| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Trap1 |
| Uniprot No | Q12931 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 60-308aa |
| 氨基酸序列 | STQTAEDKEEPLHSIISSTESVQGSTSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVSDGQALPEMEIHLQTNAEKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLDALQNQAEASSKIIGQFGVGFYSAFMVADRVEVYSRSAAPGSLGYQWLSDGSGVFEIAEASGVRTGTKIIIHLKSDCKEFSSEARVRDVVTKYSNFVSFPLYLNGRRMNTLQAIWMMDPKDVRE |
| 预测分子量 | 54.5kDa |
| 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TRAP1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Mitochondrial chaperone TRAP1 regulates the mitochondrial permeability transition pore in cancer cells*
**作者**：Altieri, D.C., et al.
**摘要**：该研究利用重组TRAP1蛋白，揭示了其在癌细胞线粒体中的分子伴侣功能，证明TRAP1通过调控线粒体通透性转换孔(mPTP)的开放，抑制细胞凋亡，从而增强肿瘤细胞在氧化应激下的存活能力。
2. **文献名称**：*TRAP1-dependent protein folding in the mitochondrial matrix promotes cancer growth and survival*
**作者**：Masuda, Y., et al.
**摘要**：作者通过重组TRAP1蛋白的体外实验，结合癌细胞模型，发现TRAP1参与线粒体基质内关键代谢酶(如SDH和ATP合酶)的折叠，其活性缺失导致线粒体功能紊乱，抑制肿瘤生长。
3. **文献名称**：*Structure-based design of TRAP1-selective inhibitors with anticancer activity*
**作者**：Lavery, L.A., et al.
**摘要**：该研究通过重组表达纯化人源TRAP1蛋白，解析其晶体结构，并基于结构设计出选择性抑制剂。实验表明，这些抑制剂可特异性阻断TRAP1的ATP酶活性，在体内外模型中均表现出抗肿瘤效果。
*注：若需扩展，可补充2018年Kang团队关于TRAP1与神经退行性疾病的研究，涉及重组蛋白在tau蛋白聚集中的作用分析。建议通过PubMed/Google Scholar以“TRAP1 recombinant”+关键词进一步检索最新文献。*
Trap1 (TNF receptor-associated protein 1), also known as HSP75 or TRAP-1. is a mitochondrial chaperone protein belonging to the heat shock protein 90 (HSP90) family. It plays a critical role in maintaining mitochondrial integrity, regulating cellular stress responses, and modulating apoptosis. Initially identified through its interaction with the TNF receptor, Trap1 is primarily localized in the mitochondrial matrix, where it assists in protein folding, stabilizes electron transport chain complexes, and protects against oxidative stress. Its function is closely tied to ATP-dependent conformational regulation of client proteins, including those involved in metabolic reprogramming and survival pathways.
Recombinant Trap1 protein is engineered for in vitro studies to dissect its molecular mechanisms and therapeutic potential. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it retains ATPase activity and chaperone functions, enabling research on its interaction with co-chaperones, client proteins (e.g., cyclophilin D), and inhibitors. Trap1 has garnered attention in cancer biology due to its overexpression in tumors, where it promotes cell survival under hypoxia and chemotherapy resistance by suppressing mitochondrial apoptosis. Conversely, its downregulation is linked to neurodegenerative disorders, highlighting its dual role in health and disease.
Studies using recombinant Trap1 have advanced drug discovery, particularly for HSP90 inhibitors repurposed to target mitochondrial chaperones. Its structural analysis has revealed unique domain arrangements distinct from cytosolic HSP90 isoforms, offering specificity for tailored therapies. Ongoing research aims to clarify Trap1's role in metabolic diseases, aging, and its crosstalk with oncogenic signaling pathways, positioning it as a multifaceted regulator of cellular homeostasis.
×
