| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ALDH1A1 |
| Uniprot No | P00352 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-501aa |
| 氨基酸序列 | SSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI GPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN S |
| 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. |
1. **"Recombinant ALDH1A1 Purification and Enzymatic Characterization"** - Smith et al. (2015)
*摘要*：本研究报道了在大肠杆菌中高效表达并纯化重组人源ALDH1A1蛋白的方法，验证了其催化视黄醛转化为视黄酸的酶活性，并分析了其动力学参数。
2. **"Structural Insights into ALDH1A1 by X-ray Crystallography"** - Jackson et al. (2017)
*摘要*：通过重组ALDH1A1蛋白的晶体结构解析，揭示了其底物结合口袋的构象变化，为靶向ALDH1A1的抑制剂设计提供了结构基础。
3. **"ALDH1A1 Overexpression Promotes Chemoresistance in Cancer Stem Cells"** - Liu et al. (2019)
*摘要*：利用重组ALDH1A1蛋白进行体外功能实验，证实其高表达通过增强氧化应激防御能力，介导肿瘤干细胞对化疗药物的耐药性。
4. **"ALDH1A1 in Lipid Metabolism: Recombinant Protein-Based Functional Study"** - Chen et al. (2020)
*摘要*：研究发现重组ALDH1A1蛋白通过调控PPARγ信号通路影响脂肪细胞分化，提示其在代谢综合征中的潜在作用。
(注：上述文献为示例性内容，实际引用需核对真实出版物。)
ALDH1A1. a member of the aldehyde dehydrogenase 1A subfamily, is a critical NAD⁺-dependent enzyme involved in cellular detoxification and metabolic processes. It catalyzes the oxidation of various endogenous and exogenous aldehydes, including retinaldehyde to retinoic acid (RA), a key signaling molecule in embryonic development, cell differentiation, and homeostasis. Structurally, ALDH1A1 functions as a homotetramer, with each subunit containing a conserved catalytic domain that binds NAD⁺ and substrate. Its expression is tissue-specific, enriched in the liver, brain, and stem cells, where it plays roles in detoxifying cytotoxic aldehydes and maintaining redox balance.
In cancer biology, ALDH1A1 has gained attention as a biomarker for cancer stem cells (CSCs) due to its overexpression in tumor-initiating populations across multiple malignancies, such as breast, lung, and ovarian cancers. High ALDH1A1 activity correlates with enhanced chemoresistance, metastasis, and poor prognosis, likely through RA signaling pathways that promote self-renewal and survival of CSCs. Additionally, ALDH1A1 is implicated in oxidative stress resistance by metabolizing lipid peroxidation-derived aldehydes (e.g., 4-hydroxynonenal), thereby protecting cells from apoptosis.
Recombinant ALDH1A1 protein, typically produced in E. coli or mammalian expression systems, retains enzymatic activity and is widely used to study its biochemical properties, inhibitor screening, and RA biosynthesis mechanisms. Purified variants may include tags (e.g., His-tag) for detection and purification. Researchers utilize this protein to explore its role in CSC maintenance, chemoresistance pathways, and potential therapeutic targeting. Its application extends to developing ALDH1A1 inhibitors as adjuvants to conventional chemotherapy. Despite progress, questions remain regarding isoform-specific functions and context-dependent regulatory mechanisms in diseases.
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