| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TXN |
| Uniprot No | P10599 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-105aa |
| 氨基酸序列 | MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV |
| 预测分子量 | 12 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TXN(硫氧还蛋白)重组蛋白的参考文献示例。**请注意，以下内容为模拟生成的示例，实际文献需通过学术数据库核实**：
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1. **文献名称**：Production and Characterization of Recombinant Human Thioredoxin in *E. coli*
**作者**：Sahaf, B., Rosen, A.
**摘要**：研究报道了在大肠杆菌中高效表达重组人硫氧还蛋白(Trx)的方法，纯化后蛋白显示显著的抗氧化活性，并验证了其在细胞模型中对氧化应激的保护作用。
2. **文献名称**：Recombinant Thioredoxin Suppresses Neuronal Apoptosis in Cerebral Ischemia-Reperfusion Injury
**作者**：Yoshida, T., et al.
**摘要**：通过动物实验证明，重组Trx能减轻脑缺血再灌注损伤中的神经元凋亡，机制涉及抑制线粒体氧化应激和调节凋亡相关蛋白表达。
3. **文献名称**：Yeast-Expressed Recombinant Thioredoxin Maintains Structural Stability and Enzymatic Activity
**作者**：Lundström, J., Holmgren, A.
**摘要**：在酵母系统中成功表达重组Trx，通过晶体学和酶学分析证实其与天然蛋白结构一致，且具备高效的二硫键还原酶活性。
4. **文献名称**：Therapeutic Potential of Recombinant Thioredoxin in Pulmonary Fibrosis
**作者**：Nakamura, H., et al.
**摘要**：在小鼠模型中，重组Trx通过抑制TGF-β信号通路和减少胶原沉积，显著缓解博来霉素诱导的肺纤维化，提示其临床治疗潜力。
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**建议**：如需真实文献，可通过PubMed、Google Scholar等平台搜索关键词(如“recombinant thioredoxin expression”或“thioredoxin therapeutic application”)，并筛选近年高被引研究。
**Background of TXN (Thioredoxin) Recombinant Protein**
Thioredoxin (TXN) is a small, evolutionarily conserved redox-active protein (~12 kDa) central to cellular redox regulation. Naturally present in prokaryotes and eukaryotes, it features a conserved CXXC active site motif that enables its redox activity by catalyzing disulfide bond reduction. TXN operates in tandem with thioredoxin reductase (TrxR) and NADPH, forming the thioredoxin system, which maintains intracellular redox homeostasis, repairs oxidative damage, and regulates signaling pathways.
Recombinant TXN is engineered via genetic cloning, often expressed in *E. coli* or eukaryotic systems, followed by purification (e.g., affinity chromatography with His-tags). Its stability, solubility, and ease of modification make it a versatile tool. In research, recombinant TXN serves as a molecular chaperone to enhance soluble expression of difficult proteins. Industrially, it supports enzyme production and biocatalysis by stabilizing redox-sensitive proteins.
Biomedically, TXN is implicated in diseases linked to oxidative stress, including cancer, neurodegeneration, and inflammation. It regulates transcription factors (e.g., NF-κB, p53), apoptosis, and immune responses. Recombinant TXN is studied for therapeutic applications, such as mitigating chemotherapy-induced side effects or serving as a drug target in cancer. Its antioxidant properties also attract interest in anti-aging and metabolic disorder research.
Overall, TXN recombinant protein bridges fundamental redox biology with translational applications, offering insights into disease mechanisms and biotechnological innovations.
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