纯度 | > 95 % SDS-PAGE. |
种属 | Human |
靶点 | ACOT13 |
Uniprot No | Q9NPJ3 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-140aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMTSMTQSLREVIKAMTKARNFERVLGKITL VSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMALLCTERGAP GVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFTSVDLTNKATGKLIA QGRHTKHLGN |
预测分子量 | 17 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ACOT13重组蛋白的示例参考文献(注:文献信息为示例性质,建议通过学术数据库验证和获取完整内容):
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1. **文献名称**: *"Structural and Functional Characterization of Recombinant Human Acyl-CoA Thioesterase 13 (ACOT13)"*
**作者**: Su, X., et al.
**摘要**: 通过重组表达和纯化人源ACOT13蛋白,结合X射线晶体学分析其三维结构,揭示了该酶对长链酰基辅酶A的水解活性,并探讨其在过氧化物酶体脂肪酸代谢中的潜在作用。
2. **文献名称**: *"ACOT13 Regulates Mitochondrial Lipid Metabolism via Hydrolysis of Long-Chain Fatty Acyl-CoA Esters"*
**作者**: Hunt, M.C., et al.
**摘要**: 研究重组ACOT13蛋白的酶动力学特性,发现其特异性分解C16-C20酰基辅酶A,并通过细胞实验证明其过表达影响线粒体脂肪酸氧化,提示其在能量代谢中的调控功能。
3. **文献名称**: *"Recombinant ACOT13 Modulates Hepatic Insulin Sensitivity by Altering Cellular Lipid Composition"*
**作者**: Zhang, Y., et al.
**摘要**: 利用重组ACOT13蛋白进行体外肝细胞实验,发现其通过调节酰基辅酶A水平影响脂质代谢通路,从而改善胰岛素抵抗,为代谢综合征治疗提供新靶点。
4. **文献名称**: *"Cloning, Expression, and Biochemical Analysis of ACOT13 in a Bacterial System"*
**作者**: Cheng, Z., et al.
**摘要**: 报道在大肠杆菌中高效表达并纯化重组ACOT13蛋白,通过酶活性测定确定其最适pH和底物偏好性,为后续功能研究提供工具。
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建议通过 **PubMed** 或 **Google Scholar** 检索关键词 *"ACOT13 recombinant protein"* 或 *"Acyl-CoA thioesterase 13"* 获取最新及真实文献。
ACOT13 (Acyl-CoA Thioesterase 13) is a member of the acyl-CoA thioesterase family, which plays a critical role in lipid metabolism by hydrolyzing acyl-CoA thioesters into free fatty acids and coenzyme A. This enzymatic activity regulates cellular levels of acyl-CoA substrates, influencing processes such as fatty acid oxidation, lipid synthesis, and signaling pathways. ACOT13 is localized to mitochondria and exhibits substrate specificity for medium- to long-chain acyl-CoAs, suggesting its involvement in mitochondrial lipid homeostasis and energy production.
Recombinant ACOT13 protein is engineered for research and therapeutic applications. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains catalytic activity and structural integrity, enabling functional studies. Researchers utilize recombinant ACOT13 to investigate its regulatory mechanisms in metabolic disorders, including obesity, diabetes, and non-alcoholic fatty liver disease (NAFLD). Its role in modulating acyl-CoA pools also links it to cellular stress responses and apoptosis, highlighting potential relevance in cancer biology.
Structurally, ACOT13 contains a conserved thioesterase domain and a mitochondrial targeting sequence. Post-translational modifications, such as phosphorylation, may fine-tune its activity. Recent studies explore its interactions with metabolic enzymes and signaling molecules, providing insights into its broader regulatory networks. Recombinant variants with tags (e.g., His-tag) facilitate purification and detection, streamlining *in vitro* assays and structural analyses.
Overall, recombinant ACOT13 serves as a vital tool for dissecting lipid metabolism pathways and developing targeted therapies for metabolic diseases, while ongoing research continues to uncover its multifaceted roles in cellular physiology.
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