| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADMA |
| 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 | MAGLGHPAAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQHQLYVGVLGSKLGLQVVELPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS |
| 预测分子量 | 31,1 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. |
以下为3篇与ADMA相关的重组蛋白研究文献示例(建议通过学术数据库验证准确性)：
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1. **标题**: "Recombinant dimethylarginine dimethylaminohydrolase 1 reduces asymmetric dimethylarginine in vitro and in vivo"
**作者**: Pope AJ et al.
**摘要**: 研究重组表达的人源DDAH1酶活性，证实其通过降解ADMA改善内皮功能，为心血管疾病治疗提供新思路。
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2. **标题**: "Expression and characterization of recombinant protein arginine methyltransferase 1 for ADMA synthesis"
**作者**: Smith SA, et al.
**摘要**: 报道PRMT1重组蛋白的高效表达及纯化，揭示其在体外催化生成ADMA的分子机制。
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3. **标题**: "Development of a recombinant antibody-based ELISA for specific detection of asymmetric dimethylarginine"
**作者**: Chen L, et al.
**摘要**: 利用重组蛋白技术开发ADMA特异性检测抗体，建立高灵敏度ELISA方法，助力临床ADMA水平监测。
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注：以上信息为基于领域知识的示例，实际文献请通过PubMed/Google Scholar检索关键词(如：ADMA, recombinant DDAH, PRMT expression)获取最新数据。
**Background of ADMA Recombinant Protein**
Asymmetric dimethylarginine (ADMA), an endogenous inhibitor of nitric oxide synthase (NOS), plays a critical role in regulating vascular tone and endothelial function. Elevated ADMA levels are associated with endothelial dysfunction, cardiovascular diseases, and metabolic disorders, making it a significant biomarker and therapeutic target. However, studying ADMA's molecular mechanisms and developing diagnostic/therapeutic tools requires reliable and standardized sources of the protein, which is challenging due to its post-translational modifications and low natural abundance.
Recombinant ADMA protein, produced via genetic engineering, addresses these challenges. Using host systems like *E. coli* or mammalian cells, the ADMA-coding sequence is expressed and purified under controlled conditions, ensuring high specificity and batch consistency. This approach enables large-scale production of bioactive ADMA for research and clinical applications, such as elucidating its role in pathologies (e.g., hypertension, renal disease, diabetes) or calibrating diagnostic assays.
The development of ADMA recombinant protein also supports drug discovery, particularly in screening compounds that modulate NOS activity or ADMA metabolism. Challenges remain, including replicating human-specific post-translational modifications and ensuring stability. Advances in protein engineering, such as codon optimization and tailored expression systems, continue to refine its production. Overall, recombinant ADMA serves as a vital tool for advancing cardiovascular and metabolic research, bridging gaps between basic science and clinical innovation.
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