纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LIPT1 |
Uniprot No | Q9Y234 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 26-373aa |
氨基酸序列 | KTVKNGLILQSISNDVYQNLAVEDWIHDHMNLEGKPILFFWQNSPSVVIGRHQNPWQECNLNLMREEGIKLARRRSGGGTVYHDMGNINLTFFTTKKKYDRMENLKLIVRALNAVQPQLDVQATKRFDLLLDGQFKISGTASKIGRTTAYHHCTLLCSTDGTFLSSLLKSPYQGIRSNATASIPSLVKNLLEKDPTLTCEVLMNAVATEYAAYHQIDNHIHLINPTDETLFPGINSKAKELQTWEWIYGKTPKFSINTSFHVLYEQSHLEIKVFIDIKNGRIEICNIEAPDHWLPLEIRDKLNSSLIGSKFCPTETTMLTNILLRTCPQDHKLNSKWNILCEKIKGIM |
预测分子量 | 45.7 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LIPT1重组蛋白的3篇代表性文献概览(注:内容基于模拟文献,建议通过学术数据库核实具体信息):
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1. **文献名称**:*Heterologous Expression and Functional Analysis of Human LIPT1 in E. coli*
**作者**:Smith A, et al. (2018)
**摘要**:该研究通过在大肠杆菌中重组表达人源LIPT1蛋白,优化了纯化条件,并证实其具有催化硫辛酸转移至丙酮酸脱氢酶复合体的活性,为后续酶学研究提供了工具。
2. **文献名称**:*Crystal Structure of Recombinant LIPT1 Reveals Key Residues for Substrate Binding*
**作者**:Johnson R, et al. (2020)
**摘要**:利用重组LIPT1蛋白进行X射线晶体学分析,解析了其三维结构,揭示了底物结合口袋的关键氨基酸残基,为理解其催化机制及疾病相关突变的影响提供了结构基础。
3. **文献名称**:*Defective Mitochondrial Lipoylation Due to LIPT1 Mutations: Rescue by Recombinant Protein Supplementation*
**作者**:Lee S, et al. (2019)
**摘要**:研究证明LIPT1基因突变导致细胞模型中线粒体硫辛酸化缺陷,并通过添加重组LIPT1蛋白部分恢复代谢功能,提示其在相关遗传病治疗中的潜在价值。
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如需具体文献,建议在PubMed或Web of Science中以关键词“LIPT1 recombinant”“lipoyltransferase expression”进一步检索。
**Background of Recombinant LIPT1 Protein**
LIPT1 (Lipoyltransferase 1) is a mitochondrial enzyme critical for protein lipoylation, a post-translational modification essential for the activity of key metabolic enzyme complexes. It catalyzes the transfer of lipoyl groups to specific lysine residues on the E2 subunits of the pyruvate dehydrogenase (PDH) and α-ketoglutarate dehydrogenase (α-KGDH) complexes, which are central to the tricarboxylic acid (TCA) cycle and cellular energy production. Dysregulation of LIPT1 is linked to metabolic disorders, including severe neonatal-onset encephalopathy and epilepsy, underscoring its physiological importance.
Recombinant LIPT1 protein is engineered to enable detailed study of its structure, function, and interaction networks. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells*), the recombinant form often includes affinity tags (e.g., His-tag) for simplified purification. Its production facilitates biochemical assays, such as enzymatic activity analysis, substrate specificity studies, and inhibitor screening for therapeutic development. Additionally, recombinant LIPT1 serves as a tool to investigate molecular mechanisms underlying lipoylation defects in genetic diseases or metabolic syndromes.
Research applications also extend to structural biology (e.g., X-ray crystallography, cryo-EM) to resolve mechanistic details of lipoyltransfer reactions. Furthermore, recombinant LIPT1 is valuable for generating antibodies, validating genetic variants in clinical diagnostics, and modeling disease-associated mutations in *in vitro* systems. By providing a controlled, high-purity protein source, recombinant LIPT1 accelerates both basic research and translational efforts targeting mitochondrial dysfunction and related pathologies.
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