Recombinant Human TXNRD1 protein

中文名： 硫氧还原蛋白还原酶1(TXNRD1)重组蛋白
别名： TXNRD1；GRIM12；Thioredoxin reductase 1, cytoplasmic

货号: PA1000-3347

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	TXNRD1
Uniprot No	Q16881-5
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	2-499aa
氨基酸序列	MASMTGGQQMGRGHHHHHHENLYFQGGEFNGPEDLPKSYDYDLIIIGGGS GGLAAAKEAAQYGK KVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLM HQAALLGQALQDSRNYGWKVEETVKHDWDR MIEAVQNHIGSLNWGYRV ALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGER PR YLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDV TVMVRSILLRGF DQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTP GRLRVVAQSTNSEEIIEGEYNTVMLAIG RDACTRKIGLETVGVKINEK TGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQR LYAG STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLE WTIPSRDNNK CYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKC GLTKKQLDSTIGIHPVCAEVFTTLSV TKRSGASILQAGCUG
预测分子量	58 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

以下是关于TXNRD1重组蛋白的3篇代表性文献的简要信息(文献为示例性质，实际引用时请核实原文)：

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1. **文献名称**: *Structural insights into human thioredoxin reductase 1-based inhibition by natural product curcumin*

**作者**: Cheng Q, et al.

**摘要**: 该研究解析了人源TXNRD1重组蛋白的晶体结构，并探讨了姜黄素对其酶活性的抑制作用，揭示了天然产物靶向TXNRD1的分子机制，为抗氧化和抗癌药物开发提供依据。

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2. **文献名称**: *Recombinant expression and functional characterization of thioredoxin reductase 1 in cancer cell redox homeostasis*

**作者**: Arnér ESJ, et al.

**摘要**: 通过大肠杆菌表达系统获得高纯度TXNRD1重组蛋白，证明其在维持癌细胞氧化还原平衡中的关键作用，并验证其作为化疗增敏靶点的潜力。

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3. **文献名称**: *Targeting TXNRD1 in cancer therapy: Insights from recombinant protein-based drug screening*

**作者**: Duan L, et al.

**摘要**: 利用重组TXNRD1蛋白进行高通量药物筛选，发现多个小分子抑制剂可选择性抑制其活性，为靶向TXNRD1的抗癌策略提供实验基础。

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**备注**：以上文献信息为模拟示例，实际研究中建议通过PubMed或Web of Science以“TXNRD1 recombinant”为关键词检索最新论文，重点关注其重组表达方法、结构功能研究或疾病应用方向。

背景信息

**Background of TXNRD1 Recombinant Protein**

Thioredoxin reductase 1 (TXNRD1) is a selenocysteine-containing oxidoreductase central to maintaining cellular redox homeostasis. As a key component of the thioredoxin (Trx) system, TXNRD1 catalyzes the reduction of oxidized thioredoxin using NADPH as an electron donor, thereby regulating processes like DNA synthesis, antioxidant defense, and signal transduction. Its role in mitigating oxidative stress links it to numerous physiological and pathological conditions, including cancer, neurodegeneration, and inflammatory diseases. Dysregulation of TXNRD1 is often associated with increased oxidative damage and disease progression.

Recombinant TXNRD1 protein is engineered through genetic cloning, typically expressed in *E. coli* or mammalian systems to ensure proper folding and selenocysteine incorporation, critical for enzymatic activity. Purification methods, such as affinity chromatography, yield high-purity protein for functional studies. Researchers utilize recombinant TXNRD1 to investigate its enzymatic mechanisms, redox interactions, and role in cellular pathways. It serves as a tool for screening inhibitors or activators, aiding drug development targeting diseases with redox imbalances.

In cancer research, TXNRD1 overexpression in tumors highlights its potential as a therapeutic target. Inhibitors of TXNRD1. such as auranofin, are explored for their antitumor effects. Additionally, recombinant TXNRD1 aids in studying resistance to oxidative therapies and elucidating its interplay with other antioxidant systems like glutathione. Structural studies using recombinant protein variants (e.g., mutant or truncated forms) further dissect its catalytic domains and regulatory mechanisms.

Overall, TXNRD1 recombinant protein is vital for advancing understanding of redox biology and developing therapies for diseases linked to oxidative stress. Its applications span biochemistry, molecular medicine, and pharmacology, underscoring its significance in both basic and translational research.