| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FA2H |
| Uniprot No | Q7L5A8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-372aa |
| 氨基酸序列 | MAPAPPPAASFSPSEVQRRLAAGACWVRRGARLYDLSSFVRHHPGGEQLLRARAGQDISADLDGPPHRHSANARRWLEQYYVGELRGEQQGSMENEPVALEETQKTDPAMEPRFKVVDWDKDLVDWRKPLLWQVGHLGEKYDEWVHQPVTRPIRLFHSDLIEGLSKTVWYSVPIIWVPLVLYLSWSYYRTFAQGNVRLFTSFTTEYTVAVPKSMFPGLFMLGTFLWSLIEYLIHRFLFHMKPPSDSYYLIMLHFVMHGQHHKAPFDGSRLVFPPVPASLVIGVFYLCMQLILPEAVGGTVFAGGLLGYVLYDMTHYYLHFGSPHKGSYLYSLKAHHVKHHFAHQKSGFGISTKLWDYCFHTLTPEKPHLKTQ |
| 分子量 | 69.2 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是与重组人FA2H蛋白相关的3篇代表性文献(文献信息为学术假设示例，供参考)：
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1. **文献名称**: *Recombinant human FA2H enzyme characterization and its role in α-hydroxylation of fatty acids*
**作者**: Johnson, R. et al.
**摘要**: 报道了重组人FA2H蛋白在大肠杆菌中的表达及纯化方法，并验证了其在体外催化C18:0脂肪酸生成2-羟基脂肪酸的活性，揭示了FA2H在鞘脂代谢中的关键作用。
2. **文献名称**: *FA2H mutations disrupt cellular lipid homeostasis in hereditary leukodystrophies*
**作者**: Schneider, S.A. et al.
**摘要**: 通过重组FA2H蛋白功能实验，证明FA2H基因突变会导致酶活性丧失，引发脑白质中异常脂质堆积，阐明了其在遗传性脑白质营养不良症中的病理机制。
3. **文献名称**: *Structural insights into the catalytic mechanism of human FA2H protein*
**作者**: Li, Y. & Wang, X.
**摘要**: 利用重组FA2H蛋白的晶体结构解析，揭示了其底物结合域和铁离子依赖性催化机制，为开发针对FA2H相关疾病的药物提供结构基础。
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注：上述文献为基于领域知识的模拟示例，实际引用时请通过数据库(如PubMed、Web of Science)核实真实文献信息。
Recombinant human FA2H (fatty acid 2-hydroxylase) protein is a genetically engineered form of the FA2H enzyme, which plays a critical role in lipid metabolism. FA2H catalyzes the hydroxylation of fatty acids at the C2 position, generating 2-hydroxy fatty acids that are essential components of sphingolipids, particularly in the nervous system. These lipids contribute to membrane structure, myelin sheath formation, and cellular signaling.
Mutations in the FA2H gene are linked to neurodegenerative disorders, such as hereditary spastic paraplegia (SPG35) and leukodystrophy, as well as skin barrier defects. Recombinant FA2H protein is produced via heterologous expression systems (e.g., E. coli or mammalian cells) for functional studies. It enables researchers to investigate enzyme kinetics, substrate specificity, and interactions with cellular components. Its applications extend to modeling lipid-related pathologies, screening therapeutic compounds, and developing enzyme replacement strategies.
Research on recombinant FA2H also aids in understanding the biochemical mechanisms underlying sphingolipid homeostasis and myelin maintenance, offering insights into therapeutic targets for demyelinating diseases. The protein’s stability and activity are often optimized for in vitro assays, supporting advances in both basic science and translational medicine.
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