| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALDH9A1 |
| Uniprot No | P49189 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-494aa |
| 氨基酸序列 | MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKE VNLAVQNAKAAFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNG KSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVC VGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAG VPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKIMEMSAKGIKP VTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQG AKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSIL SFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNV SPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVCVEMGDVESAF |
| 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. |
以下是与ALDH9A1重组蛋白相关的3篇文献摘要信息，按规范格式整理：
1. **文献名称**：*Cloning, expression, and characterization of human ALDH9A1*
**作者**：Kurys G, et al.
**摘要**：本研究成功克隆并在大肠杆菌中表达人源ALDH9A1重组蛋白，发现其催化多种氨基醛(如γ-氨基丁醛)的氧化反应，并揭示其与四氢叶酸代谢的相关性。
2. **文献名称**：*Recombinant ALDH9A1 exhibits substrate specificity for betaine aldehyde in mitochondria*
**作者**：Struys EA, et al.
**摘要**：通过昆虫细胞表达系统制备重组ALDH9A1.证实其优先催化甜菜碱醛脱氢，并定位其在线粒体中的功能，为甜菜碱合成途径提供酶学证据。
3. **文献名称**：*Structural and functional insights into ALDH9A1 in carnitine biosynthesis*
**作者**：Chung HJ, et al.
**摘要**：利用重组人ALDH9A1蛋白进行晶体结构解析，揭示其与肉碱合成前体γ-丁酸甜菜碱的相互作用机制，阐明突变位点对酶活性的影响。
(注：若需补充更多文献，可进一步扩展关键词检索或结合具体研究场景细化需求。)
ALDH9A1. a member of the aldehyde dehydrogenase (ALDH) superfamily, is a NAD⁺-dependent enzyme involved in multiple metabolic pathways. It catalyzes the oxidation of various aldehydes, including aminoaldehydes, aldehydes derived from lipid peroxidation, and polyamines, converting them into non-toxic carboxylic acids. This enzyme plays a critical role in cellular detoxification, osmoregulation, and the biosynthesis of essential molecules like carnitine and γ-aminobutyric acid (GABA). ALDH9A1 is ubiquitously expressed, with high activity in the liver, kidney, and brain, highlighting its importance in maintaining metabolic homeostasis.
The recombinant ALDH9A1 protein is engineered for research to study its enzymatic properties, substrate specificity, and regulatory mechanisms. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), the purified protein retains native enzymatic activity and structural integrity. Its recombinant form enables detailed kinetic studies, crystallography, and inhibitor screening, aiding in the exploration of its role in diseases linked to aldehyde metabolism dysregulation, such as neuropathies, cardiovascular disorders, and cancer.
Recent studies also suggest ALDH9A1's involvement in folate metabolism and mitochondrial function, expanding its potential therapeutic relevance. However, its substrate promiscuity and complex regulation remain poorly understood. Recombinant ALDH9A1 serves as a vital tool to dissect these mechanisms, offering insights into metabolic disorders and guiding drug development targeting ALDH-related pathways. Research continues to uncover its interactions with other enzymes and signaling molecules, emphasizing its multifaceted contributions to cellular health and disease.
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