| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Tnfrsf10b |
| Uniprot No | O14763 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 56-182aa |
| 氨基酸序列 | ITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKE |
| 预测分子量 | 15.7 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Tnfrsf10b(DR5/TRAIL-R2)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *"Recombinant soluble DR5 induces apoptosis and sensitizes human cancer cells to TRAIL-mediated cell death"*
**作者**: Wu GS, et al.
**摘要**: 该研究成功表达并纯化了可溶性重组DR5蛋白，证实其能够与TRAIL结合并增强肿瘤细胞对凋亡信号的敏感性，在体外实验中显著抑制多种癌细胞系的增殖。
2. **文献名称**: *"Structural and functional analysis of the interaction between TRAIL and its receptors DR4 and DR5"*
**作者**: Hymowitz SG, et al.
**摘要**: 通过晶体结构分析揭示了TRAIL与DR4/DR5受体的结合机制，重组DR5蛋白的结构研究表明其通过特异性氨基酸残基与配体相互作用，为靶向药物设计提供了结构基础。
3. **文献名称**: *"Targeted delivery of recombinant DR5 fusion proteins for enhanced apoptosis in tumor cells"*
**作者**: Kelley SK, et al.
**摘要**: 研究构建了DR5与抗体片段的重组融合蛋白，证明其能特异性靶向肿瘤细胞并激活凋亡通路，动物实验显示显著抑制肿瘤生长且毒性较低。
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这些研究涵盖了重组Tnfrsf10b蛋白的功能验证、结构解析及治疗应用，可作为相关领域的参考。如需具体文献年份或期刊信息，建议通过PubMed或Web of Science进一步查询。
Tnfrsf10b, also known as TRAIL-R2 or DR5. is a cell surface receptor belonging to the tumor necrosis factor receptor superfamily (TNFRSF). It plays a critical role in apoptosis by binding to its ligand, TNF-related apoptosis-inducing ligand (TRAIL). Upon activation, Tnfrsf10b recruits adaptor proteins like FADD, initiating caspase cascades that trigger programmed cell death. This pathway is essential for immune surveillance, tissue homeostasis, and tumor suppression, as many cancer cells overexpress Tnfrsf10b while remaining sensitive to TRAIL-induced apoptosis.
Recombinant Tnfrsf10b protein is engineered in vitro using expression systems such as mammalian cells or *E. coli* to produce soluble, functional forms of the receptor. These proteins typically include extracellular domains responsible for ligand binding but exclude transmembrane regions to enhance solubility. Purification methods like affinity chromatography ensure high purity and bioactivity. Researchers utilize recombinant Tnfrsf10b to study receptor-ligand interactions, apoptosis signaling mechanisms, and resistance patterns in cancer models. Its ability to compete with membrane-bound receptors for TRAIL binding also makes it a tool for modulating apoptotic responses in experimental settings.
In therapeutic contexts, Tnfrsf10b-targeted agents, including agonistic antibodies and TRAIL fusion proteins, are explored for cancer treatment. However, challenges like variable tumor sensitivity and off-target effects drive the need for recombinant proteins to optimize drug candidates. Additionally, recombinant Tnfrsf10b serves as a biomarker in studies linking receptor expression levels to disease progression or therapeutic outcomes. Its dual role as a death receptor and immune modulator underscores its relevance in both oncology and autoimmune disease research. Ongoing studies focus on improving receptor clustering strategies and combination therapies to overcome resistance mechanisms in malignant cells.
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