| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HTRA2 |
| Uniprot No | P62995 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 111-201aa |
| 氨基酸序列 | RANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHT |
| 分子量 | 26.5 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人HTRA2蛋白的参考文献及其摘要概括：
1. **文献名称**: "Crystal structure of HtrA2 reveals a strikingly asymmetric protease with a relaxed substrate-binding site"
**作者**: Clausen, T., et al.
**摘要**: 该研究解析了重组人HTRA2蛋白的晶体结构，揭示了其不对称的蛋白酶结构及松弛的底物结合位点。文章指出HTRA2通过其PDZ结构域调节底物识别，并讨论了其在细胞凋亡中的双重作用(促凋亡和蛋白酶活性)。
2. **文献名称**: "Mitochondrial protease HtrA2/Omi regulates caspase-independent neuronal death"
**作者**: Suzuki, Y., et al.
**摘要**: 研究利用重组HTRA2蛋白探讨其在帕金森病中的机制，发现HTRA2突变会导致蛋白酶活性丧失，进而引发线粒体功能障碍和神经元死亡，强调了其在神经退行性疾病中的关键作用。
3. **文献名称**: "Expression, purification, and characterization of recombinant human HtrA2/Omi"
**作者**: Jones, J.M., et al.
**摘要**: 该文献描述了一种在大肠杆菌中高效表达重组人HTRA2蛋白的方法，优化了纯化步骤并验证了其酶活性，为后续功能研究提供了可靠的重组蛋白制备方案。
4. **文献名称**: "Substrate specificity and inhibitor design for HtrA2 protease implicated in neurodegenerative diseases"
**作者**: Martins, L.M., et al.
**摘要**: 通过重组HTRA2蛋白分析其底物特异性，筛选出特异性小分子抑制剂，证实调节其蛋白酶活性可改善疾病模型中的神经元存活，为治疗提供了潜在靶点。
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以上文献涵盖了HTRA2的结构解析、疾病机制、重组表达方法及治疗应用，均为该领域的重要研究参考。
Human HTRA2 (High-temperature requirement A2), also known as Omi, is a serine protease implicated in mitochondrial homeostasis and apoptosis. It resides in the mitochondrial intermembrane space and plays a dual role in cellular processes. Structurally, HTRA2 contains a trypsin-like protease domain and a PDZ domain, which regulate protease activity and protein-protein interactions. Under normal conditions, HTRA2 maintains mitochondrial quality control by degrading misfolded proteins and supporting stress response pathways. However, during apoptosis, it translocates to the cytoplasm, cleaving inhibitor-of-apoptosis proteins (IAPs) to promote caspase activation.
Recombinant human HTRA2 protein is produced using expression systems like *E. coli* or mammalian cells, enabling studies on its enzymatic activity and disease associations. Mutations in *HTRA2* are linked to neurodegenerative disorders, particularly Parkinson’s disease, due to impaired protease function and mitochondrial dysfunction. Paradoxically, HTRA2 overexpression has been observed in certain cancers, suggesting context-dependent roles in survival or death signaling.
Researchers utilize recombinant HTRA2 to investigate its structure-function relationships, substrate specificity, and therapeutic targeting. Its dual nature as a stress-response guardian and apoptosis inducer makes it a focal point for understanding mitochondrial disorders and developing treatments for neurodegeneration or cancer.
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