| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AANAT |
| Uniprot No | Q16613 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-207aa |
| 氨基酸序列 | MSTQSTHPLKPEAPRLPPGIPESPSCQRRHTLPASEFRCLTPEDAVSAFE IEREAFISVLGVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWD KERLMQESLTLHRSGGHIAHLHVLAVHRAFRQQGRGPILLWRYLHHLGSQ PAVRRAALMCEDALVPFYERFSFHAVGPCAITVGSLTFMELHCSLRGHPF LRRNSGC |
| 预测分子量 | 52 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AANAT重组蛋白的3篇参考文献及其摘要：
1. **文献名称**：*Crystal structure of a recombinant arylalkylamine N-acetyltransferase*
**作者**：Ganguly, S., et al.
**摘要**：该研究通过大肠杆菌重组表达绵羊AANAT蛋白，利用X射线晶体学解析其三维结构(分辨率2.2 Å)，揭示了其底物结合位点及催化机制，为褪黑素合成的调控提供结构基础。
2. **文献名称**：*Structural and functional analysis of human serotonin N-acetyltransferase*
**作者**：Wolf, E., et al.
**摘要**：作者在昆虫细胞中重组表达人源AANAT，结合酶动力学和突变实验，证明其活性依赖磷酸化修饰，并发现特定赖氨酸残基对底物结合及昼夜节律调控的关键作用。
3. **文献名称**：*Comparative kinetics of recombinant vertebrate arylalkylamine N-acetyltransferases*
**作者**：Cazaméa-Catal, I., et al.
**摘要**：研究通过比较斑马鱼、鸡和哺乳动物重组AANAT的酶学特性，发现不同物种间催化效率差异显著，提示进化过程中AANAT功能可能适应了特定生理需求。
(注：以上文献信息为示例，实际引用需根据具体论文核实。)
Arylalkylamine N-acetyltransferase (AANAT) is a critical enzyme in the melatonin biosynthesis pathway, catalyzing the conversion of serotonin to N-acetylserotonin, the immediate precursor of melatonin. This enzyme plays a central role in regulating circadian rhythms, as melatonin synthesis follows a strict day-night cycle influenced by light exposure. AANAT’s activity is tightly controlled at transcriptional, translational, and post-translational levels, making it a key regulatory point for maintaining physiological and behavioral rhythms across species.
Recombinant AANAT refers to the engineered version of this protein produced through heterologous expression systems, such as *E. coli*, yeast, or mammalian cell cultures. Its production enables large-scale studies of the enzyme’s structure, kinetics, and regulatory mechanisms. For instance, recombinant AANAT has been instrumental in elucidating how phosphorylation by protein kinases modulates its stability and activity. Structural studies using X-ray crystallography and cryo-EM have revealed conserved catalytic domains and substrate-binding sites, providing insights into enzyme-substrate interactions and potential drug targets.
Applications of recombinant AANAT span basic research and biotechnology. It is used to screen for inhibitors or activators that could modulate melatonin levels, with implications for treating sleep disorders, depression, or circadian rhythm disruptions. In industrial settings, engineered AANAT variants are explored for cost-effective melatonin production. Additionally, transgenic models expressing recombinant AANAT help dissect its role in development, aging, and diseases like cancer, where dysregulated melatonin signaling is observed.
Despite its utility, challenges remain in maintaining the enzyme’s stability and activity *in vitro*, prompting ongoing optimization of expression systems and purification protocols. Overall, recombinant AANAT serves as a vital tool for advancing chronobiology research and therapeutic innovation.
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