| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Trx2 |
| Uniprot No | P10202 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-318aa |
| 氨基酸序列 | MLADGFETDIAIPSGISRPDAAALQRCEGRVVFLPTIRRQLTLADVAHESFVSGGVSPDTLGLLLAYRRRFPAVITRVLPTRIVACPLDVGLTHAGTVNLRNTSPVDLCNGDPISLVPPVFEGQATDVRLDSLDLTLRFPVPLPSPLAREIVARLVARGIRDLNPSPRNPGGLPDLNVLYYNGSRLSLLADVQQLGPVNAELRSLVLNMVYSITEGTTIILTLIPRLFALSAQDGYVNALLQMQSVTREAAQLIHPEAPALMQDGERRLPLYEALVAWLTHAGQLGDTLALAPVVRVCTFDGAAVVRSGDMAPVIRYP |
| 预测分子量 | 41.2 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Trx2重组蛋白的3篇参考文献示例(内容为虚构，仅作格式参考)：
1. **《Recombinant Trx2 protein expression and antioxidant activity analysis》**
*作者：Zhang L et al.*
摘要：研究报道了通过大肠杆菌系统高效表达重组Trx2蛋白的工艺，并验证其清除活性氧(ROS)的能力，证明其在线粒体氧化应激保护中的潜在应用价值。
2. **《Trx2 recombinant protein mitigates myocardial ischemia-reperfusion injury in rats》**
*作者：Chen Y et al.*
摘要：通过动物实验证明，外源性重组Trx2蛋白可减轻心肌缺血再灌注损伤，机制涉及抑制线粒体途径凋亡及调节ASK1-JNK信号通路。
3. **《Engineering a Trx2-based fusion protein for targeted drug delivery》**
*作者：Wang H et al.*
摘要：利用重组Trx2蛋白的稳定性与穿透性，构建靶向肿瘤细胞的融合药物载体，显著提高了化疗药物在细胞内的富集效率并降低毒副作用。
注：以上文献信息为模拟示例，实际研究中需以真实发表的论文为准。建议通过PubMed或Web of Science检索关键词"recombinant Trx2"获取具体文献。
**Background of Trx2 Recombinant Protein**
Thioredoxin-2 (Trx2) is a mitochondrial-specific member of the thioredoxin family, a class of small redox proteins critical for maintaining cellular redox homeostasis. Trx2 plays a pivotal role in regulating mitochondrial antioxidant defense systems, apoptosis, and cellular survival. Unlike its cytosolic counterpart, Trx1. Trx2 is localized exclusively in mitochondria, where it participates in scavenging reactive oxygen species (ROS) and repairing oxidative damage to proteins, lipids, and DNA. Structurally, Trx2 contains a conserved CXXC active site motif, enabling its redox activity through dithiol-disulfide exchange reactions.
The significance of Trx2 extends to its interaction with mitochondrial proteins, including peroxiredoxin-3 and apoptosis-inducing factor (AIF), to modulate redox signaling and cell death pathways. Dysregulation of Trx2 has been implicated in various pathologies, such as neurodegenerative disorders, cardiovascular diseases, and cancer, highlighting its therapeutic potential. Recombinant Trx2 protein, produced via genetic engineering in bacterial (e.g., *E. coli*) or eukaryotic expression systems, retains the native protein's functional properties. This recombinant form is widely used in research to study mitochondrial oxidative stress mechanisms, screen antioxidant therapies, and explore mitochondrial dysfunction in disease models.
Advances in recombinant technology have enabled high-yield purification of Trx2. often incorporating tags like His-tag for affinity chromatography. Its application in preclinical studies, including neuroprotection and ischemia-reperfusion injury models, underscores its relevance in translational medicine. Continued research on Trx2 aims to elucidate its role in aging, metabolic regulation, and as a biomarker for mitochondrial health, driving innovation in redox biology and therapeutic development.
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