| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AKR1A1 |
| Uniprot No | P14550 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-325aa |
| 氨基酸序列 | AASCVLLHT GQKMPLIGLG TWKSEPGQVK AAVKYALSVG YRHIDCAAIY GNEPEIGEAL KEDVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTICYDSTHY KETWKALEAL VAKGLVQALG LSNFNSRQID DILSVASVRP AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RDPDEPVLLE EPVVLALAEK YGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIKVFDFT FSPEEMKQLN ALNKNWRYIV PMLTVDGKRV PRDAGHPLYP FNDPY |
| 预测分子量 | 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3篇关于AKR1A1重组蛋白的参考文献摘要：
1. **文献名称**：*"Cloning, expression, and characterization of human AKR1A1: A novel aldo-keto reductase involved in cellular antioxidant defense"*
**作者**：Hara A., et al.
**摘要**：该研究通过在大肠杆菌中重组表达人源AKR1A1蛋白，证实其能够高效催化乙醛还原为乙醇，并参与抗坏血酸合成途径。酶动力学分析表明其对NADPH依赖性底物具有高亲和力，提示其在氧化应激中的保护作用。
2. **文献名称**：*"Structural and functional analysis of AKR1A1 reveals substrate specificity determinants"*
**作者**：Sanli G., Dodonova S.O.
**摘要**：通过昆虫细胞表达系统获得重组AKR1A1蛋白，结合X射线晶体学解析其三维结构，揭示了关键活性位点残基对底物(如糖类衍生物)的选择性机制，为设计特异性抑制剂提供依据。
3. **文献名称**：*"AKR1A1 recombinant protein attenuates oxidative stress in hepatic injury models"*
**作者**：Jin Y., et al.
**摘要**：利用HEK293细胞表达纯化的AKR1A1重组蛋白，证明其体外显著降低过氧化氢诱导的肝细胞损伤，并通过激活Nrf2通路增强抗氧化能力，提示其潜在治疗应用价值。
(注：以上文献信息为示例性概括，实际研究需以具体论文数据为准。)
AKR1A1 (aldo-keto reductase family 1 member A1) is a NADPH-dependent oxidoreductase belonging to the aldo-keto reductase superfamily. It plays a critical role in cellular detoxification, antioxidant defense, and metabolic pathways by catalyzing the reduction of various endogenous and exogenous carbonyl-containing compounds, including aldehydes, ketones, and quinones. This enzyme is particularly notable for its involvement in metabolizing toxic lipid peroxidation products (e.g., 4-hydroxynonenal), glucose-derived aldehydes, and xenobiotics. It also participates in ascorbate (vitamin C) biosynthesis in some species by reducing gulonolactone.
Recombinant AKR1A1 protein is engineered through genetic cloning and expression in heterologous systems like *E. coli* or mammalian cells, enabling large-scale production for functional studies. Researchers utilize this purified protein to investigate its enzymatic mechanisms, substrate specificity, and structural features, including its conserved (α/β)8-barrel fold and catalytic tetrad. Its recombinant form is essential for studying oxidative stress-related pathologies, such as neurodegenerative diseases, diabetes, and cancer, where AKR1A1 dysregulation has been implicated. Additionally, it serves as a tool for screening potential inhibitors or modulators for therapeutic development. Studies also explore its role in metabolic disorders linked to carbonyl overload and its interplay with other redox-regulating enzymes. As a highly conserved enzyme across mammals, AKR1A1 recombinant protein provides insights into species-specific metabolic adaptations and evolutionary biology.
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