| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AGT |
| Uniprot No | P01019 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 44-427aa |
| 氨基酸序列 | VIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNS |
| 预测分子量 | 57.9kDa |
| 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AGT(血管紧张素原)重组蛋白的3篇代表性文献摘要，供参考：
1. **文献名称**：High-yield production of recombinant human angiotensinogen for biochemical studies
**作者**：J. E. Murphy et al.
**摘要**：该研究建立了基于哺乳动物细胞的重组人AGT高效表达系统，通过优化载体设计和纯化流程，获得了高纯度且具有生物活性的AGT蛋白，为肾素-血管紧张素系统的体外研究提供可靠工具。
2. **文献名称**：Crystal structure of angiotensinogen and its molecular mechanism in hypertension
**作者**：T. Zhou et al.
**摘要**：首次解析了重组人AGT蛋白的晶体结构(PDB: 4APH)，揭示了其N端血管紧张素肽段的构象特征，阐明了AGT在肾素切割过程中的构象变化机制，为高血压相关突变研究提供结构依据。
3. **文献名称**：Recombinant AGT variants reveal key residues regulating oxidative stress response
**作者**：K. Tanaka et al.
**摘要**：通过构建系列重组AGT突变体，发现Cys18和Cys138的氧化还原状态显著影响蛋白稳定性，证明AGT在调控细胞氧化应激中具有超出血管紧张素生成的新功能。
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注：上述文献信息为领域典型研究方向模拟，实际文献检索建议通过PubMed(https://pubmed.ncbi.nlm.nih.gov)使用关键词 "recombinant angiotensinogen" 获取最新研究。若需DNA修复相关AGT(O6-alkylguanine-DNA alkyltransferase)文献，请补充说明调整检索策略。
**Background of AGT Recombinant Protein**
Alkylguanine-DNA alkyltransferase (AGT), also known as O⁶-methylguanine-DNA methyltransferase (MGMT), is a DNA repair enzyme critical for maintaining genomic integrity. It directly reverses alkylation damage, particularly at the O⁶ position of guanine—a common mutagenic lesion caused by alkylating agents (e.g., chemotherapeutic drugs or environmental toxins). Unlike most repair mechanisms, AGT does not require cofactors or hydrolysis; instead, it transfers alkyl groups from damaged DNA to its active-site cysteine residue, irreversibly inactivating itself in a "suicide" mechanism. This unique property underscores its role in cellular resistance to alkylation-based therapies.
Recombinant AGT proteins are engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional enzymes for research and therapeutic applications. These proteins retain the native repair activity and are pivotal in studying DNA repair mechanisms, cancer biology, and drug resistance. For instance, AGT overexpression in tumors is linked to resistance against alkylating chemotherapeutics like temozolomide, driving interest in AGT inhibitors (e.g., O⁶-benzylguanine) to sensitize cancer cells.
Additionally, recombinant AGT enables structure-function studies, revealing insights into its catalytic domain, substrate specificity, and mutation-associated dysfunction. Engineered AGT variants are also explored for bioengineering, such as protein-tagging systems (e.g., SNAP-tag) that leverage its covalent substrate-binding property for molecular labeling.
Overall, AGT recombinant proteins bridge fundamental research and translational applications, offering tools to dissect DNA repair pathways, develop anticancer strategies, and innovate biotechnological platforms.
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