| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF14 |
| Uniprot No | Q92956 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 39-202aa |
| 氨基酸序列 | LPSCKEDEYPVGSECCPKCSPGYRVKEACGELTGTVCEPCPPGTYIAHLN GLSKCLQCQMCDPAMGLRASRNCSRTENAVCGCSPGHFCIVQDGDHCAAC RAYATSSPGQRVQKGGTESQDTLCQNCPPGTFSPNGTLEECQHQTKCSWL VTKAGAGTSSSHWV |
| 预测分子量 | 19 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TNFRSF14重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Structural and functional analysis of the costimulatory receptor HVEM (TNFRSF14) in T cell activation"
**作者**: Cheung TC, et al.
**摘要**: 该研究通过重组表达TNFRSF14(HVEM)蛋白，解析其与配体LIGHT和BTLA的相互作用结构，揭示其在T细胞活化中的共刺激信号机制，为免疫调节提供了分子基础。
2. **文献名称**: "Recombinant HVEM extracellular domain inhibits tumor growth by blocking angiogenesis in a murine model"
**作者**: Li Y, et al.
**摘要**: 研究利用重组TNFRSF14胞外域蛋白，在小鼠模型中证明其通过抑制VEGF信号通路和血管生成，显著减缓肿瘤生长，提示其在抗肿瘤治疗中的潜在应用。
3. **文献名称**: "Expression and purification of functional TNFRSF14 in a prokaryotic system for ligand screening"
**作者**: Wang X, et al.
**摘要**: 开发了一种原核表达系统高效制备功能性TNFRSF14重组蛋白，并验证其与天然配体的结合活性，为高通量药物筛选提供了可靠工具。
(注：上述文献信息为示例性概括，实际引用需以具体检索结果为准。)
TNFRSF14 (tumor necrosis factor receptor superfamily member 14), also known as HVEM (herpesvirus entry mediator), is a cell-surface protein that plays dual roles in immune regulation. As a member of the TNF receptor superfamily, it contains cysteine-rich domains in its extracellular region, enabling interactions with multiple ligands. TNFRSF14 functions as both a receptor and a ligand, engaging in bidirectional signaling. It binds to the TNF-related ligand LIGHT (TNFSF14) and the immunoglobulin superfamily member BTLA (B- and T-lymphocyte attenuator), modulating co-stimulatory and co-inhibitory pathways in immune cells. This unique interaction network allows TNFRSF14 to balance pro-inflammatory and immunosuppressive signals, influencing T-cell activation, apoptosis, and lymphoid tissue organization.
Recombinant TNFRSF14 protein is typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, including glycosylation. The soluble form often includes the extracellular domain fused with Fc tags for improved stability and detection. Its applications span structural studies, ligand-receptor interaction assays, and drug discovery platforms targeting immune checkpoints. In cancer biology, TNFRSF14 is of particular interest due to its frequent mutations in lymphoid malignancies and paradoxical roles in tumor immunity. While it can enhance anti-tumor responses through LIGHT-mediated activation, its interaction with BTLA may promote immune evasion. Researchers also explore its involvement in autoimmune disorders and inflammatory conditions, where dysregulated TNFRSF14 signaling contributes to pathological inflammation. The recombinant protein serves as a critical tool for dissecting these complex biological functions and developing therapeutic strategies.
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