| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRPV1 |
| Uniprot No | Q8NER1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-124aa |
| 氨基酸序列 | CPDPLDGDPNSRPPPAKPQLSTAKSRTRLFGKGDSEEAFPVDCPHEEGEL DSCPTITVSPVITIQRPGDGPTGARLLSQDSVAASTEKTLRLYDRRSIFE AVAQ |
| 预测分子量 | 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TRPV1重组蛋白的3篇经典文献摘要概括，涵盖结构解析、功能研究和表达系统开发方向：
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1. **文献名称**：*Structure of the TRPV1 ion channel determined by electron cryo-microscopy*
**作者**：Liao, M., Cao, E., Julius, D., & Cheng, Y. (2013)
**摘要**：本研究利用冷冻电镜技术解析了重组TRPV1蛋白(在HEK293细胞中表达并纯化)的近原子分辨率结构，揭示了其四聚体构象和辣椒素结合位点，阐明了温度与配体激活通道的分子机制。
2. **文献名称**：*TRPV1 structures in distinct conformations reveal activation mechanisms*
**作者**：Cao, E., Liao, M., Cheng, Y., & Julius, D. (2013)
**摘要**：通过重组TRPV1蛋白的结构分析，比较了其开放/关闭状态构象差异，发现细胞膜内S4-S5 linker区域在门控过程中的关键作用，为药物设计提供了结构基础。
3. **文献名称**：*The capsaicin receptor: a heat-activated ion channel in the pain pathway*
**作者**：Caterina, M.J., Schumacher, M.A., Tominaga, M., Rosen, T.A., & Julius, D. (1997)
**摘要**：首次克隆并重组表达了TRPV1基因(通过非洲爪蟾卵母细胞和哺乳动物细胞系统)，证实其可被辣椒素、热(>43°C)及质子激活，奠定了TRPV1作为痛觉传感器的理论基础。
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以上研究均涉及重组TRPV1蛋白的应用，包括表达纯化、结构生物学及功能验证，是领域内的重要参考文献。
TRPV1 (Transient Receptor Potential Vanilloid 1) is a non-selective cation channel belonging to the TRP superfamily, widely expressed in sensory neurons and non-neuronal tissues. It functions as a polymodal receptor activated by diverse stimuli, including capsaicin (the pungent compound in chili peppers), noxious heat (>43°C), acidic pH, and endogenous lipid mediators. TRPV1 plays a central role in detecting and integrating thermal, chemical, and inflammatory pain signals, making it a critical target for pain management research.
Recombinant TRPV1 proteins are engineered in heterologous expression systems (e.g., HEK293 cells, insect cells) to study its structure-function relationships, ligand interactions, and regulatory mechanisms. Purified recombinant TRPV1 retains its ability to form functional homotetramers, enabling in vitro studies such as electrophysiology (patch-clamp) and structural analysis (cryo-EM). These tools have revealed key domains involved in channel gating, including the ankyrin repeat region, transmembrane helices, and ligand-binding pockets.
Research on recombinant TRPV1 has advanced drug discovery, particularly for chronic pain, neuroinflammation, and cancer. However, challenges persist due to its complex modulation by phosphorylation, desensitization, and interactions with intracellular proteins. Efforts to develop TRPV1 antagonists have been hampered by side effects like hyperthermia, highlighting the need for tissue-specific targeting. Overall, recombinant TRPV1 remains a vital tool for deciphering nociception mechanisms and designing novel analgesics.
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