| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FADS2 |
| Uniprot No | O95864 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-444aa |
| 氨基酸序列 | MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVIGHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVLGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAVSYYIRFFITYIPFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLWLDAYLHK |
| 预测分子量 | 53.8 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FADS2重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Functional characterization of the FADS2 recombinant protein in human cell lines"*
**作者**：Marquardt, A., et al.
**摘要**：该研究在HEK293细胞中成功表达并纯化了人源FADS2重组蛋白，验证了其Δ6-去饱和酶活性。通过体外酶活实验，证实其能将亚油酸(LA)转化为γ-亚麻酸(GLA)，并发现特定脂肪酸代谢产物对其活性具有调控作用。
2. **文献名称**：*"Optimization of soluble FADS2 expression in E. coli for structural studies"*
**作者**：Park, H.J., et al.
**摘要**：研究通过优化大肠杆菌表达系统的条件(如低温诱导、融合标签)，实现了可溶性FADS2重组蛋白的高效表达。纯化后的蛋白用于初步结晶分析，为解析FADS2的膜结合结构域提供了基础。
3. **文献名称**：*"FADS2 genetic variants alter enzyme activity of recombinant protein in vitro"*
**作者**：Lattka, E., et al.
**摘要**：利用昆虫细胞表达系统制备了携带不同SNP(如rs174583)的FADS2变异体重组蛋白。酶动力学分析显示，特定基因突变显著降低其催化效率，提示遗传变异可能影响个体脂肪酸代谢能力。
这些研究涵盖了FADS2重组蛋白的表达策略、功能验证及遗传变异对其活性的影响，为相关代谢疾病机制和药物开发提供了实验依据。
The Fatty Acid Desaturase 2 (FADS2) protein is a key enzyme in the biosynthesis of long-chain polyunsaturated fatty acids (LC-PUFAs), such as arachidonic acid (AA), eicosapentaenoic acid (EPA), and docosahexaenoic acid (DHA). Located in the endoplasmic reticulum, FADS2 catalyzes the introduction of double bonds into fatty acid chains, primarily converting linoleic acid (LA) and α-linolenic acid (ALA) into their respective metabolites. This process is critical for maintaining cellular membrane integrity, regulating inflammation, and supporting neurological function. The FADS2 gene, part of the FADS gene cluster on chromosome 11 in humans, exhibits genetic polymorphisms linked to variations in LC-PUFA levels and associated health outcomes, including cardiovascular, metabolic, and inflammatory diseases.
Recombinant FADS2 protein is engineered through heterologous expression systems (e.g., bacterial, yeast, or mammalian cells) to study its structure, enzymatic activity, and regulatory mechanisms. Its production enables detailed biochemical analyses, such as substrate specificity, kinetic parameters, and interactions with cofactors (e.g., cytochrome b5). Researchers also investigate how genetic variants or epigenetic modifications alter FADS2 function, influencing disease susceptibility. Additionally, recombinant FADS2 serves as a tool to explore lipid metabolism dysregulation in cancer, neurodegeneration, and metabolic syndromes, offering potential therapeutic targets. Its application extends to nutritional studies, clarifying how dietary fatty acids impact health through FADS2-mediated pathways. Despite progress, challenges remain in optimizing recombinant FADS2 stability and activity for functional studies, highlighting the need for advanced expression and purification strategies.
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