纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | NDUFV2 |
Uniprot No | P19404 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 33-249aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSGAGGALF VHRDTPENNP DTPFDFTPEN YKRIEAIVKN YPEGHKAAAV LPVLDLAQRQ NGWLPISAMN KVAEVLQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK VGETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTAK DIEEIIDELK AGKIPKPGPR SGRFSCEPAG GLTSLTEPPK GPGFGVQAGL |
预测分子量 | 26 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NDUFV2重组蛋白的示例参考文献(内容为假设性概括,建议通过学术数据库验证具体文献):
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1. **文献名称**: *Structural Insights into Human NDUFV2 Assembly in Mitochondrial Complex I*
**作者**: Smith A, et al.
**摘要**: 本研究通过重组表达人源NDUFV2蛋白,结合X射线晶体学分析其三维结构,揭示了其在复合物I中的核心作用,并探讨了其与辅酶Q结合的分子机制。
2. **文献名称**: *Recombinant NDUFV2 Expression and Functional Analysis in Leigh Syndrome Models*
**作者**: Chen L, et al.
**摘要**: 利用大肠杆菌系统表达重组NDUFV2蛋白,研究其在Leigh综合征患者细胞模型中的功能缺失,发现其突变导致线粒体复合物I活性下降及ROS生成增加。
3. **文献名称**: *High-Yield Purification of Recombinant NDUFV2 for Drug Screening*
**作者**: Gupta R, et al.
**摘要**: 开发了一种高效的真核表达系统(HEK293细胞)用于NDUFV2重组蛋白的纯化,并验证其在针对线粒体疾病的小分子药物筛选中的应用潜力。
4. **文献名称**: *NDUFV2 Mutations Alter Electron Transfer Efficiency: Evidence from Recombinant Protein Studies*
**作者**: Tanaka K, et al.
**摘要**: 通过体外重组NDUFV2蛋白与复合物I亚基的互作实验,证明特定突变会破坏电子传递链的稳定性,导致ATP合成障碍,为相关神经退行性疾病提供机制解释。
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**说明**:以上文献信息为示例性概括,实际研究中需通过PubMed、Web of Science等平台检索具体文献。建议结合关键词“NDUFV2 recombinant protein”、“complex I assembly”或“mitochondrial disorders”进一步筛选。
**Background of NDUFV2 Recombinant Protein**
NDUFV2 (NADH:ubiquinone oxidoreductase core subunit V2) is a critical component of mitochondrial Complex I (NADH:ubiquinone oxidoreductase), the first and largest enzyme in the electron transport chain (ETC). Complex I facilitates ATP production by catalyzing the transfer of electrons from NADH to ubiquinone, coupled with proton translocation across the mitochondrial inner membrane. NDUFV2. located in the hydrophilic matrix arm of Complex I, plays a pivotal role in electron transfer through its involvement in binding NADH and coordinating iron-sulfur (Fe-S) clusters.
Recombinant NDUFV2 protein is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional versions of the subunit for *in vitro* studies. This tool enables researchers to explore the structural and mechanistic details of Complex I assembly, electron transport efficiency, and interactions with ancillary proteins. Dysfunction of NDUFV2. due to mutations or altered expression, is linked to severe mitochondrial disorders, such as Leigh syndrome, neurodegenerative diseases, and cardiomyopathies, underscoring its importance in cellular energy homeostasis.
Studies leveraging recombinant NDUFV2 have advanced understanding of disease pathogenesis, facilitated drug screening for mitochondrial disorders, and supported structural analyses (e.g., cryo-EM) to resolve Complex I architecture. Ongoing research aims to elucidate how NDUFV2 mutations disrupt ETC activity and contribute to metabolic and neurological pathologies, offering potential therapeutic targets. The recombinant protein thus serves as a vital resource for both basic and translational investigations into mitochondrial biology and energy-related diseases.
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