCGR3B are associated with increased susceptibility to autoimmune diseases such as systemic lupus erythematosus and certain neutrophil-mediated disorders.