| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSD17B10 |
| Uniprot No | Q99714 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-261aa |
| 氨基酸序列 | AAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVIRLDGAIRMQP |
| 预测分子量 | 42.8kDa |
| 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HSD17B10重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅供格式参考)：
1. **文献名称**：*Recombinant expression and functional characterization of human HSD17B10 in Escherichia coli*
**作者**：Yang, S.Y. et al.
**摘要**：本研究利用大肠杆菌系统成功表达并纯化了重组HSD17B10蛋白，验证其作为17β-羟基类固醇脱氢酶和线粒体NAD⁺依赖性脱氢酶的双重活性，揭示了其在类固醇代谢和能量代谢中的关键作用。
2. **文献名称**：*Crystal structure of HSD17B10 reveals insights into substrate binding and mitochondrial dysfunction-related mutations*
**作者**：He, X. et al.
**摘要**：通过X射线晶体学解析了重组HSD17B10的三维结构，发现其活性位点对类固醇和支链脂肪酸的识别机制，并探讨了与X-linked精神发育迟滞相关的突变如何破坏蛋白结构及功能。
3. **文献名称**：*Functional analysis of HSD17B10 mutations using recombinant protein models in neurodegenerative disease*
**作者**：Tzeng, S.R. et al.
**摘要**：通过体外重组表达野生型及突变型HSD17B10蛋白，发现特定突变(如R130C)显著降低其脱氢酶活性，提示该蛋白功能异常可能通过线粒体代谢紊乱参与阿尔茨海默病的病理过程。
(注：实际文献需通过学术数据库检索确认。)
HSD17B10. also known as 17β-hydroxysteroid dehydrogenase type 10. ABAD (amyloid-beta-binding alcohol dehydrogenase), or ERAB (endoplasmic reticulum-associated Aβ-binding protein), is a multifunctional mitochondrial enzyme encoded by the HSD17B10 gene. It belongs to the short-chain dehydrogenase/reductase (SDR) superfamily and plays diverse roles in cellular metabolism. Structurally, it functions as a homotetramer, with each subunit containing a Rossmann-fold NAD⁺-binding domain critical for its enzymatic activity.
Originally identified for its role in steroid metabolism, HSD17B10 catalyzes the oxidation of 17β-hydroxysteroids and the metabolism of neuroactive steroids. However, its biological significance extends beyond steroidogenesis. It is involved in fatty acid β-oxidation, branched-chain amino acid catabolism, and the degradation of isoleucine. Notably, HSD17B10 is a component of the mitochondrial RNase P complex, essential for tRNA maturation and mitochondrial DNA replication. This dual role in metabolism and RNA processing underscores its importance in cellular homeostasis.
Recombinant HSD17B10 protein is commonly produced in bacterial (e.g., E. coli) or eukaryotic expression systems for structural and functional studies. Its recombinant form enables investigations into substrate specificity, catalytic mechanisms, and interactions with pathological ligands like amyloid-β (Aβ) in Alzheimer’s disease. Research has linked HSD17B10 mutations to X-linked intellectual disability (XLID) and neurodegeneration, often attributed to disrupted mitochondrial function or aberrant protein interactions.
Current studies focus on its potential as a therapeutic target, particularly in neurodegenerative disorders. Recombinant protein tools have been instrumental in screening inhibitors and elucidating its pathological roles. Despite progress, questions remain about its tissue-specific functions and regulatory mechanisms, driving ongoing research in disease models and structural biology.
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