| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AUH |
| Uniprot No | Q13825 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 68-339aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSSEMKTEDELRVRHLEEENRGIVVLGINR AYGKNSLSKNLIKMLSKAVDALKSDKKVRTIIIRSEVPGIFCAGADLKER AKMSSSEVGPFVSKIRAVINDIANLPVPTIAAIDGLALGGGLELALACDI RVAASSAKMGLVETKLAIIPGGGGTQRLPRAIGMSLAKELIFSARVLDGK EAKAVGLISHVLEQNQEGDAAYRKALDLAREFLPQGPVAMRVAKLAINQG MEVDLVTGLAIEEACYAQTIPTKDRLEGLLAFKEKRPPRYKGE |
| 预测分子量 | 31 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AUH重组蛋白的3篇参考文献示例(注：文献为示例性内容，具体文献需根据实际数据库检索)：
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1. **文献名称**: "Cloning, Expression, and Characterization of Recombinant Human AUH Protein in Escherichia coli"
**作者**: Zhang L, et al.
**摘要**: 本研究报道了人源AUH基因在大肠杆菌中的重组表达及纯化。通过优化密码子使用和诱导条件，成功获得可溶性AUH重组蛋白。纯化后的蛋白经酶活测定显示其具有羟酰辅酶A水解酶活性，为后续功能研究奠定基础。
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2. **文献名称**: "Structural and Functional Analysis of AUH in Mitochondrial Metabolism"
**作者**: Wang Y, et al.
**摘要**: 通过X射线晶体学解析了重组AUH蛋白的三维结构，揭示了其底物结合位点及催化机制。功能实验表明，AUH在脂肪酸β-氧化中起关键作用，且其突变体与遗传性代谢疾病相关。
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3. **文献名称**: "AUH Recombinant Protein Attenuates Oxidative Stress in Cellular Models"
**作者**: Chen X, et al.
**摘要**: 研究利用HEK293细胞表达重组AUH蛋白，发现其通过调节线粒体活性氧(ROS)水平减轻氧化损伤。结果表明AUH可能作为潜在靶点治疗代谢紊乱相关疾病。
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注：以上文献信息为模拟示例，实际文献需通过PubMed、Web of Science等平台检索确认。
**Background of AUH Recombinant Protein**
The AUH (AU RNA-binding protein/enoyl-CoA hydratase) recombinant protein is a bifunctional enzyme encoded by the *AUH* gene, initially identified for its dual roles in RNA metabolism and mitochondrial fatty acid β-oxidation. Structurally, AUH belongs to the hydratase/isomerase superfamily and contains an N-terminal RNA-binding domain, enabling interactions with AU-rich elements (AREs) in mRNA 3' untranslated regions (UTRs), and a C-terminal enoyl-CoA hydratase domain involved in lipid metabolism.
AUH's RNA-binding activity links it to post-transcriptional gene regulation, particularly in ARE-mediated mRNA stability and turnover. This function is critical in processes like inflammation, apoptosis, and stress responses. Meanwhile, its enzymatic role in converting 3-trans-enoyl-CoA to 3-hydroxyacyl-CoA supports mitochondrial energy production through fatty acid degradation. Dysregulation of AUH is implicated in metabolic disorders, neurodegenerative diseases, and cancers, highlighting its physiological relevance.
Recombinant AUH protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its structural, biochemical, and functional properties. Purified AUH enables in vitro analyses of RNA-protein interactions, enzymatic kinetics, and structural characterization (e.g., X-ray crystallography). It also serves as a tool for screening small-molecule modulators targeting metabolic or RNA-related pathways.
Recent studies explore AUH's role in iron homeostasis and its potential as a biomarker or therapeutic target. Advances in recombinant technology continue to enhance its application in mechanistic studies and drug development, bridging gaps between AUH's molecular functions and disease pathologies.
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