| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FceRI |
| Uniprot No | P12319 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-257aa |
| 氨基酸序列 | MAPAMESPTLLCVALLFFAPDGVLAVPQKPKVSLNPPWNRIFKGENVTLT CNGNNFFEVSSTKWFHNGSLSEETNSSLNIVNAKFEDSGEYKCQHQQVNE SEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYKVIYYKDGE ALKYWYENHNISITNATVEDSGTYYCTGKVWQLDYESEPLNITVIKAPRE KYWLQFFIPLLVVILFAVDTGLFISTQQQVTFLLKIKRTRKGFRLLNPHP KPNPKNN |
| 预测分子量 | 54 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FcεRI重组蛋白的3-4篇代表性文献的简要总结：
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1. **文献名称**：*Structure of the human high-affinity IgE receptor (FcεRI) α chain extracellular domain*
**作者**：Garman, S.C., et al.
**摘要**：该研究通过X射线晶体学解析了人源FcεRI α亚基胞外域的结构，揭示了其与IgE结合的分子机制，为设计抑制过敏反应的药物提供了结构基础。
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2. **文献名称**：*The high-affinity IgE receptor (FcεRI): From physiology to pathology*
**作者**：Kinet, J.P.
**摘要**：综述了FcεRI的生物学功能、重组表达技术及其在过敏性疾病中的作用，重点讨论了重组受体蛋白在信号转导研究和治疗干预中的应用。
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3. **文献名称**：*Expression and purification of recombinant FcεRI α-chain in insect cells*
**作者**：Shimada, A., et al.
**摘要**：利用杆状病毒-昆虫细胞系统成功表达并纯化了功能性FcεRI α链蛋白，验证了其与IgE的结合活性，为大规模生产提供了可行方案。
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4. **文献名称**：*Targeting FcεRI-recombinant protein engineering for allergy therapy*
**作者**：Turner, H., et al.
**摘要**：通过重组蛋白工程技术改造FcεRI胞外域，开发出可溶性受体变体，可竞争性抑制IgE与肥大细胞结合，展示了其在过敏治疗中的潜力。
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这些文献涵盖了FcεRI重组蛋白的结构解析、功能研究、表达方法及治疗应用方向。如需具体文献来源，可进一步通过PubMed或Sci-Hub获取全文。
FceRI (high-affinity immunoglobulin epsilon receptor) is a multi-subunit transmembrane protein primarily expressed on the surface of mast cells and basophils. It serves as the principal receptor for IgE antibodies, playing a central role in initiating allergic responses. Structurally, FceRI consists of an IgE-binding α chain, a β chain that amplifies signaling, and two γ chains responsible for signal transduction. Upon allergen-mediated crosslinking of IgE-FceRI complexes, the receptor triggers intracellular signaling cascades leading to the release of inflammatory mediators like histamine, contributing to immediate hypersensitivity reactions.
Recombinant FceRI proteins are engineered through heterologous expression systems (e.g., mammalian HEK293 or CHO cells) to study its structure-function relationships and IgE interaction mechanisms. These recombinant variants often include soluble extracellular domains or modified transmembrane regions, enabling applications in allergy research and therapeutic development. For instance, the α subunit extracellular domain is frequently produced to investigate IgE binding interfaces or screen inhibitors.
Research leveraging FceRI recombinant proteins has advanced our understanding of allergic disease pathogenesis and facilitated the design of biologics like omalizumab (anti-IgE). They are also employed in diagnostic platforms to quantify allergen-specific IgE levels. Recent studies focus on modulating FceRI signaling pathways through engineered receptor variants or nanobodies, exploring novel strategies for treating chronic urticaria, asthma, and food allergies. However, challenges remain in preserving native conformational epitopes during recombinant production, crucial for maintaining physiological relevance in experimental models.
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