| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ECHS1 |
| Uniprot No | P30084 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-290aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMASGANFEYIIAEKRGKNNTVGLIQLNRPK ALNALCDGLIDELNQALKIFEEDPAVGAIVLTGGDKAFAAGADIKEMQNL SFQDCYSSKFLKHWDHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGE KAQFAQPEILIGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQA GLVSKICPVETLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGS KLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ |
| 预测分子量 | 31 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ECHS1重组蛋白的3篇代表性文献示例(注：文献信息为示例，实际引用需核实)：
1. **文献名称**：*Structural insights into human short-chain enoyl-CoA hydratase (ECHS1) deficiency*
**作者**：Fukao T, et al.
**摘要**：解析了人源ECHS1重组蛋白的晶体结构，揭示了其催化活性位点及突变(如R130C)导致酶功能缺陷的分子机制，与线粒体脂肪酸代谢紊乱相关。
2. **文献名称**：*Functional characterization of ECHS1 variants associated with Leigh syndrome*
**作者**：Sakai C, et al.
**摘要**：通过重组表达ECHS1突变体蛋白，分析其酶动力学参数和热稳定性，发现致病突变导致底物结合能力下降，解释了患者神经退行性病变的代谢基础。
3. **文献名称**：*Substrate specificity of ECHS1 in branched-chain amino acid metabolism*
**作者**：Haapalainen AM, et al.
**摘要**：利用重组ECHS1蛋白进行体外酶活实验，证实其对支链脂肪酸代谢中间体的高催化效率，并揭示其双功能酶活性在能量代谢中的调控作用。
(提示：实际文献需通过PubMed或Web of Science以关键词“ECHS1 recombinant protein”或“ECHS1 structure/function”检索获取。)
Enoyl-CoA hydratase short-chain 1 (ECHS1) is a mitochondrial enzyme critical in fatty acid β-oxidation and branched-chain amino acid metabolism. It catalyzes the hydration of 2-trans-enoyl-CoA intermediates to 3-hydroxyacyl-CoA during these pathways. Structurally, ECHS1 functions as a homodimer, with each subunit containing a conserved "crotonase fold" that facilitates substrate binding. The human ECHS1 gene maps to chromosome 10q26.2-q26.3 and encodes a 290-amino acid protein.
Recombinant ECHS1 protein is typically produced using expression systems like *E. coli* or mammalian cells to study its enzymatic properties and pathological mechanisms. Researchers engineer vectors containing the ECHS1 coding sequence with affinity tags (e.g., His-tag) for purification. This recombinant form retains native catalytic activity, enabling *in vitro* studies of substrate specificity and inhibition kinetics.
ECHS1 deficiency, caused by mutations in the ECHS1 gene, is linked to severe metabolic disorders characterized by Leigh syndrome-like symptoms, developmental regression, and neurodegeneration. Recombinant ECHS1 serves as a vital tool for functional characterization of disease-associated variants, drug screening for potential chaperone therapies, and structural analysis through X-ray crystallography. Recent studies also explore its role in cancer metabolism, as altered ECHS1 expression correlates with tumor progression in certain malignancies. The protein's stability and conserved functional domains across species make it valuable for comparative biochemical research and therapeutic development.
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