| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ECI1 |
| Uniprot No | P42126 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 42-302aa |
| 氨基酸序列 | FGSQRVLVE PDAGAGVAVM KFKNPPVNSL SLEFLTELVI SLEKLENDKS FRGVILTSDR PGVFSAGLDL TEMCGRSPAH YAGYWKAVQE LWLRLYQSNL VLVSAINGAC PAGGCLVALT CDYRILADNP RYCIGLNETQ LGIIAPFWLK DTLENTIGHR AAERALQLGL LFPPAEALQV GIVDQVVPEE QVQSTALSAI AQWMAIPDHA RQLTKAMMRK ATASRLVTQR DADVQNFVSF ISKDSIQKSL QMYLERLKEE KG |
| 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. |
以下是关于ECI1重组蛋白的3篇文献摘要示例(注：部分内容为模拟，供参考)：
1. **文献名称**：Cloning and functional characterization of recombinant ECI1 in yeast
**作者**：Zhang Y, et al.
**摘要**：研究报道了ECI1基因的克隆及在酵母系统中的重组表达，证实其编码的烯酰辅酶A异构酶参与脂肪酸β-氧化代谢途径，重组蛋白活性检测显示其对短链烯酰辅酶A底物具有高催化效率。
2. **文献名称**：Structural analysis of human ECI1 by recombinant expression and X-ray crystallography
**作者**：Lee S, et al.
**摘要**：通过大肠杆菌系统表达并纯化ECI1重组蛋白，利用X射线晶体学解析其三维结构，揭示其活性位点关键氨基酸残基，为酶催化机制及代谢疾病相关突变研究提供结构基础。
3. **文献名称**：Role of ECI1 in peroxisomal lipid metabolism: Insights from recombinant protein knockout models
**作者**：Müller C, et al.
**摘要**：通过构建ECI1敲除细胞模型，结合重组蛋白回补实验，证明ECI1缺失导致过氧化物酶体中支链脂肪酸代谢异常，重组ECI1恢复代谢稳态，强调其在脂代谢中的关键作用。
(提示：实际文献需通过PubMed或Google Scholar检索确认。)
ECI1 (Enoyl-CoA Delta Isomerase 1), also known as ECI or ACAA2. is a mitochondrial enzyme critical in fatty acid β-oxidation, a key metabolic pathway for energy production. It specifically catalyzes the isomerization of 3-trans-enoyl-CoA to 2-trans-enoyl-CoA intermediates, enabling the breakdown of unsaturated fatty acids. This function is essential for metabolizing dietary and stored lipids, particularly under conditions of fasting or high energy demand. Deficiencies in ECI1 activity are linked to metabolic disorders, such as mitochondrial enoyl-CoA isomerase deficiency, characterized by impaired energy metabolism and organ dysfunction.
Recombinant ECI1 protein is produced using biotechnological methods, typically by cloning the ECI1 gene into expression vectors (e.g., bacterial, yeast, or mammalian systems) to enable large-scale production. This engineered protein retains the enzymatic activity of native ECI1. making it a valuable tool for studying fatty acid metabolism, enzyme kinetics, and substrate specificity in vitro. Researchers use it to model metabolic diseases, screen potential therapeutic compounds, or investigate mechanisms underlying lipid-related pathologies like obesity, diabetes, and cardiovascular diseases.
Beyond basic research, recombinant ECI1 has applications in diagnostics, aiding in the detection of enzymatic deficiencies, and in drug development for metabolic syndrome or rare genetic disorders. Its structural characterization also contributes to understanding mitochondrial enzyme dynamics and designing targeted therapies. Overall, recombinant ECI1 serves as a bridge between biochemical research and clinical solutions for metabolic health challenges.
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