| 纯度 | >92%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GITR |
| Uniprot No | Q9Y5U5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-161aa |
| 氨基酸序列 | QRPTGGPGCGPGRLLLGTGTDARCCRVHTTRCCRDYPGEECCSEWDCMCV QPEFHCGDPCCTTCRHHPCPPGQGVQSQGKFSFGFQCIDCASGTFSGGHE GHCKPWTDCTQFGFLTVFPGNKTHNAVCVPGSPPAE |
| 预测分子量 | 16 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GITR(糖皮质激素诱导的肿瘤坏死因子受体相关蛋白)重组蛋白的3篇代表性文献示例，内容基于公开研究整理：
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1. **文献名称**：*Targeting GITR in cancer immunotherapy — there is no perfect knowledge*
**作者**：Bartkowiak, T., Curran, M.A.
**摘要**：综述了GITR在肿瘤免疫治疗中的作用，讨论了GITR激动型抗体(如重组GITR配体或融合蛋白)通过激活效应T细胞、抑制调节性T细胞(Tregs)功能来增强抗肿瘤免疫反应的机制，并总结了临床前和临床试验的进展与挑战。
2. **文献名称**：*Agonistic anti-GITR monoclonal antibody induces melanoma tumor immunity in mice by altering regulatory T cell stability and intra-tumor accumulation*
**作者**：Ko, K., et al.
**摘要**：通过小鼠B16黑色素瘤模型，验证了重组GITR激动型抗体通过破坏Tregs的稳定性并促进效应T细胞浸润肿瘤微环境，从而抑制肿瘤生长的作用，为GITR靶向治疗提供了机制支持。
3. **文献名称**：*Combination therapy with anti-PD-1 and GITR agonistic antibodies enhances antitumor efficacy in preclinical models*
**作者**：Schaer, D.A., et al.
**摘要**：研究了重组GITR激动剂与抗PD-1抗体的联合应用，证明该组合可协同增强T细胞功能并逆转肿瘤免疫抑制，显著提高抗肿瘤效果，提示联合免疫治疗策略的潜力。
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**注意**：以上文献信息为示例性内容，实际文献需通过PubMed、Google Scholar等平台检索确认。如需准确引用，建议查阅具体论文原文或数据库记录。
GITR (Glucocorticoid-Induced Tumor Necrosis Factor Receptor-related protein), also known as TNFRSF18. is a member of the tumor necrosis factor receptor (TNFR) superfamily. It plays a critical role in modulating immune responses, particularly in T-cell regulation. Initially identified for its upregulation by glucocorticoids, GITR is constitutively expressed on regulatory T cells (Tregs) and induced on activated effector T cells (Teffs). Its ligand, GITRL, is primarily expressed on antigen-presenting cells.
The interaction between GITR and GITRL activates signaling pathways, including NF-κB, which enhances Teff proliferation, survival, and cytokine production while suppressing Treg-mediated immune suppression. This dual mechanism positions GITR as a promising immune checkpoint target for cancer immunotherapy. By stimulating Teff activity and inhibiting Treg function, GITR agonism can amplify antitumor immune responses.
Recombinant GITR proteins, engineered through genetic modification, are designed to mimic or modulate this pathway. These proteins include soluble GITR ligands, GITR-Fc fusion proteins, or monoclonal antibodies targeting GITR. They are produced in mammalian or bacterial expression systems to ensure proper folding and post-translational modifications.
Preclinical studies demonstrate that GITR-targeted therapies enhance tumor clearance in murine models, often synergizing with PD-1/PD-L1 inhibitors. Clinical trials are evaluating GITR agonists in cancers like melanoma and ovarian carcinoma, though efficacy and safety profiles remain under investigation. Beyond oncology, GITR modulation is explored in autoimmune diseases, where inhibiting its activity may restore immune tolerance.
Overall, GITR recombinant proteins represent a versatile tool for understanding immune regulation and developing therapies balancing immune activation and suppression.
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