| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DDAH2 |
| Uniprot No | O95865 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-285aa |
| 氨基酸序列 | MGTPGEGLGRCSHALIRGVPESLASGEGAGAGLPALDLAKAQREHGVLGGKLRQRLGLQLLELPPEESLPLGPLLGDTAVIQGDTALITRPWSPARRPEVDGVRKALQDLGLRIVEIGDENATLDGTDVLFTGREFFVGLSKWTNHRGAEIVADTFRDFAVSTVPVSGPSHLRGLCGMGGPRTVVAGSSDAAQKAVRAMAVLTDHPYASLTLPDDAAADCLFLRPGLPGVPPFLLHRGGGDLPNSQEALQKLSDVTLVPVSCSELEKAGAGLSSLCLVLSTRPHS |
| 预测分子量 | 61.2 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. |
以下是模拟生成的关于DDAH2重组蛋白的参考文献示例(非真实文献，仅供格式参考)：
1. **《Expression and characterization of recombinant human DDAH2 for nitric oxide regulation studies》**
- 作者：Smith A, et al.
- 摘要：研究利用大肠杆菌系统重组表达并纯化人源DDAH2蛋白，证实其催化ADMA水解的活性，为NO代谢研究提供工具。
2. **《Structural insights into DDAH2 substrate specificity through crystallographic analysis》**
- 作者：Wang L, et al.
- 摘要：解析DDAH2的晶体结构，揭示其与底物结合的活性位点特征，阐明催化过程中关键氨基酸残基的作用机制。
3. **《DDAH2 recombinant protein attenuates endothelial dysfunction in diabetic mouse models》**
- 作者：Zhang Y, et al.
- 摘要：通过动物实验证明外源性重组DDAH2可降低ADMA水平，改善糖尿病模型血管内皮功能，提示其治疗潜力。
4. **《High-throughput screening of DDAH2 inhibitors using a fluorescence-based enzymatic assay》**
- 作者：Lee J, et al.
- 摘要：基于重组DDAH2蛋白建立高通量筛选平台，发现新型小分子抑制剂，为心血管疾病药物开发提供候选分子。
注：以上内容为学术写作示例，实际文献需通过PubMed、Web of Science等数据库检索获取。
DDAH2 (dimethylarginine dimethylaminohydrolase 2) is a key enzyme in the regulation of nitric oxide (NO) synthesis, a critical signaling molecule involved in vascular homeostasis, immune response, and neurotransmission. It specifically hydrolyzes endogenous asymmetric dimethylarginine (ADMA) and monomethylarginine (MMA), which are competitive inhibitors of nitric oxide synthase (NOS). By metabolizing these methylarginines, DDAH2 indirectly enhances NO production, making it a pivotal regulator of cardiovascular and endothelial function.
The DDAH2 gene is located on chromosome 6 in humans and encodes a protein distinct from its isoform DDAH1 in tissue distribution and substrate affinity. While DDAH1 is predominantly expressed in the liver and kidneys, DDAH2 is found in tissues with high NO demand, such as blood vessels, immune cells, and the placenta. Dysregulation of DDAH2 activity has been linked to pathologies like hypertension, atherosclerosis, and preeclampsia, highlighting its therapeutic potential.
Recombinant DDAH2 protein is produced using expression systems (e.g., E. coli, mammalian cells) to enable functional and structural studies. Purified recombinant forms allow researchers to investigate enzymatic kinetics, substrate interactions, and inhibitor screening. Its crystal structure has been resolved, aiding in understanding catalytic mechanisms and drug design.
Current research focuses on modulating DDAH2 activity to treat NO-related disorders. For example, DDAH2 overexpression or activators may ameliorate endothelial dysfunction, while inhibitors could mitigate conditions associated with excessive NO. Recombinant DDAH2 also serves as a tool to study methylarginine metabolism in cellular models, offering insights into disease mechanisms and biomarker development. Its role in immune regulation and angiogenesis further expands its biomedical relevance.
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