| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IgG4 |
| Uniprot No | P01861 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 99-326aa |
| 氨基酸序列 | ESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQ EDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKE YKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCL VKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQ EGNVFSCSVMHEALHNHYTQKSLSLSLE |
| 预测分子量 | 26 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于IgG4重组蛋白的3篇代表性文献的简要总结(注：文献信息为模拟示例，非真实存在，仅供参考)：
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1. **文献名称**：*Structural Dynamics of IgG4 Antibodies and Implications for Therapeutic Design*
**作者**：Smith A, et al.
**摘要**：研究解析了IgG4抗体的动态结构特征，发现其重链(CH3)结构域的不稳定性导致Fab臂交换，形成单价抗原结合。提出通过定点突变增强稳定性，为重组IgG4工程化提供策略。
2. **文献名称**：*IgG4-Based Recombinant Antibodies in Cancer Immunotherapy*
**作者**：Chen L, et al.
**摘要**：探讨重组IgG4抗体在肿瘤治疗中的应用，强调其低Fc介导的细胞毒性(ADCC/CDC)特性可减少正常细胞损伤，同时通过PD-1/PD-L1阻断增强抗肿瘤免疫应答。
3. **文献名称**：*Engineering IgG4 Recombinant Proteins for Reduced Inflammation in Autoimmune Diseases*
**作者**：Wang Y, et al.
**摘要**：通过重组技术改造IgG4的Fc区域，降低与Fcγ受体的结合能力，从而减少炎症反应。动物实验显示其在类风湿性关节炎模型中显著减轻病理症状。
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如需真实文献，建议通过PubMed或Google Scholar搜索关键词“IgG4 recombinant engineering”、“IgG4 therapeutic antibodies”等获取近年研究。
**Background of IgG4 Recombinant Proteins**
IgG4. a subclass of immunoglobulin G, plays a unique role in the immune system due to its structural and functional characteristics. Unlike other IgG subclasses (e.g., IgG1), IgG4 exhibits limited effector functions, such as reduced binding to Fcγ receptors and complement proteins, making it less inflammatory. This property stems from its flexible hinge region and CH3 domain modifications, which enable "Fab-arm exchange"—a process where half-molecules of two IgG4 antibodies swap heavy-light chain pairs, forming monovalent, bispecific antibodies. While this dynamic behavior supports immune tolerance in physiological contexts, it poses challenges for therapeutic applications, necessitating engineering to stabilize the molecule.
Recombinant IgG4 proteins are produced via genetic engineering, often using mammalian cell systems (e.g., CHO cells) to ensure proper folding and post-translational modifications. Their design frequently incorporates mutations, such as S228P in the hinge region, to prevent Fab-arm exchange and enhance stability. These modifications retain IgG4’s low effector function while improving homogeneity for clinical use.
Therapeutically, recombinant IgG4 antibodies are leveraged in scenarios where minimizing immune activation is critical. For example, immune checkpoint inhibitors (e.g., pembrolizumab) utilize IgG4 backbones to block inhibitory pathways (e.g., PD-1/PD-L1) without triggering excessive inflammation. Additionally, their engineered bispecific formats are explored in cancer immunotherapy to target multiple antigens simultaneously.
Despite advantages, challenges remain in optimizing production yield, stability, and avoiding unintended interactions. Advances in protein engineering and glycoengineering continue to refine IgG4-based therapeutics, balancing efficacy with safety. Overall, recombinant IgG4 proteins represent a versatile tool in biopharmaceuticals, particularly for applications requiring precise immune modulation.
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