抗人 IgG3 抗体对
01AB00176
Human IgG3 is one of the four subclasses of immunoglobulin G (IgG) antibodies. It has a unique structure characterized by an extended and flexible hinge region, which is much longer than the other IgG subclasses. This elongated hinge allows greater flexibility and movement of the Fab arms relative to the Fc region, contributing to IgG3's potent effector functions such as complement activation and binding to Fc receptors. However, IgG3 also has a shorter half-life compared to other IgG subclasses, primarily due to an arginine at position 435 that impairs its binding to the neonatal Fc receptor (FcRn) responsible for antibody recycling. Notably, IgG3 exhibits extensive allotypic diversity, with over 15 known allelic variations in the hinge region length and sequence. This structural variability influences IgG3's effector functions and has implications for its therapeutic potential.
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技术参数
- 靶点基因名
- IGHG3
- 蛋白别名
- immunoglobulin heavy constant gamma 3 (G3m marker); Human IgG3
- UniProt
- P01860
- 物种
- Human
产品详情
- 靶点名称
- Human IgG3
- 蛋白名称
- immunoglobulin heavy constant gamma 3 (G3m marker)
- 蛋白别名
- Immunoglobulin heavy constant gamma 3; HDC; Heavy chain disease protein; Ig gamma-3 chain C region
- 靶点基因名
- IGHG3
- UniProt
- P01860
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Human IgG3 is one of the four subclasses of immunoglobulin G (IgG) antibodies. It has a unique structure characterized by an extended and flexible hinge region, which is much longer than the other IgG subclasses. This elongated hinge allows greater flexibility and movement of the Fab arms relative to the Fc region, contributing to IgG3's potent effector functions such as complement activation and binding to Fc receptors. However, IgG3 also has a shorter half-life compared to other IgG subclasses, primarily due to an arginine at position 435 that impairs its binding to the neonatal Fc receptor (FcRn) responsible for antibody recycling. Notably, IgG3 exhibits extensive allotypic diversity, with over 15 known allelic variations in the hinge region length and sequence. This structural variability influences IgG3's effector functions and has implications for its therapeutic potential.