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Recombinant Human TRPV3 protein

  • 中文名: 转化受体电位阳离子通道亚家族V成员3(TRPV3)重组蛋白
  • 别    名: TRPV3;Transient receptor potential cation channel subfamily V member 3
货号: PA2000-508DB
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点TRPV3
Uniprot No Q8NET8
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-790aa
氨基酸序列MKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTSPPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLKKRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNINPNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGADVNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNILHALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYILSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEMLTLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMGWLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLGFGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGELCKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTDFNKIQDSSRNNSKTTLNAFEEVEEFPETSV
预测分子量 93.1 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.

参考文献

以下是3篇关于TRPV3重组蛋白研究的参考文献及其摘要概括:

1. **文献名称**: "Structure of human TRPV3 in the closed state"

**作者**: Xu, H., et al. (2022)

**摘要**: 该研究通过冷冻电镜解析了人源TRPV3重组蛋白在关闭状态下的高分辨率结构,揭示了其跨膜区门控机制及与脂质分子的相互作用,为理解其温度敏感性和疾病相关突变提供结构基础。

2. **文献名称**: "TRPV3 mediates temperature-dependent keratinocyte proliferation in skin"

**作者**: Luo, J., et al. (2018)

**摘要**: 利用重组TRPV3蛋白和基因敲除模型,发现TRPV3通过感知生理温度变化调控角质形成细胞的钙内流,进而影响皮肤屏障功能,提示其在特应性皮炎等疾病中的潜在作用。

3. **文献名称**: "A synthetic small molecule targeting TRPV3 for topical analgesia"

**作者**: Smith, G.D., et al. (2020)

**摘要**: 研究通过高通量筛选鉴定了可特异性激活重组TRPV3通道的小分子化合物,证明其局部应用可通过调节痛觉神经元活性缓解炎症性疼痛,为开发新型镇痛药物提供依据。

(注:以上文献信息为示例性质,具体发表年份及作者请以实际文献为准。)

背景信息

TRPV3 (Transient Receptor Potential Vanilloid 3) is a temperature-sensitive, calcium-permeable ion channel belonging to the TRP family. It is primarily expressed in epithelial tissues, including skin keratinocytes, oral mucosa, and the gastrointestinal tract, where it functions as a molecular sensor for warm temperatures (33–39°C). Beyond thermosensation, TRPV3 participates in diverse physiological processes such as skin barrier formation, hair growth, itch transduction, and inflammatory responses. Its dysfunction has been linked to skin disorders (e.g., Olmsted syndrome, pruritus), chronic pain, and neurodegenerative conditions.

Recombinant TRPV3 proteins are engineered in heterologous expression systems (e.g., HEK293 cells, Xenopus oocytes) to study channel structure-function relationships, ligand interactions, and regulatory mechanisms. The full-length protein contains six transmembrane domains, cytoplasmic N- and C-termini, and a pore-forming loop between the fifth and sixth domains. Post-translational modifications (e.g., glycosylation) and lipid microenvironment critically influence its gating behavior and thermal sensitivity.

Research on recombinant TRPV3 has accelerated since its cryo-EM structure was resolved (2018), revealing distinct conformational states and potential drug-binding pockets. These proteins enable high-throughput screening of agonists/antagonists for therapeutic development, particularly targeting inflammatory skin diseases and neuropathic pain. However, challenges persist in maintaining native-like channel properties during recombinant expression, as TRPV3 exhibits sensitization upon repeated activation—a hallmark feature complicating in vitro studies. Current efforts focus on optimizing purification protocols and developing membrane mimetics to preserve functional stability.

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