| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ELOVL1 |
| Uniprot No | Q9BW60 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-279aa |
| 氨基酸序列 | MEAVVNLYQEVMKHADPRIQGYPLMGSPLLMTSILLTYVYFVLSLGPRIMANRKPFQLRGFMIVYNFSLVALSLYIVYEFLMSGWLSTYTWRCDPVDYSNSPEALRMVRVAWLFLFSKFIELMDTVIFILRKKDGQVTFLHVFHHSVLPWSWWWGVKIAPGGMGSFHAMINSSVHVIMYLYYGLSAFGPVAQPYLWWKKHMTAIQLIQFVLVSLHISQYYFMSSCNYQYPVIIHLIWMYGTIFFMLFSNFWYHSYTKGKRLPRALQQNGAPGIAKVKAN |
| 预测分子量 | 32,6 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. |
以下是围绕ELOVL1重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
---
1. **文献名称**：*Functional characterization of recombinant ELOVL1 in very long-chain fatty acid elongation*
**作者**：Smith A, et al.
**摘要**：本研究在大肠杆菌中成功表达并纯化了重组ELOVL1蛋白，证实其催化C22至C26脂肪酸的延伸活性，并通过体外酶活实验揭示其底物特异性及对神经鞘脂合成的关键作用。
2. **文献名称**：*ELOVL1 recombinant protein rescues lipid dysfunction in a mouse model of ichthyosis*
**作者**：Chen L, et al.
**摘要**：通过向ELOVL1基因敲除小鼠注射重组ELOVL1蛋白，发现其可恢复表皮角质层超长链脂肪酸(VLCFA)水平，缓解鱼鳞病样皮肤表型，提示潜在治疗应用价值。
3. **文献名称**：*Structural insights into ELOVL1 substrate binding domain via crystallography*
**作者**：Yamamoto K, et al.
**摘要**：利用X射线晶体学解析重组ELOVL1蛋白的底物结合域结构，发现其保守的组氨酸-谷氨酸对在催化中的关键作用，为设计酶活性调节剂提供依据。
4. **文献名称**：*ELOVL1 overexpression alters lipid metabolism in hepatocellular carcinoma cells*
**作者**：Gomez-Ruiz B, et al.
**摘要**：在肝癌细胞中表达重组ELOVL1蛋白，发现其通过增加VLCFA合成促进脂筏形成，进而激活促增殖信号通路，提示ELOVL1在癌症代谢中的潜在调控机制。
---
注：如需真实文献，建议通过PubMed或Google Scholar检索关键词“ELOVL1 recombinant protein”，筛选近年高影响力论文。
The ELOVL1 (Elongation of Very Long-Chain Fatty Acids 1) protein is a member of the ELOVL family of enzymes, which play critical roles in the elongation of fatty acids by catalyzing the formation of very long-chain fatty acids (VLCFAs) through the addition of two-carbon units. Specifically, ELOVL1 is integral to the synthesis of saturated and monounsaturated VLCFAs (C20–C36), which are essential components of sphingolipids, ceramides, and other lipid species. These lipids contribute to cellular membrane structure, signaling, and barrier function in tissues such as the skin and brain.
Recombinant ELOVL1 protein refers to the genetically engineered form of the enzyme produced in vitro, often using expression systems like bacteria, yeast, or mammalian cells. This allows for controlled study of its enzymatic activity, structure, and interactions. ELOVL1 contains conserved motifs characteristic of fatty acid elongases, including a histidine-rich catalytic domain and transmembrane regions that anchor it to the endoplasmic reticulum, where elongation occurs.
Research on ELOVL1 has highlighted its physiological and pathological significance. Mutations in the ELOVL1 gene are linked to neurodevelopmental disorders, such as infantile-onset progressive encephalopathy and ichthyosis, reflecting its role in maintaining neuronal integrity and epidermal homeostasis. Studies using recombinant ELOVL1 have elucidated mechanisms underlying VLCFA dysregulation in diseases like Sjögren-Larsson syndrome and hereditary spastic paraplegia. Additionally, ELOVL1 is explored in cancer biology, as altered VLCFA metabolism may influence tumor cell survival and drug resistance.
The availability of recombinant ELOVL1 facilitates drug discovery, enabling high-throughput screening for inhibitors or modulators to target lipid metabolism pathways. Its application extends to generating disease models and advancing gene therapy strategies for ELOVL1-related disorders. Ongoing research continues to unravel its regulatory networks and potential therapeutic implications.
×
