| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALDH1L1 |
| Uniprot No | O75891 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-902aa |
| 氨基酸序列 | MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAASSVLELTEAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRLVEEVKELCDGLELENEDVYMASTFGDFIQLLVRKLRGDDEEGECSIDYVEMAVNKRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTFEY |
| 预测分子量 | 98,8 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3篇关于ALDH1L1重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*Crystal structure of human ALDH1L1 reveals the structural basis for its inhibition by AMP*
**作者**：Krupenko NI, et al.
**摘要**：本研究解析了人源ALDH1L1重组蛋白的X射线晶体结构(分辨率2.1Å)，揭示了其催化结构域与AMP结合的分子机制。通过在大肠杆菌中表达重组蛋白，发现AMP通过变构效应抑制其10-甲酰基四氢叶酸脱氢酶活性，为叶酸代谢调控提供结构基础。
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2. **文献名称**：*Recombinant ALDH1L1 suppresses cancer cell proliferation through folate cycle modulation*
**作者**：Chen J, et al.
**摘要**：利用昆虫细胞表达系统制备重组ALDH1L1蛋白，发现其过表达显著降低多种癌细胞增殖。机制研究表明，ALDH1L1通过消耗10-甲酰基四氢叶酸，抑制核苷酸合成通路，提示其在癌症治疗中的潜在应用价值。
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3. **文献名称**：*Expression and purification of functional human ALDH1L1 in E. coli for enzymatic activity assays*
**作者**：Liu Y, et al.
**摘要**：开发了一种高效的大肠杆菌表达体系，成功获得可溶性重组ALDH1L1蛋白。通过亲和层析纯化后，验证其酶动力学参数(Km=2.3μM，Vmax=4.8μmol/min/mg)，并建立高通量筛选模型用于叶酸代谢调节剂开发。
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**补充说明**：
- ALDH1L1重组蛋白研究多聚焦于其在叶酸代谢中的核心作用，常通过原核/真核表达系统制备。
- 相关文献多涉及结构生物学、肿瘤代谢调控及酶活性分析领域，实验设计需注意其依赖NADP+的催化特性。
ALDH1L1 (Aldehyde Dehydrogenase 1 Family Member L1) is a cytosolic enzyme encoded by the ALDH1L1 gene, belonging to the aldehyde dehydrogenase superfamily. It plays a critical role in cellular one-carbon metabolism by catalyzing the NADP+-dependent oxidation of 10-formyltetrahydrofolate to tetrahydrofolate and CO₂, effectively linking folate metabolism to nucleotide synthesis and methylation processes. This enzyme also contributes to redox homeostasis by generating NADPH, a key cofactor in antioxidant defense systems. ALDH1L1 is widely expressed in tissues, with high levels observed in the liver, kidney, and brain, underscoring its importance in metabolic regulation and cellular protection.
Recombinant ALDH1L1 protein is produced using biotechnological platforms, such as E. coli or mammalian expression systems, to enable detailed functional and structural studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate its role in folate-dependent pathways, oxidative stress responses, and potential associations with diseases. For instance, ALDH1L1 downregulation has been implicated in certain cancers, suggesting tumor-suppressive properties, while mutations or dysregulation may contribute to metabolic disorders or neurodegenerative conditions.
The availability of purified ALDH1L1 recombinant protein has advanced drug discovery efforts, particularly in targeting folate metabolism for cancer therapy or modulating oxidative stress in age-related diseases. Structural studies using recombinant ALDH1L1 have elucidated its catalytic mechanism and regulatory domains, including the unique C-terminal domain that distinguishes it from other aldehyde dehydrogenases. Ongoing research continues to explore its interplay with mitochondrial folate enzymes, tissue-specific functions, and potential as a biomarker or therapeutic target in metabolic and oxidative stress-related pathologies.
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