| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LIAS |
| Uniprot No | O43766 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-372aa |
| 氨基酸序列 | LSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKRKTKDL |
| 预测分子量 | 45.8 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3篇关于LIAS(硫辛酸合成酶)重组蛋白研究的参考文献示例(注：文献信息为模拟生成，仅供参考)：
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1. **标题**：*Heterologous Expression and Functional Characterization of Recombinant Human Lipoic Acid Synthase*
**作者**：Zhang, Y. et al.
**摘要**：研究通过在大肠杆菌中异源表达人源LIAS重组蛋白，优化纯化条件并验证其催化硫辛酸合成的酶活性，为体外研究硫辛酸代谢提供工具。
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2. **标题**：*Crystal Structure of Bacterial LIAS Reveals Key Residues for Iron-Sulfur Cluster Binding*
**作者**：Tanaka, K. et al.
**摘要**：解析了细菌来源的LIAS蛋白晶体结构，阐明其依赖铁硫簇的催化机制，为设计针对LIAS的抑制剂奠定结构基础。
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3. **标题**：*Recombinant LIAS Supplementation Ameliorates Metabolic Dysfunction in Cellular Models of Mitochondrial Disease*
**作者**：Gomez, M. et al.
**摘要**：通过体外实验证明重组LIAS蛋白可恢复线粒体疾病细胞模型的硫辛酸水平，改善能量代谢异常，提示其潜在治疗价值。
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4. **标题**：*High-Yield Production of Recombinant LIAS in Yeast for Industrial Applications*
**作者**：Wang, L. et al.
**摘要**：开发了基于毕赤酵母的重组LIAS高效表达系统，实现低成本规模化生产，为食品或医药工业中硫辛酸的生物合成提供新策略。
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**提示**：实际文献需通过PubMed/Web of Science等平台以关键词“LIAS recombinant protein”或“lipoic acid synthase expression”检索，并筛选近年研究(如2018-2023)。部分相关领域期刊包括*Biochimie*、*Protein Expression and Purification*及*Metabolic Engineering*。
Lipoic acid synthase (LIAS) is a key enzyme involved in the biosynthesis of lipoic acid, a essential cofactor for mitochondrial enzymes in energy metabolism and antioxidant defense. LIAS catalyzes the final step in lipoic acid production by inserting two sulfur atoms into octanoyl-ACP, forming the dithiolane ring structure characteristic of lipoic acid. This post-translational modification is critical for the activation of pyruvate dehydrogenase and α-ketoglutarate dehydrogenase complexes in the tricarboxylic acid cycle, as well as glycine cleavage systems.
Recombinant LIAS proteins are engineered through genetic modification to enable large-scale production in heterologous expression systems such as *E. coli* or yeast. These systems overcome the challenges of low natural abundance and purification difficulties from native sources. The recombinant protein typically retains conserved domains, including the radical S-adenosylmethionine (SAM) binding site and iron-sulfur clusters crucial for its catalytic activity. Researchers often incorporate affinity tags (e.g., His-tag) to facilitate purification and tracking.
Studies on recombinant LIAS have advanced understanding of its structure-function relationships, including insights into sulfur insertion mechanisms and interactions with partner proteins. Its applications extend to investigating metabolic disorders linked to lipoic acid deficiency, such as mitochondrial diseases and diabetes complications. Additionally, recombinant LIAS serves as a tool for developing therapeutic strategies targeting oxidative stress and energy metabolism dysregulation. Recent work also explores its potential in synthetic biology approaches for lipoic acid production and enzyme engineering to enhance catalytic efficiency.
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