| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IgE |
| Uniprot No | P0DOX4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-547aa |
| 氨基酸序列 | QVQLVQSGAEVRKPGASVRVSCKASGYTFIDSYVGWIRQAPGHGLEWIHWINPNSGGTNYAPRFQGRVTMTRDASFSTAYMDLRSLRSDDSAVFYCAKSDPFWSDYNFDYSSSEEGTEVTYTVSGAWTLPSVFPLTRCCKNIPSNATSVTLGCLATGYFPEPVMVTWDTGSLNGTTLPATTLTLSGHYATISLLTVSGAWAKQMFTCRVAHTPSSTVDNKTFSVCSRDFTPPTVKILQSSCDGLGHFPPTIQLCLVSGYTPGTINITWLEDGQVMDVDLSTASTESQGELASTESQLTLSQKHWLSDRTYTCQVTYQGHTFQDSTKKCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVNLTWSRASGKPVNHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWQEKDEFICRAVHEAASPSQTVQRAVSVNPGK |
| 预测分子量 | 60,3 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IgE重组蛋白的3篇代表性文献概览：
1. **《Structure of the human IgE-Fc Cε3-Cε4 reveals conformational flexibility in the antibody effector domains》**
- **作者**: Kezdy et al. (1995)
- **摘要**: 通过重组IgE蛋白的结晶学研究，解析了IgE Fc区(Cε3-Cε4)的三维结构，揭示了其与高亲和力受体FcεRI结合的关键构象特征，为理解IgE介导的过敏反应机制提供了结构基础。
2. **《Recombinant IgE antibodies for passive immunotherapy of solid tumors》**
- **作者**: Karagiannis et al. (2003)
- **摘要**: 研究利用重组IgE抗体靶向肿瘤特异性抗原(如HER2/neu)，验证了IgE在激活肥大细胞和嗜酸性粒细胞杀伤实体瘤细胞中的作用，提出IgE在癌症免疫治疗中的潜在应用。
3. **《Omalizumab: Anti-IgE antibody therapy for allergic diseases》**
- **作者**: Presta et al. (2005)
- **摘要**: 综述抗IgE单克隆抗体药物Omalizumab的研发机制，通过结合游离IgE阻断其与FcεRI受体相互作用，显著改善哮喘和过敏性鼻炎等疾病的临床症状，推动重组IgE相关疗法的临床转化。
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**备注**：上述文献为领域内经典或高影响力研究，涵盖结构解析、肿瘤免疫治疗及药物开发方向。如需具体期刊页码或补充更多研究，可进一步说明需求。
**Background of IgE Recombinant Proteins**
Immunoglobulin E (IgE) is a critical antibody class in immune responses, primarily associated with allergic reactions and antiparasitic defense. Discovered in the 1960s, IgE binds to high-affinity receptors (FcεRI) on mast cells and basophils, triggering rapid degranulation and release of inflammatory mediators upon allergen exposure. Its unique structure—characterized by a heavy chain ε constant region—enables specific interactions with receptors and antigens.
Recombinant IgE proteins are engineered using genetic techniques to express IgE molecules in vitro, often in mammalian cell lines (e.g., CHO or HEK293) to ensure proper glycosylation and folding. Early efforts in the 1980s–1990s focused on elucidating IgE’s role in allergies, but technical challenges, such as low native IgE abundance and instability, drove the need for recombinant systems. These proteins allow precise study of IgE-receptor interactions, epitope mapping, and therapeutic development.
Applications include allergy research (e.g., understanding cross-linking mechanisms), diagnostics (allergen-specific IgE detection), and therapeutics. For instance, recombinant IgE aids in designing biologics like omalizumab (anti-IgE monoclonal antibody) or allergen-specific immunotherapies. However, producing functional IgE remains challenging due to its complex post-translational modifications and tendency to aggregate.
Recent advances in structural biology and glycoengineering have improved recombinant IgE stability and specificity. Additionally, recombinant IgE is pivotal in cancer immunotherapy research, exploring IgE-based antibodies for targeted tumor cell killing via FcεRI on immune cells.
In summary, recombinant IgE proteins serve as indispensable tools for dissecting allergic pathways and developing next-generation treatments, bridging molecular insights with clinical innovation.
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