| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OPLAH |
| Uniprot No | O14841 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 209-302aa |
| 氨基酸序列 | RELGFTHVSLSSEAMPMVRIVPRGHTACADAYLTPAIQRYVQGFCRGFQGQLKDVQVLFMRSDGGLAPMDTFSGSSAVLSGPAGGVVGYSATTY |
| 预测分子量 | 17.4 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OPLAH(5-氧脯氨酸酶)重组蛋白研究的参考文献示例(注：部分文献为示例性描述，建议通过学术数据库核实具体信息)：
1. **"Cloning and Functional Expression of Human 5-Oxoprolinase in Escherichia coli"**
*作者：Kumar, S., et al. (2008)*
**摘要**：研究报道了人源OPLAH基因的克隆及其在大肠杆菌中的重组表达，成功获得具有酶活性的蛋白，并对其催化特性进行了初步分析，为后续代谢疾病研究奠定基础。
2. **"Recombinant Expression and Characterization of Human 5-Oxoprolinase in Insect Cells"**
*作者：Tanaka, M., et al. (2015)*
**摘要**：利用杆状病毒-昆虫细胞表达系统高效表达人源OPLAH，通过纯化获得高纯度蛋白，并测定其酶动力学参数，揭示了pH和金属离子对活性的影响。
3. **"Heterologous Production of OPLAH in Pichia pastoris for Glutathione Metabolism Studies"**
*作者：Zhang, Y., et al. (2012)*
**摘要**：在毕赤酵母中重组表达OPLAH，优化发酵条件后获得可溶性蛋白，应用于体外谷胱甘肽代谢途径的重建，验证了其在代谢网络中的功能。
4. **"Structural Insights into Recombinant OPLAH via X-ray Crystallography"**
*作者：Müller, R., et al. (2020)*
**摘要**：通过重组表达人源OPLAH并进行晶体结构解析，揭示了其底物结合域和催化机制，为设计针对该酶的抑制剂提供结构基础。
**建议**：以上文献为示例性质，具体研究可通过PubMed、Web of Science等平台以关键词“OPLAH recombinant”、“5-oxoprolinase expression”检索最新成果。
**Background of OPLAH Recombinant Protein**
OPLAH (5-Oxoprolinase, ATP-Hydrolyzing), also known as pyroline-5-carboxylate reductase, is a critical enzyme in the glutathione degradation pathway and proline metabolism. It catalyzes the ATP-dependent hydrolysis of 5-oxoproline (a byproduct of glutathione breakdown) into L-glutamate, replenishing cellular glutamate pools and maintaining redox homeostasis. Dysregulation of OPLAH activity has been linked to metabolic disorders, oxidative stress-related pathologies, and neurodegenerative conditions.
Recombinant OPLAH protein is produced using genetic engineering techniques, typically expressed in heterologous systems like *E. coli*, yeast, or mammalian cells. This approach enables large-scale production of purified, bioactive OPLAH for functional studies and therapeutic exploration. Its recombinant form retains enzymatic activity, allowing researchers to investigate its role in cellular detoxification, amino acid recycling, and redox balance. Structural studies using recombinant OPLAH have also shed light on its catalytic mechanism and interaction with cofactors like ATP and magnesium ions.
In biomedical research, OPLAH recombinant protein serves as a tool to model metabolic diseases, screen potential enzyme modulators, or develop enzyme replacement therapies. For instance, defects in OPLAH are associated with 5-oxoprolinuria, a rare disorder characterized by excessive urinary excretion of 5-oxoproline. Recombinant OPLAH could offer therapeutic potential in such cases. Challenges in its application include optimizing stability, activity, and delivery in vivo. Current studies focus on engineering OPLAH variants with enhanced catalytic efficiency or modified substrate specificity, leveraging advances in protein engineering and structural biology.
Overall, OPLAH recombinant protein represents a vital resource for unraveling metabolic pathways and exploring targeted interventions for glutathione-related disorders.
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