| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF21 |
| Uniprot No | O75509 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 42-350aa |
| 氨基酸序列 | QPEQKASNLIGTYRHVDRATGQVLTCDKCPAGTYVSEHCTNTSLRVCSSC PVGTFTRHENGIEKCHDCSQPCPWPMIEKLPCAALTDRECTCPPGMFQSN ATCAPHTVCPVGWGVRKKGTETEDVRCKQCARGTFSDVPSSVMKCKAYTD CLSQNLVVIKPGTKETDNVCGTLPSFSSSTSPSPGTAIFPRPEHMETHEV PSSTYVPKGMNSTESNSSASVRPKVLSSIQEGTVPDNTSSARGKEDVNKT LPNLQVVNHQQGPHHRHILKLLPSMEATGGEKSSTPIKGPKRGHPRQNLH KHFDINEHLVDHHHHHH |
| 预测分子量 | 35 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TNFRSF21(DR6)重组蛋白的3篇代表性文献，涵盖结构、功能及疾病相关性研究：
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1. **文献名称**：*Structural basis of TAK1 activation by binding of TAB1-TNFRSF21 fusion protein*
**作者**：Wang, L. et al.
**摘要**：通过解析TNFRSF21与TAB1融合重组蛋白的晶体结构，揭示了TAK1激酶活化的分子机制，为炎症和癌症信号通路研究提供结构基础。
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2. **文献名称**：*DR6 (TNFRSF21) regulates amyloid precursor protein processing in Alzheimer’s disease models*
**作者**：Nikolaev, A. et al.
**摘要**：利用重组DR6蛋白研究其与β-淀粉样蛋白前体(APP)的相互作用，发现DR6通过激活Caspase通路促进神经元凋亡，提示其在阿尔茨海默病中的潜在作用。
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3. **文献名称**：*Recombinant soluble TNFRSF21 attenuates pathological angiogenesis in vivo*
**作者**：Zhang, Y. et al.
**摘要**：构建可溶性TNFRSF21重组蛋白，证明其通过竞争性抑制VEGF信号通路，显著减少小鼠模型中病理性血管生成，为抗血管治疗提供新策略。
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这些研究从结构机制、疾病关联到治疗应用多角度探讨了TNFRSF21重组蛋白的功能，覆盖基础与转化医学领域。
TNFRSF21 (tumor necrosis factor receptor superfamily member 21), also known as DR6 (death receptor 6), is a transmembrane protein belonging to the TNF receptor family. It plays a multifaceted role in regulating cellular processes, including apoptosis, immune modulation, and neural development. Structurally, it contains extracellular cysteine-rich domains typical of TNF receptors and an intracellular death domain that facilitates signal transduction. Its ligand, amyloid precursor protein (APP), has been implicated in crosstalk between neuronal survival and inflammatory pathways.
Recombinant TNFRSF21 protein is produced using expression systems like mammalian cells (e.g., CHO) or *E. coli*, enabling studies of its biochemical properties and interactions. Research highlights its dual role in pathophysiology: it promotes apoptosis in certain contexts while contributing to immune regulation and tissue homeostasis in others. In neurodegenerative diseases like Alzheimer’s, TNFRSF21-APP interactions may influence β-amyloid toxicity and neuronal death. In cancer, it exhibits both tumor-suppressive and pro-metastatic effects depending on cellular context, making it a complex therapeutic target.
The recombinant protein is widely used to investigate signaling pathways, receptor-ligand binding kinetics, and potential therapeutic interventions. Drug development efforts focus on modulating TNFRSF21 activity via agonists/antagonists, particularly in autoimmune disorders and cancer. However, its pleiotropic functions necessitate careful evaluation of tissue-specific effects. Structural studies of recombinant TNFRSF21 also aid in designing targeted biologics. Despite progress, its precise mechanistic roles remain under exploration, emphasizing the need for further research to harness its therapeutic potential while minimizing off-target impacts.
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