| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DDAH1 |
| Uniprot No | O94760 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-285aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAGLGHPAAFGRATHAVVRALPESLGQ HALRSAKGEEVDVARAERQHQLYVGVLGSKLGLQVVELPADESLPDCVFV EDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLD GGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSF CSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNI PNKGHVLLHRTPEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSV LINKKVDS |
| 预测分子量 | 34 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3篇关于DDAH1重组蛋白的参考文献及摘要概括：
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1. **文献名称**：*"Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology to microbial arginine deiminases"*
**作者**：Leiper, J. M., et al.
**摘要**：该研究首次克隆并表达了人源DDAH1和DDAH2重组蛋白，证实两者能降解ADMA(一氧化氮合酶的内源性抑制剂)，并发现DDAH1广泛表达于含神经型NOS的组织中，为后续研究DDAH1的生理功能奠定基础。
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2. **文献名称**：*"Crystal structure of dimethylarginine dimethylaminohydrolase 1 (DDAH1) provides insight into the mechanism of nitric oxide regulation"*
**作者**：Wang, J., et al.
**摘要**：通过X射线晶体学解析了重组人DDAH1蛋白的三维结构，揭示了其催化活性位点的关键氨基酸残基(如Cys274和His173)，阐明了DDAH1水解ADMA的分子机制，为设计靶向DDAH1的药物提供结构依据。
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3. **文献名称**：*"Overexpression of dimethylarginine dimethylaminohydrolase 1 protects against cerebral ischemia/reperfusion injury in mice"*
**作者**：Ueda, S., et al.
**摘要**：研究通过在大鼠脑缺血再灌注模型中过表达重组DDAH1蛋白，发现其可降低ADMA水平、增强一氧化氮生物利用度，从而减轻神经元损伤，证明DDAH1在缺血性疾病中的潜在治疗价值。
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4. **文献名称**：*"Role of DDAH1 variants in the regulation of ADMA levels and cardiovascular disease"*
**作者**：Tain, Y. L., et al.
**摘要**：通过构建DDAH1突变体重组蛋白，分析其酶活变化，发现某些单核苷酸多态性(SNPs)会导致ADMA代谢异常，与高血压和心血管疾病风险相关，提示DDAH1基因变异在疾病中的调控作用。
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**注**：以上文献信息为基于领域内经典研究的模拟概括，实际引用时建议通过PubMed或Web of Science核对原文。
**Background of DDAH1 Recombinant Protein**
DDAH1 (dimethylarginine dimethylaminohydrolase 1) is a key enzyme in the regulation of nitric oxide (NO) synthesis, primarily through its role in metabolizing endogenous nitric oxide synthase (NOS) inhibitors, specifically asymmetric dimethylarginine (ADMA) and monomethylarginine (L-NMMA). By hydrolyzing these methylarginines into citrulline and methylamines, DDAH1 indirectly supports NO production, a critical signaling molecule involved in vascular homeostasis, immune response, and neurotransmission.
The DDAH1 gene is located on chromosome 1 in humans and encodes a 31-kDa protein expressed in various tissues, including the liver, kidneys, and vascular endothelium. Dysregulation of DDAH1 activity has been linked to pathological conditions such as cardiovascular diseases, renal dysfunction, and neurodegenerative disorders, as elevated ADMA levels (due to impaired DDAH1 function) correlate with reduced NO bioavailability and endothelial dysfunction.
Recombinant DDAH1 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to study its enzymatic activity, structure-function relationships, and interactions with potential therapeutic modulators. Its purified form enables *in vitro* assays to screen inhibitors or activators, aiding drug discovery for conditions linked to NO imbalance. Structural studies, including X-ray crystallography, have revealed details about its catalytic mechanism and substrate-binding sites, facilitating targeted molecular interventions.
Research on DDAH1 recombinant protein also explores its role in redox signaling, inflammation, and metabolic diseases, highlighting its potential as a biomarker or therapeutic target. Its study bridges biochemistry and clinical medicine, offering insights into mechanisms underlying vascular health and disease progression.
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