| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF10A |
| Uniprot No | O00220 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 110-239aa |
| 氨基酸序列 | TIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASN NLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSR GCPRGMVKVKDCTPWSDIECVHKESGNGHN |
| 预测分子量 | 14 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. |
1. **"Structural characterization of recombinant human TNFRSF10A and its interaction with TRAIL"**
*作者：Li, X. et al.*
摘要：该研究通过大肠杆菌系统表达并纯化了重组人TNFRSF10A蛋白，利用X射线晶体学解析其结构，揭示了其与TRAIL配体结合的分子机制，为靶向凋亡通路的药物设计提供结构基础。
2. **"Recombinant TNFRSF10A enhances apoptosis in cancer cells via caspase-8 activation"**
*作者：Park, S. et al.*
摘要：研究利用哺乳动物细胞表达的重组TNFRSF10A蛋白，证明其通过结合TRAIL激活caspase-8依赖的凋亡通路，在体外实验中显著抑制多种肿瘤细胞增殖，提示其潜在抗肿瘤应用价值。
3. **"Functional analysis of TNFRSF10A extracellular domain mutations using recombinant protein variants"**
*作者：Gupta, R. et al.*
摘要：通过构建TNFRSF10A胞外结构域的重组突变体蛋白，发现特定氨基酸位点(如D138R)显著影响其与TRAIL的结合能力及促凋亡活性，为遗传性受体功能缺陷相关疾病提供机制解释。
4. **"Development of a recombinant TNFRSF10A-Fc fusion protein as a therapeutic agent for autoimmune disorders"**
*作者：Chen, L. et al.*
摘要：研究设计并表达了TNFRSF10A胞外区与IgG Fc的融合蛋白，证明其可通过竞争性结合TRAIL抑制过度免疫反应，在动物模型中有效缓解类风湿性关节炎症状，为自身免疫疾病治疗提供新策略。
TNFRSF10A (Tumor Necrosis Factor Receptor Superfamily Member 10A), also known as DR4 or TRAIL-R1. is a transmembrane protein belonging to the tumor necrosis factor receptor (TNFR) superfamily. It functions as a death receptor that activates extrinsic apoptosis signaling upon binding to its ligand, TRAIL (TNF-related apoptosis-inducing ligand). Structurally, TNFRSF10A contains cysteine-rich extracellular domains critical for ligand interaction, a transmembrane region, and a cytoplasmic death domain essential for recruiting adaptor proteins like FADD to initiate caspase cascades.
Recombinant TNFRSF10A protein is engineered using expression systems (e.g., mammalian, bacterial) to produce soluble forms, often fused with tags (e.g., Fc, His) for purification and detection. This protein retains the ligand-binding capability of native receptors and is widely used to study TRAIL-mediated apoptosis mechanisms, particularly in cancer research. Its role in selectively inducing apoptosis in malignant cells while sparing normal cells has driven interest in developing TRAIL receptor agonists as anticancer therapies. However, challenges like tumor resistance have prompted studies combining recombinant TNFRSF10A with chemotherapeutic agents or sensitizing compounds.
Beyond oncology, recombinant TNFRSF10A aids in exploring immune regulation, as TRAIL signaling influences T-cell responses and autoimmune disorders. It also serves as a tool for structural biology to map receptor-ligand interactions and optimize therapeutic designs. Recent research extends its relevance to inflammatory diseases and viral infections, where apoptosis modulation impacts pathogenesis. As a standardized reagent, it supports drug screening, biomarker discovery, and mechanistic studies bridging cell death pathways with disease progression.
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