| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFSF18 |
| Uniprot No | Q9UNG2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 50-177aa |
| 氨基酸序列 | LFCSIVMLLFLCSFSWLIFIFLQLETAKEPCMAKFGPLPSKWQMASSEPP CVNKVSDWKLEILQNGLYLIYGQVAPNANYNDVAPFEVRLYKNKDMIQTL TNKSKIQNVGGTYELHVGDTIDLIFNSE |
| 预测分子量 | 21 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TNFSF18(GITRL)重组蛋白的3篇代表性文献摘要示例：
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1. **文献名称**: *Recombinant GITRL modulates regulatory T cell activity and enhances antitumor immunity in murine models*
**作者**: Wang et al. (2016)
**摘要**: 研究利用大肠杆菌表达系统制备重组TNFSF18蛋白，发现其能通过激活GITR信号通路抑制调节性T细胞(Treg)的免疫抑制功能，在黑色素瘤小鼠模型中显著增强CD8+ T细胞的抗肿瘤活性。
2. **文献名称**: *Structural basis of GITR recognition by the GITR ligand revealed by X-ray crystallography*
**作者**: Li et al. (2018)
**摘要**: 通过哺乳动物细胞表达纯化获得TNFSF18重组蛋白，解析其与受体GITR的复合物晶体结构，揭示两者特异性结合的分子机制，为靶向药物设计提供结构基础。
3. **文献名称**: *Recombinant GITRL protein alleviates experimental autoimmune encephalomyelitis by balancing Th17/Treg responses*
**作者**: Martinez-Lostao et al. (2020)
**摘要**: 研究发现酵母表达系统生产的TNFSF18重组蛋白可通过调控Th17/Treg细胞比例，显著减轻多发性硬化症模型小鼠的神经炎症症状，提示其在自身免疫疾病中的治疗潜力。
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注：上述文献信息为示例性质，实际引用需以具体论文内容为准。建议通过PubMed或Web of Science等数据库以“TNFSF18 recombinant protein”或“GITRL recombinant”为关键词检索最新研究。
TNFSF18 (Tumor Necrosis Factor Superfamily Member 18), also known as GITR Ligand (GITRL), is a type II transmembrane protein belonging to the TNF superfamily. It plays a critical role in modulating immune responses by interacting with its receptor, GITR (Glucocorticoid-Induced TNFR-Related Protein). The TNFSF18-GITR axis is primarily involved in regulating T-cell activation, differentiation, and immune tolerance. Structurally, TNFSF18 exists as a homotrimer, with its extracellular domain mediating receptor binding and signal transduction. Recombinant TNFSF18 protein, typically produced in mammalian expression systems (e.g., HEK293 or CHO cells), retains the bioactive trimeric conformation and is engineered as a soluble form for research or therapeutic applications.
Functionally, TNFSF18 enhances effector T-cell responses while suppressing regulatory T-cell (Treg) activity, making it a potential target for cancer immunotherapy. By antagonizing Treg-mediated immunosuppression, recombinant TNFSF18 may promote antitumor immunity. Conversely, dysregulation of this pathway has been implicated in autoimmune diseases, highlighting its dual role in immune homeostasis. In preclinical studies, recombinant TNFSF18 has shown promise in enhancing vaccine efficacy and synergizing with checkpoint inhibitors. Its therapeutic potential is under investigation in oncology, particularly for cancers with high Treg infiltration. However, challenges remain in balancing immune activation with off-target inflammation. As a research tool, recombinant TNFSF18 is widely used to dissect GITR signaling mechanisms and validate drug candidates targeting this pathway.
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