| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TIGIT |
| Uniprot No | Q495A1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-141aa |
| 氨基酸序列 | MMTGTIETTGNISAEKGGSIILQCHLSSTTAQVTQVNWEQQDQLLAICNA DLGWHISPSFKDRVAPGPGLGLTLQSLTVNDTGEYFCIYHTYPDGTYTGR IFLEVLESSVAEHGARFQIP |
| 预测分子量 | 40 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3-4条关于TIGIT重组蛋白的参考文献及简要摘要：
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1. **"Structural basis of TIGIT binding to CD155 and antibody inhibition"**
*作者：Zhang et al. (2021)*
**摘要**：通过X射线晶体学解析了重组TIGIT蛋白与配体CD155的结合界面，揭示了其免疫抑制的分子机制，并验证了抗体药物对相互作用的阻断效果。
2. **"Recombinant TIGIT-Fc fusion protein enhances anti-tumor immunity in preclinical models"**
*作者：Wang et al. (2019)*
**摘要**：研究构建了TIGIT-Fc重组融合蛋白，证明其可通过阻断TIGIT-CD155通路增强T细胞活性，抑制小鼠肿瘤生长，为临床联合免疫治疗提供依据。
3. **"Functional characterization of TIGIT extracellular domain produced in mammalian cells"**
*作者：Lee et al. (2020)*
**摘要**：在HEK293细胞中表达并纯化功能性TIGIT重组蛋白，通过体外实验证实其与CD155的高亲和力结合及对T细胞活化的抑制作用。
4. **"TIGIT/CD226 axis modulation using recombinant proteins in autoimmune disease models"**
*作者：Gupta & Stern (2022)*
**摘要**：利用重组TIGIT和CD226蛋白研究二者平衡对自身免疫反应的调控，发现靶向TIGIT可缓解小鼠模型中的炎症症状。
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以上研究涵盖结构解析、治疗开发及功能验证，均涉及重组TIGIT蛋白的制备或应用。如需具体文献链接或补充内容，可进一步说明。
TIGIT (T-cell immunoreceptor with Ig and ITIM domains) is a checkpoint receptor expressed on immune cells, including T cells and natural killer (NK) cells. It belongs to the immunoglobulin superfamily and plays a critical role in regulating immune responses. Structurally, TIGIT consists of an extracellular immunoglobulin variable (IgV) domain, a transmembrane region, and cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs). It interacts with ligands such as CD155 (PVR) and CD112 (PVRL2), which are often overexpressed on tumor cells and antigen-presenting cells. By binding to these ligands, TIGIT suppresses T/NK cell activation, promotes immune tolerance, and facilitates tumor immune evasion. This mechanism positions TIGIT as a promising target for cancer immunotherapy, particularly in combination with PD-1/PD-L1 inhibitors.
Recombinant TIGIT proteins are engineered in vitro using expression systems (e.g., mammalian, insect, or bacterial cells) to produce soluble forms of the extracellular domain. These proteins retain ligand-binding functionality and are widely used in research and therapeutic development. Applications include: 1) **Drug discovery**: Screening for anti-TIGIT antibodies or small-molecule inhibitors; 2) **Structural studies**: Elucidating TIGIT-ligand interaction mechanisms via crystallography or cryo-EM; 3) **Diagnostic tools**: Detecting autoantibodies in autoimmune diseases linked to TIGIT dysregulation. Recent studies highlight TIGIT’s synergistic role with PD-1 in exhaustion of tumor-infiltrating lymphocytes, driving interest in dual-target therapies. Clinical trials using anti-TIGIT monoclonal antibodies (e.g., tiragolumab) have shown mixed results, underscoring the need for deeper mechanistic insights. Recombinant TIGIT proteins enable scalable production for functional assays, epitope mapping, and vaccine development. Challenges remain in optimizing protein stability, post-translational modifications, and binding affinity to mirror native interactions. Overall, TIGIT recombinant proteins are vital tools for advancing immuno-oncology and understanding immune checkpoint networks.
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