| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF18 |
| Uniprot No | Q9Y5U5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-162aa |
| 氨基酸序列 | QRPTGGPGCGPGRLLLGTGTDARCCRVHTTRCCRDYPGEECCSEWDCMCVQPEFHCGDPCCTTCRHHPCPPGQGVQSQGKFSFGFQCIDCASGTFSGGHEGHCKPWTDCTQFGFLTVFPGNKTHNAVCVPGSPPAEP |
| 预测分子量 | 40.8 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TNFRSF18重组蛋白的3篇参考文献示例(注：文献为虚拟示例，仅供格式参考)：
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1. **文献名称**: *Structural characterization of TNFRSF18 recombinant protein and its interaction with GITRL*
**作者**: Zhang Q, et al.
**摘要**: 本研究通过重组表达技术制备了可溶性TNFRSF18蛋白，并利用X射线晶体学解析其三维结构，揭示了其与配体GITRL结合的关键结构域，为靶向该通路的药物设计提供了分子基础。
2. **文献名称**: *Recombinant TNFRSF18-Fc fusion protein enhances T cell activation in vitro and tumor immunity in vivo*
**作者**: Lee S, et al.
**摘要**: 构建了TNFRSF18-Fc融合蛋白，证明其能有效阻断调节性T细胞(Treg)的抑制功能，并在体外实验中增强效应T细胞的增殖与细胞因子分泌。动物实验显示其显著抑制黑色素瘤生长。
3. **文献名称**: *Optimized production of bioactive TNFRSF18 in E. coli and functional validation in autoimmune models*
**作者**: Müller R, et al.
**摘要**: 开发了一种基于大肠杆菌的高效TNFRSF18重组蛋白表达系统，通过复性工艺获得具有生物活性的蛋白。功能实验表明，该蛋白可调节自身免疫模型中的炎症反应，提示其治疗潜力。
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以上文献摘要聚焦于重组蛋白的结构、功能及治疗应用，涵盖基础研究与临床前实验。如需真实文献，建议通过PubMed或Web of Science以关键词“TNFRSF18 recombinant”或“GITR recombinant protein”检索。
**Background of TNFRSF18 Recombinant Protein**
TNFRSF18 (Tumor Necrosis Factor Receptor Superfamily Member 18), also known as glucocorticoid-induced TNFR-related protein (GITR) or activation-inducible TNFR family receptor (AITR), is a type I transmembrane protein belonging to the TNF receptor superfamily. It is primarily expressed on regulatory T cells (Tregs), activated conventional T cells, and innate immune cells. Structurally, TNFRSF18 contains extracellular cysteine-rich domains critical for ligand binding, a transmembrane region, and an intracellular domain that mediates downstream signaling via TRAF (TNF receptor-associated factor) adaptor proteins.
The natural ligand for TNFRSF18. GITRL, is expressed on antigen-presenting cells (APCs). Their interaction plays a dual role in immune regulation: it enhances effector T cell activation and survival while suppressing the immunosuppressive function of Tregs. This dual mechanism positions TNFRSF18 as a key modulator of immune homeostasis and antitumor responses.
Recombinant TNFRSF18 protein is engineered to mimic or modulate this receptor-ligand interaction. It is typically produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, though prokaryotic systems are also explored for cost efficiency. The recombinant protein often includes an Fc fusion tag to improve stability and prolong half-life *in vivo*.
In research and therapeutics, TNFRSF18 recombinant proteins are investigated for their potential in cancer immunotherapy. Agonistic anti-TNFRSF18 antibodies or Fc-fusion proteins aim to boost antitumor immunity by activating effector T cells and neutralizing Treg-mediated suppression. Preclinical studies show promise in enhancing checkpoint inhibitor efficacy, while early-phase clinical trials explore safety and combinatorial approaches. Challenges remain in balancing immune activation with autoimmune risks, necessitating precise targeting strategies. Overall, TNFRSF18 recombinant proteins represent a promising tool for understanding immune regulation and developing next-generation immunotherapies.
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