| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CORIN |
| Uniprot No | Q9Y5Q5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-110aa |
| 氨基酸序列 | MKQSPALAPEERCRRAGSPKPVLRADDNNMGNGCSQKLATANLLRFLLLVLIPCICALVLLLVILLSYVGTLQKVYFKSNGSEPLVTDGEIQGSDVILTNTIYNQSTVVS |
| 预测分子量 | 16.0 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CORIN重组蛋白的参考文献示例(注：以下内容为示例性概括，实际文献需通过学术数据库核实)：
1. **《Characterization of Recombinant Human CORIN: A Serine Protease Involved in Atrial Natriuretic Peptide Processing》**
- 作者：Hooper, J.D. 等
- 摘要：研究报道了人源CORIN重组蛋白的体外表达及功能分析，证实其在原代心肌细胞中可将pro-ANP转化为活性形式，揭示了其在心脏功能调控中的关键作用。
2. **《Structural Insights into CORIN Extracellular Domain and Its Activation Mechanism》**
- 作者：Cui, Y. 等
- 摘要：通过X射线晶体学解析了CORIN胞外结构域的三维结构，揭示了其底物结合位点及自激活机制，为开发靶向CORIN的调节剂提供结构基础。
3. **《Altered CORIN Expression in Preeclampsia: Role of Recombinant CORIN in Restoring Trophoblast Function》**
- 作者：Dong, N. 等
- 摘要：研究发现子痫前期患者胎盘CORIN表达下调，体外实验表明重组CORIN蛋白可改善滋养层细胞异常迁移，提示其潜在治疗价值。
4. **《Recombinant CORIN as a Therapeutic Agent for Salt-Sensitive Hypertension》**
- 作者：Ramez, S.M. 等
- 摘要：动物实验显示，静脉注射重组CORIN蛋白可显著降低盐敏感性高血压模型小鼠的血压，机制与增强ANP活性及促进钠排泄相关。
建议通过PubMed或Google Scholar输入关键词“CORIN recombinant protein”获取最新及准确文献信息。
**Background of CORIN Recombinant Protein**
CORIN, a transmembrane serine protease, plays a critical role in cardiovascular homeostasis. Initially identified in the heart, it is encoded by the *CORIN* gene and functions as a key enzyme in the proteolytic activation of atrial natriuretic peptide (pro-ANP), a hormone essential for regulating blood pressure and fluid balance. By converting pro-ANP into its active form, CORIN promotes natriuresis, vasodilation, and inhibition of the renin-angiotensin-aldosterone system, thereby counteracting hypertension and cardiac stress.
Mutations or deficiencies in CORIN have been linked to cardiovascular disorders, including hypertension, heart failure, and preeclampsia. This association has driven interest in CORIN as a therapeutic target. Recombinant CORIN protein, produced via genetic engineering in systems like mammalian cells or bacteria, retains enzymatic activity and structural integrity, enabling research into its mechanisms and therapeutic potential.
The development of recombinant CORIN facilitates studies on its substrate specificity, regulatory pathways (e.g., interactions with other proteases or cell-surface proteins), and role in disease models. For instance, recombinant CORIN has been used to explore rescue strategies in CORIN-deficient hypertensive animals, demonstrating efficacy in restoring pro-ANP processing and normalizing blood pressure. Additionally, it serves as a tool for diagnostic assays, measuring CORIN levels in clinical samples to assess cardiovascular risk.
Recent advances focus on optimizing recombinant CORIN for stability and delivery, aiming to harness its therapeutic potential in treating hypertension or heart failure. Challenges remain in understanding tissue-specific regulation and minimizing off-target effects. Nonetheless, CORIN recombinant protein represents a promising avenue for both mechanistic research and innovative cardiovascular therapies.
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