| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFS6 |
| Uniprot No | O75380 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-124aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSFGVRVSP TGEKVTHTGQ VYDDKDYRRI RFVGRQKEVN ENFAIDLIAE QPVSEVETRV IACDGGGGAL GHPKVYINLD KETKTGTCGY CGLQFRQHHH |
| 预测分子量 | 13 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NDUFS6重组蛋白的3篇参考文献及其摘要概述：
1. **文献名称**：*Structural and Functional Analysis of Human NDUFS6 in Complex I Assembly*
**作者**：Smith A, et al.
**摘要**：本研究通过重组表达人源NDUFS6蛋白，结合X射线晶体学解析其三维结构，揭示了其在线粒体复合体I组装中的关键作用，并验证了特定突变对复合体酶活性的影响。
2. **文献名称**：*Recombinant NDUFS6 Rescues Mitochondrial Dysfunction in Cellular Models*
**作者**：Chen L, et al.
**摘要**：利用重组NDUFS6蛋白在NDUFS6缺陷的细胞模型中进行功能回补实验，证明其可恢复复合体I的活性并改善线粒体呼吸缺陷，为相关遗传性线粒体疾病的治疗提供依据。
3. **文献名称**：*Cloning and Expression of NDUFS6 in E. coli: Implications for Disease Pathogenesis*
**作者**：Wang Y, et al.
**摘要**：报道了在大肠杆菌中高效表达重组NDUFS6蛋白的方法，通过体外实验验证其与复合体I其他亚基的相互作用，并探讨了NDUFS6突变导致Leigh综合征的分子机制。
(注：上述文献为示例性内容，实际引用需以具体论文为准。)
NDUFS6 (NADH:ubiquinone oxidoreductase core subunit S6) is a critical component of mitochondrial complex I, the largest enzyme in the electron transport chain (ETC) responsible for oxidative phosphorylation. This nuclear-encoded protein plays an essential role in assembling and stabilizing complex I’s structure, facilitating the transfer of electrons from NADH to ubiquinone. Mutations in the NDUFS6 gene are associated with mitochondrial disorders, including Leigh syndrome and other neurodegenerative conditions characterized by energy deficiency in high-demand tissues like the brain and muscles.
Recombinant NDUFS6 protein is engineered through molecular cloning techniques, typically expressed in bacterial (e.g., E. coli) or eukaryotic systems (e.g., mammalian cell lines) to study its function, interactions, and pathological mechanisms. Its production enables researchers to investigate complex I deficiencies at a molecular level, model disease-causing mutations, and screen potential therapeutic compounds. Structural studies using recombinant NDUFS6 help map binding sites and conformational changes critical for enzyme activity.
Challenges in producing functional recombinant NDUFS6 include maintaining proper protein folding, preserving post-translational modifications (e.g., phosphorylation), and ensuring integration into in vitro complex I models. Despite these hurdles, recombinant NDUFS6 serves as a vital tool for developing gene therapies, enzyme replacement strategies, and diagnostic assays for mitochondrial diseases. Recent advances in cryo-EM and gene-editing technologies have further enhanced its utility in deciphering complex I dysfunction and exploring precision medicine approaches.
×
