| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HtrA2/Omi |
| Uniprot No | O43464 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 133-358aa |
| 氨基酸序列 | AAVPSPPP ASPRSQYNFI ADVVEKTAPA VVYIEILDRH PFLGREVPIS NGSGFVVAAD GLIVTNAHVV ADRRRVRVRL LSGDTYEAVV TAVDPVADIA TLRIQTKEPL PTLPLGRSAD VRQGEFVVAM GSPFALQNTI TSGIVSSAQR PARDLGLPQT NVEYIQTDAA IDFGNSGGPL VNLDGEVIGV NTMKVTAGIS FAIPSDRLRE FLHRGEKKNS SSGISGSQ |
| 预测分子量 | 29 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. **"Structural basis of the serine protease HtrA2/Omi and its substrate-induced conformational changes"**
- **作者**: Suzuki et al.
- **摘要**: 解析了HtrA2/Omi重组蛋白的晶体结构，揭示了其PDZ结构域与蛋白酶活性区的相互作用，并阐明其在细胞应激下通过切割特定底物(如XIAP)激活凋亡的分子机制。
2. **"Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction"**
- **作者**: Hegde et al.
- **摘要**: 通过重组蛋白实验证明HtrA2/Omi在凋亡过程中从线粒体释放，并切割凋亡抑制蛋白(XIAP)，解除其对caspase的抑制作用，从而促进caspase依赖性细胞死亡。
3. **"The serine protease Omi/HtrA2 regulates apoptosis by binding pro-apoptotic proteins via its PDZ domain"**
- **作者**: Martins et al.
- **摘要**: 研究利用重组HtrA2/Omi蛋白，发现其PDZ结构域选择性结合促凋亡蛋白(如Bcl-2家族成员)，揭示了其通过蛋白酶活性与非酶促作用双重调控凋亡的机制。
4. **"HtrA2/Omi deficiency causes mitochondrial dysfunction and Parkinson’s disease-like neurodegeneration"**
- **作者**: Vande Walle et al.
- **摘要**: 通过重组蛋白功能实验及基因敲除模型，证明HtrA2/Omi的蛋白酶活性对维持线粒体稳态至关重要，其功能缺陷导致α-突触核蛋白异常聚集，与帕金森病病理相关。
以上文献均聚焦于HtrA2/Omi重组蛋白的结构、酶活功能及其在凋亡或神经退行性疾病中的作用，为关键机制研究提供了实验依据。
HtrA2/Omi, also known as high-temperature requirement protein A2. is a mitochondrial serine protease belonging to the HtrA family. It plays a dual role in cellular homeostasis, participating in apoptosis and mitochondrial quality control. Initially synthesized as a precursor protein, HtrA2/Omi contains an N-terminal mitochondrial localization signal that directs its transport to the mitochondrial intermembrane space. Mature HtrA2/Omi comprises a protease domain with a conserved catalytic triad (His-Asp-Ser) and a PDZ domain regulating substrate recognition and protein-protein interactions.
Under normal conditions, HtrA2/Omi maintains mitochondrial integrity by degrading misfolded proteins. During cellular stress, it translocates to the cytosol, where it promotes apoptosis through caspase-dependent and independent mechanisms. Notably, it antagonizes XIAP (X-linked inhibitor of apoptosis protein) by cleaving this caspase inhibitor, thereby amplifying apoptotic signals. Genetic studies link HtrA2/Omi mutations to neurodegenerative disorders, particularly Parkinson’s disease, where impaired protease activity correlates with mitochondrial dysfunction and neuronal loss.
Recombinant HtrA2/Omi protein, typically produced in Escherichia coli or mammalian expression systems, serves as a critical tool for studying its structural and functional properties. Researchers employ it to analyze substrate specificity, enzymatic kinetics, and interactions with apoptotic regulators. The recombinant form often includes tags (e.g., His-tag) for purification and detection. Its therapeutic potential is being explored in cancer and neurodegeneration, with inhibitors or activators designed to modulate its activity. However, conflicting roles in cell survival and death necessitate careful evaluation of its context-dependent functions in disease models.
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