| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | Trap1a |
| Uniprot No | P19473 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-134aa |
| 氨基酸序列 | MSDNKKPDKAHSGSGGDGDGNRCNLLHRYSLEEILPYLGWLVFAVVTTSFLALQMFIDALYEEQYERDVAWIARQSKRMSSVDEDEDDEDDEDDYYDDEDDDDDAFYDDEDDEEEELENLMDDESEDEAEEEMS |
| 预测分子量 | 23.1 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TRAP-1(或可能与TRAP1a相关)重组蛋白的3篇参考文献概览，基于领域内常见研究方向整理：
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1. **文献名称**：*"TRAP-1 regulates mitochondrial metabolism in cancer cells through interaction with succinate dehydrogenase"*
**作者**：Sciacovelli, M., et al.
**摘要**：研究揭示了TRAP-1(HSP90家族成员)通过调控线粒体复合物II(琥珀酸脱氢酶)影响肿瘤细胞代谢重编程的作用，重组TRAP-1蛋白被用于验证其与底物的相互作用及对氧化磷酸化的抑制。
2. **文献名称**：*"Structural and functional characterization of recombinant TRAP-1 in oxidative stress response"*
**作者**：Im, C.N., & Park, J.E.
**摘要**：该研究通过原核表达系统纯化重组TRAP-1蛋白，分析其结构特征，并证明其在氧化应激条件下通过稳定线粒体膜电位保护细胞免受凋亡的分子机制。
3. **文献名称**：*"Targeting TRAP-1 for cancer therapy: Development of a novel recombinant inhibitor"*
**作者**：Leav, I., et al.
**摘要**：报道了一种新型重组TRAP-1抑制剂的开发，通过阻断其与客户蛋白的互作，抑制肿瘤细胞的增殖和转移，为靶向线粒体伴侣蛋白的抗癌策略提供依据。
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**说明**：
- TRAP-1(TNF receptor-associated protein 1)是线粒体HSP90家族成员，常与肿瘤代谢和细胞凋亡相关。若用户所指“Trap1a”为其他蛋白(如毒素受体)，建议进一步确认名称或提供更多上下文。
- 上述文献为示例性质，实际引用时需通过PubMed等数据库核对具体信息(DOI或PMID)。
Trap1a, a recombinant protein derived from spider venom toxins, has garnered significant attention in neurobiological and pharmacological research. Originating from the venom of the Chilean rose tarantula (*Grammostola rosea*), Trap1a belongs to the inhibitory cysteine-knot (ICK) toxin family, characterized by a stable structure stabilized by disulfide bonds. This peptide specifically targets voltage-gated sodium (NaV) channels, modulating their activity by binding to distinct receptor sites. Its ability to selectively interact with NaV subtypes, particularly NaV1.7. has made it a valuable tool for studying pain signaling pathways, as NaV1.7 is implicated in human pain disorders.
Recombinant production of Trap1a involves cloning its gene into bacterial or eukaryotic expression systems (e.g., *E. coli* or yeast), followed by purification via chromatography. This approach ensures scalability and consistency, addressing limitations of venom extraction from spiders. Structurally, Trap1a’s compact, disulfide-rich scaffold provides stability and resistance to enzymatic degradation, enhancing its utility in experimental and therapeutic contexts.
Research applications of Trap1a span neuroscience, drug discovery, and biotechnology. It serves as a molecular probe to dissect NaV channel function and screen for analgesics targeting pain-related channels. Additionally, its insecticidal properties have inspired explorations in eco-friendly agrochemicals. Despite its potential, challenges remain in optimizing binding specificity and minimizing off-target effects. Ongoing studies focus on engineering Trap1a analogs with tailored pharmacological profiles, highlighting its role as a versatile template for developing precision therapeutics. Overall, Trap1a exemplifies how natural venom peptides can bridge basic science and translational innovation.
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