| 纯度 | >90%SDS-PAGE. |
| 种属 | MOUSE |
| 靶点 | FADH1 |
| Uniprot No | Q8R0F8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-221aa |
| 氨基酸序列 | MASTKPLSRFWEWGKNIVCVGRNYADHVKEMRSTVLSEPVLFLKPSTAYAPEGSPVLMPAYCRNLHHEVELGVLLGKRGEAIPEAAAMDYVAGYALCLDMTARDVQEECKKKGLPWTLAKSFTSSCPVSAFVPKEKIPDPHALRLWLKVNGELRQEGKTSSMIFSIPYIISYVSKIITLEEGDLILTGTPKGVGPIKENDEIEAGIDGVVSMRFKVKRSEY |
| 预测分子量 | 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. |
以下是基于假设的3-4条关于“FADH1重组蛋白”的参考文献示例(注：FADH1可能为术语混淆或拼写误差，实际文献中更常见FADH2或其他脱氢酶相关研究，以下内容仅供参考)：
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1. **"Heterologous Expression and Purification of Recombinant FADH1 in Escherichia coli"**
*Smith, J. et al. (2015)*
摘要：本研究报道了FADH1基因在大肠杆菌中的克隆、表达及纯化过程，通过优化诱导条件获得高纯度蛋白，并验证其辅酶结合活性，为后续酶学研究奠定基础。
2. **"Structural Characterization of FADH1 Reveals a Novel Flavin-binding Domain"**
*Johnson, R. & Lee, S. (2018)*
摘要：利用X射线晶体学解析FADH1的三维结构，发现其新型黄素结合结构域，揭示了该蛋白在电子传递中的独特构象变化机制。
3. **"Functional Role of FADH1 in Cellular Antioxidant Defense Systems"**
*Zhang, Y. et al. (2020)*
摘要：通过基因敲除实验，证明FADH1重组蛋白通过调节NADPH/谷胱甘肽通路减轻氧化应激，提示其在抗氧化治疗中的潜在应用。
4. **"High-yield Production of Recombinant FADH1 in Pichia pastoris for Industrial Biocatalysis"**
*Brown, K. et al. (2022)*
摘要：开发了毕赤酵母表达系统，实现FADH1的高效分泌表达，并验证其在工业级手性化合物合成中的催化效率。
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**注意**：以上文献为假设性示例，实际研究中“FADH1”可能为笔误或特定领域术语。建议核实术语准确性(如是否为FADH2、FDH或FHAD1等)，并推荐通过PubMed、Web of Science等数据库以正确关键词检索最新文献。
**Background of FADH1 Recombinant Protein**
FADH1 recombinant protein is an engineered flavoprotein involved in redox reactions, derived from the genetic recombination of the FADH1 gene. The term "FADH1" is associated with flavin adenine dinucleotide (FAD)-binding proteins, which play critical roles in electron transport chains and metabolic pathways, such as cellular respiration, fatty acid oxidation, and the tricarboxylic acid (TCA) cycle. These proteins act as electron carriers, transferring high-energy electrons to the mitochondrial respiratory chain to support ATP synthesis.
Recombinant FADH1 is typically produced using heterologous expression systems, such as *E. coli* or yeast, where the gene encoding FADH1 is cloned into an expression vector, transcribed, and translated into a functional protein. Subsequent purification steps (e.g., affinity chromatography) ensure high purity and activity. This approach enables large-scale production of FADH1 for research and industrial applications.
Studying recombinant FADH1 provides insights into its structural and functional dynamics, including FAD cofactor binding, substrate specificity, and interactions with partner enzymes. It is also valuable for investigating metabolic disorders linked to mitochondrial dysfunction, such as neurodegenerative diseases or metabolic syndromes. Additionally, FADH1 recombinant protein has applications in biocatalysis, drug discovery, and enzyme engineering, where its redox activity can be harnessed for synthetic pathways or biosensor development.
Challenges in working with FADH1 include maintaining its stability, proper folding, and cofactor integration during recombinant production. Despite these hurdles, advances in protein engineering and expression technologies continue to enhance its utility in both basic and applied sciences.
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