| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFB2 |
| Uniprot No | O95178 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 34-105 aa |
| 活性数据 | AGGGVHI EPRYRQFPQL TRSQVFQSEF FSGLMWFWIL WRFWHDSEEV LGHFPYPDPS QWTDEELGIP PDDED |
| 分子量 | 12.0 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人NDUFB2蛋白的参考文献，按研究主题分类整理：
---
### 1. **《NDUFB2 mutations alter complex I assembly and mitochondrial respiration》**
**作者**: Vogel et al. (2017)
**摘要**：研究利用重组表达系统(如大肠杆菌)解析NDUFB2在线粒体复合物I组装中的作用，发现其突变会导致复合物I功能障碍，可能与脑肌病相关。通过酵母敲除模型验证其对电子传递链的影响。
---
### 2. **《Structural characterization of recombinant human NDUFB2 and its role in oxidative phosphorylation》**
**作者**: Smith et al. (2015)
**摘要**：通过杆状病毒-昆虫细胞系统重组表达NDUFB2.结合X射线晶体学解析其三维结构，揭示了其与复合物I其他亚基的相互作用界面，为药物靶点设计提供结构基础。
---
### 3. **《Functional reconstitution of NDUFB2 in a cell-free system to study mitochondrial complex I deficiency》**
**作者**: Tanaka et al. (2020)
**摘要**：建立体外重组体系，证明NDUFB2缺失导致复合物I活性下降及ROS累积，为遗传性线粒体疾病的分子机制提供实验依据。
---
### 4. **《Overexpression of recombinant NDUFB2 enhances mitochondrial metabolism in cancer cells》**
**作者**: Chen et al. (2019)
**摘要**：在HeLa细胞中过表达重组NDUFFB2.发现其通过促进复合物I活性增强癌细胞有氧代谢，提示其在肿瘤代谢重编程中的潜在作用。
---
**注**：以上文献均为虚拟示例，实际研究中建议通过PubMed或Web of Science以关键词"recombinant NDUFB2"或"NDUFB2 complex I"检索最新文献。近期研究可能聚焦于其与神经退行性疾病(如帕金森病)或癌症代谢的关联。
The recombinant human NADH:ubiquinone oxidoreductase subunit B2 (NDUFB2) protein is a critical component of mitochondrial Complex I (NADH dehydrogenase), the largest enzyme complex in the electron transport chain. Complex I facilitates the transfer of electrons from NADH to ubiquinone, coupled with proton translocation across the inner mitochondrial membrane, which drives ATP synthesis. NDUFB2. encoded by the nuclear genome, is a highly conserved iron-sulfur (Fe-S) cluster-binding subunit involved in stabilizing Complex I’s structure and maintaining its enzymatic activity. Mutations or dysregulation of NDUFB2 are linked to mitochondrial disorders, neurodegenerative diseases, and cancer due to disrupted oxidative phosphorylation (OXPHOS) and elevated oxidative stress. Recombinant NDUFB2 is typically produced using expression systems like Escherichia coli or mammalian cells, enabling studies on its structural role, interactions with other Complex I subunits, and mechanisms underlying pathological variants. Its production supports functional assays, drug discovery for mitochondrial diseases, and exploration of metabolic reprogramming in cancer. Research on recombinant NDUFB2 enhances understanding of cellular bioenergetics and provides therapeutic insights for conditions associated with mitochondrial dysfunction.
×
