| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FCER1G |
| Uniprot No | P30273 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 45-86aa |
| 氨基酸序列 | RLKIQVRKAAITSYEKSDGVYTGLSTRNQETYETLKHEKPPQ |
| 预测分子量 | 6.9 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FCER1G重组蛋白的模拟参考文献示例，基于学术文献的常见研究方向和结构整理：
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### 1. **标题**：Recombinant Expression and Functional Characterization of FCER1G in Mast Cell Signaling
**作者**：Zhang L, Chen H, et al.
**摘要**：本研究利用昆虫细胞表达系统成功克隆并纯化了重组FCER1G蛋白，验证其与FcεRIα亚基的结合能力。通过体外信号激活实验，发现重组FCER1G能够增强IgE介导的肥大细胞脱颗粒，揭示了其在过敏反应中的关键作用。
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### 2. **标题**：Structural Insights into FCER1G Interaction with Syk Kinase in Immune Receptor Signaling
**作者**：Müller S, Tanaka R, et al.
**摘要**：通过X射线晶体学解析了重组FCER1G蛋白与Syk激酶的结构复合物，阐明了其ITAM结构域如何招募下游信号分子。研究证实FCER1G的磷酸化位点突变会显著抑制B细胞受体(BCR)信号通路的激活。
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### 3. **标题**：FCER1G-Deficient Mice Rescue via Lentiviral Delivery of Recombinant FCER1G Protein
**作者**：Kim J, Park SM, et al.
**摘要**：利用慢病毒载体在FCER1G缺陷小鼠中表达重组人源FCER1G蛋白，成功恢复了肥大细胞的IgE依赖性炎症反应，为遗传性免疫缺陷疾病的治疗提供了潜在策略。
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### 4. **标题**：Prokaryotic Expression and Immunomodulatory Activity of FCER1G Fusion Protein
**作者**：Gomez A, Li W, et al.
**摘要**：通过大肠杆菌系统高效表达可溶性FCER1G融合蛋白，并证明其能够抑制过度活跃的T细胞受体信号，提示其在自身免疫性疾病中的治疗潜力。
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**注**：以上文献为模拟示例，实际研究中建议通过PubMed、Web of Science等数据库以关键词“FCER1G recombinant”或“FcRγ expression”检索最新文献，重点关注其重组表达策略、信号机制或疾病相关性研究。
The Fc epsilon receptor I gamma subunit (FCER1G) is a critical component of high-affinity immunoglobulin epsilon (IgE) receptors, primarily known for its role in allergic responses and immune regulation. Encoded by the FCER1G gene in humans, this protein forms a disulfide-linked homodimer that associates with ligand-binding α-subunits (e.g., FCER1A) and β-subunits in mast cells and basophils. As a common signaling module, it also partners with other Fc receptors (FcγRI, FcαRI) to mediate cell activation through immunoreceptor tyrosine-based activation motif (ITAM) domains.
Structurally, FCER1G contains an extracellular domain, transmembrane region, and cytoplasmic tail with conserved ITAM sequences essential for signal transduction. Upon IgE-antigen crosslinking, phosphorylated ITAMs recruit tyrosine kinases (e.g., Syk), triggering downstream pathways that lead to inflammatory mediator release. This mechanism underlies immediate hypersensitivity reactions in conditions like asthma and anaphylaxis.
Recombinant FCER1G protein is produced using mammalian or insect expression systems to ensure proper post-translational modifications. Purification typically involves affinity chromatography with tags like His or Fc fusions. The recombinant form retains functional ITAM domains while eliminating confounding variables from native cell environments, making it valuable for studying IgE receptor assembly, signal transduction mechanisms, and cross-talk between immune receptors.
Researchers use FCER1G recombinant proteins in vitro to investigate allergic disease pathophysiology, screen therapeutic inhibitors targeting IgE signaling, and model immune receptor interactions. Its applications extend to studying rare FCER1G-linked immunodeficiencies and developing diagnostic tools for hypersensitivity disorders. Mutant variants are also engineered to dissect structure-function relationships, particularly ITAM phosphorylation dynamics and adaptor protein recruitment patterns.
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