| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ECH1 |
| Uniprot No | Q13011 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 34-328aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMTGSSAQEAASGVALGEAPDHSYESLRVTS AQKHVLHVQLNRPNKRNAMNKVFWREMVECFNKISRDADCRAVVISGAGK MFTAGIDLMDMASDILQPKGDDVARISWYLRDIITRYQETFNVIERCPKP VIAAVHGGCIGGGVDLVTACDIRYCAQDAFFQVKEVDVGLAADVGTLQRL PKVIGNQSLVNELAFTARKMMADEALGSGLVSRVFPDKEVMLDAALALAA EISSKSPVAVQSTKVNLLYSRDHSVAESLNYVASWNMSMLQTQDLVKSVQ ATTENKELKTVTFSKL |
| 预测分子量 | 34 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ECH1重组蛋白的示例参考文献(注：以下内容为模拟生成，非真实存在的文献)：
1. **文献名称**：*Expression and Functional Characterization of Recombinant Human ECH1 in Escherichia coli*
**作者**：Zhang L. et al.
**摘要**：该研究成功在大肠杆菌中表达了重组人ECH1蛋白，并优化了纯化条件。通过酶活实验证实重组ECH1具有特异性催化烯酰-CoA水解的能力，为后续脂肪酸代谢研究提供了工具。
2. **文献名称**：*Structural Insights into ECH1 Catalytic Mechanism by X-ray Crystallography*
**作者**：Wang Y. et al.
**摘要**：通过X射线晶体学解析了重组ECH1蛋白的三维结构，揭示了其底物结合口袋的关键氨基酸残基，阐明了其催化烯酰-CoA水合反应的分子机制。
3. **文献名称**：*Role of Recombinant ECH1 in Regulating Lipid Metabolism in Hepatocellular Carcinoma*
**作者**：Chen R. et al.
**摘要**：研究发现肝癌细胞中重组ECH1蛋白的过表达可抑制脂肪酸氧化并促进肿瘤增殖，提示ECH1可能通过代谢重编程影响肝癌进展。
4. **文献名称**：*Development of a High-Yield Mammalian Cell System for ECH1 Production*
**作者**：Kim S. et al.
**摘要**：开发了一种基于哺乳动物细胞的重组ECH1表达系统，获得高活性且糖基化修饰的蛋白，适用于疾病模型中的功能研究与药物筛选。
(注：以上文献为模拟示例，实际引用时请核实真实文献。)
**Background of ECH1 Recombinant Protein**
ECH1 (Enoyl-CoA Hydratase 1) is a key enzyme involved in fatty acid metabolism, specifically in the mitochondrial β-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-CoA to 3-hydroxyacyl-CoA, a critical step in the breakdown of fatty acids to generate acetyl-CoA for energy production. ECH1 is part of the crotonase superfamily and is ubiquitously expressed across tissues, with high activity in organs requiring intense energy metabolism, such as the liver, heart, and skeletal muscle.
Recombinant ECH1 protein is produced using biotechnological methods, typically through expression in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells). This allows large-scale production of the purified enzyme for research and therapeutic applications. The recombinant form retains the enzymatic activity and structural features of the native protein, enabling studies on its biochemical properties, substrate specificity, and interaction with cofactors or inhibitors.
Research on ECH1 has gained attention due to its role in metabolic disorders, including mitochondrial dysfunction, obesity, and diabetes. Dysregulation of ECH1 has been linked to impaired fatty acid oxidation, contributing to lipid accumulation and metabolic syndrome. Additionally, ECH1 is implicated in cancer progression, as altered lipid metabolism in tumor cells (a hallmark of cancer) often involves enzymes like ECH1 to sustain rapid proliferation.
Structural studies of recombinant ECH1 have provided insights into its catalytic mechanism and potential as a drug target. Mutations in the *ECH1* gene are associated with rare genetic disorders, emphasizing its physiological importance. Furthermore, recombinant ECH1 is used in diagnostic assays to measure enzyme activity in clinical samples, aiding in the diagnosis of metabolic diseases.
Overall, ECH1 recombinant protein serves as a vital tool for understanding lipid metabolism, disease mechanisms, and therapeutic development, bridging basic research with clinical applications.
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