纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | AngI |
Uniprot No | P03950 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 26-147aa |
氨基酸序列 | DNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP |
预测分子量 | 18.0 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AngI(血管紧张素I)重组蛋白的模拟参考文献示例,供参考:
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1. **文献名称**:*Expression and Purification of Recombinant Angiotensin I in E. coli*
**作者**:Zhang L, et al.
**摘要**:本研究报道了在大肠杆菌系统中高效表达AngI重组蛋白的优化策略,采用His标签纯化技术获得高纯度产物,并证实其与天然AngI具有相似的免疫反应性。
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2. **文献名称**:*Structural Analysis of Recombinant AngI Using NMR Spectroscopy*
**作者**:Kimura T, et al.
**摘要**:通过核磁共振(NMR)技术解析了重组AngI的三维结构,揭示了其与血管紧张素转换酶(ACE)结合的关键位点,为开发高血压靶向药物提供结构基础。
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3. **文献名称**:*Functional Characterization of Recombinant AngI in a Rat Hypertension Model*
**作者**:Gupta R, et al.
**摘要**:在高血压大鼠模型中评估重组AngI的生理效应,发现其可显著升高血压并激活肾素-血管紧张素系统,验证了其生物活性及潜在研究应用价值。
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4. **文献名称**:*Development of a Novel AngI Fusion Protein for Antibody Production*
**作者**:Sato H, et al.
**摘要**:构建了AngI与荧光蛋白的融合表达载体,成功用于制备高特异性多克隆抗体,为心血管疾病的免疫检测技术提供新工具。
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**注**:以上文献为模拟内容,实际研究需通过PubMed、SciHub或Google Scholar等平台检索关键词“recombinant Angiotensin I”获取真实文献。
Angiotensin I (AngI) is a decapeptide (10-amino-acid peptide) derived from the enzymatic cleavage of angiotensinogen, a precursor protein synthesized primarily in the liver. As a critical component of the renin-angiotensin system (RAS), AngI serves as a key intermediary in regulating blood pressure, fluid balance, and cardiovascular homeostasis. It is generated when renin, an enzyme released by the kidneys, cleaves angiotensinogen. AngI itself is biologically inactive but acts as a substrate for angiotensin-converting enzyme (ACE), which removes two amino acids to produce the potent vasoconstrictor angiotensin II (AngII), driving systemic vascular resistance and aldosterone secretion.
Recombinant AngI protein is engineered using genetic modification techniques, typically expressed in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems. This allows large-scale production of highly pure, standardized AngI for research and therapeutic applications. Its recombinant form retains the structural and functional properties of endogenous AngI, enabling precise experimental control in studying RAS pathways, drug discovery (e.g., ACE inhibitors, angiotensin receptor blockers), and diagnostic assays. Researchers also utilize recombinant AngI to investigate mutations or dysregulation in RAS-linked diseases, such as hypertension, heart failure, and kidney disorders. Additionally, it serves as a reference material in clinical labs to measure renin or ACE activity. By providing a consistent and scalable source, recombinant AngI supports advancements in understanding cardiovascular pathophysiology and developing targeted therapies.
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