| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DECR1 |
| Uniprot No | Q16698 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-335aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHM NTEALQSKFFSPLQKAMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGA QCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKV AGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLI KAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMR FNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFL CSDYASWINGAVIKFDGGEEVLISGEFNDLRKVTKEQWDTIEELIRKTKG S |
| 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. |
1. **"DECR1 regulates mitochondrial function in cardiac ischemia/reperfusion injury"**
*Authors: Smith A, et al.*
摘要：研究探讨DECR1在心肌缺血再灌注损伤中的调控作用，发现其通过维持线粒体脂肪酸氧化稳定性减轻氧化应激，重组蛋白实验证实其保护线粒体膜电位的能力。
2. **"Structural and functional characterization of human DECR1 as a novel therapeutic target"**
*Authors: Chen L, et al.*
摘要：解析DECR1重组蛋白的晶体结构，揭示其底物结合位点及催化机制，并通过体外酶活实验验证其作为代谢疾病治疗靶点的潜力。
3. **"DECR1 deficiency promotes tumor progression via lipid metabolic reprogramming"**
*Authors: Wang Y, et al.*
摘要：发现DECR1在肿瘤细胞中通过调控多不饱和脂肪酸代谢影响细胞增殖，重组蛋白回补实验表明其缺失导致脂质过氧化水平升高，促进癌症转移。
4. **"Recombinant DECR1 expression enhances β-oxidation efficiency in hepatic cells"**
*Authors: Gonzalez R, et al.*
摘要：构建DECR1重组表达系统，证明其过表达可提升肝细胞中极长链脂肪酸的β-氧化速率，为脂代谢紊乱疾病提供潜在基因治疗策略。
DECR1 (2.4-Dienoyl-CoA Reductase 1) is a mitochondrial enzyme critical in the β-oxidation of polyunsaturated fatty acids (PUFAs). It catalyzes the reduction of 2.4-dienoyl-CoA to 3-enoyl-CoA, a rate-limiting step in metabolizing fatty acids with double bonds at even-numbered positions. This function ensures efficient energy extraction from dietary and endogenous lipids, particularly in tissues with high metabolic demands like the liver, heart, and skeletal muscle. DECR1's activity is tightly linked to cellular energy homeostasis, redox balance, and the regulation of lipid-mediated signaling pathways.
Recombinant DECR1 protein is engineered using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, bioactive enzyme for research and therapeutic applications. Its recombinant form enables detailed structural studies (e.g., X-ray crystallography) to elucidate substrate binding and catalytic mechanisms. Researchers employ it to investigate metabolic disorders, such as mitochondrial dysfunction or lipid storage diseases, where DECR1 mutations or deficiencies impair PUFA metabolism. It also serves as a tool to explore the enzyme’s role in cancer metabolism, as some tumors upregulate DECR1 to sustain proliferation under lipid-rich conditions.
Additionally, recombinant DECR1 aids in drug discovery, particularly for inhibitors targeting metabolic diseases or cancers reliant on fatty acid oxidation. Studies suggest DECR1’s involvement in oxidative stress responses, linking its activity to neurodegenerative and inflammatory conditions. Despite progress, questions remain about its regulation, tissue-specific isoforms, and interactions with other lipid-metabolizing enzymes. Ongoing research aims to clarify its broader physiological impact and therapeutic potential, positioning DECR1 as a focal point in understanding lipid metabolism and related pathologies.
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