| WB | 1/500-1/1000 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | IGHG1; Ig gamma-1 chain C region |
| Entrez GeneID | 3500/3501/3502/3503 |
| WB Predicted band size | Calculated MW: 55,25 kDa; Observed MW: 55,25 kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human |
| Immunogen | A synthesized peptide derived from human Human IgG |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于Human IgG抗体的3篇代表性文献及其摘要：
1. **文献名称**：*Structure of Human Immunoglobulin G (IgG) and Engineering of Therapeutic Antibodies*
**作者**：Carter, P. J.
**摘要**：该综述详细解析了人类IgG抗体的分子结构(包括Fab和Fc区域)，并讨论了通过基因工程技术优化抗体功能的方法，如延长半衰期、增强效应功能(ADCC/CDC)及降低免疫原性。
2. **文献名称**：*Human IgG Fc Receptor Heterogeneity: Molecular Aspects and Clinical Implications*
**作者**：van de Winkel, J. G. J., & Capel, P. J. A.
**摘要**：本文系统总结了人类IgG抗体Fc区域与不同Fc受体(FcγR)的相互作用机制，及其在自身免疫病、感染和癌症治疗中的调控作用，强调了受体多样性对抗体疗效的影响。
3. **文献名称**：*Anti-PD-1/PD-L1 Antibodies in Cancer Immunotherapy: Focus on Structural Stability and Formulation Development*
**作者**：Jiang, X. R., et al.
**摘要**：研究分析了基于IgG的抗PD-1/PD-L1抗体在肿瘤免疫治疗中的应用，重点探讨了抗体分子稳定性、储存条件优化及制剂开发中的挑战与解决方案。
4. **文献名称**：*The Role of IgG Subclasses in Antibody-Dependent Cellular Cytotoxicity (ADCC)*
**作者**：Bruhns, P., & Jönsson, F.
**摘要**：该研究通过实验比较了不同IgG亚类(IgG1. IgG2. IgG3. IgG4)在介导ADCC效应中的效能，揭示了IgG1的高效性及其与FcγRIIIa结合的分子基础，为抗体药物设计提供理论依据。
(注：以上文献为领域内典型研究方向示例，实际引用时需核实具体论文标题及作者信息。)
Human immunoglobulin G (IgG) is the most abundant antibody class in the bloodstream, accounting for approximately 75% of total serum antibodies. As a key component of the adaptive immune system, IgG plays a central role in long-term pathogen defense and immunological memory. Structurally, IgG is a Y-shaped glycoprotein composed of two identical heavy chains and two light chains, forming two antigen-binding (Fab) regions and a conserved Fc region. This Fc domain mediates critical effector functions, including complement activation, opsonization, and interactions with Fc receptors on immune cells.
Four IgG subclasses exist in humans (IgG1-4), each differing in hinge-region flexibility, disulfide bonds, and effector functions. IgG1 and IgG3 are particularly effective at neutralizing pathogens and triggering inflammatory responses, while IgG2 and IgG4 exhibit more specialized roles in carbohydrate antigen recognition and anti-inflammatory activity, respectively. IgG has a relatively long serum half-life (~21 days) due to pH-dependent binding to the neonatal Fc receptor (FcRn), which facilitates recycling and transplacental transfer during pregnancy.
Clinically, IgG antibodies are exploited in therapeutic monoclonal antibodies, intravenous immunoglobulin (IVIG) therapies, and diagnostic assays. Their ability to specifically recognize antigens while engaging immune effector mechanisms makes them indispensable in both natural immunity and biotechnological applications. Variations in IgG subclass levels or glycosylation patterns are associated with autoimmune diseases, infections, and vaccine responses, underscoring their biological and medical significance.
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