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| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RLN1 |
| Uniprot No | P04808 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-53aa |
| 氨基酸序列 | VAAKWKDD VIKLCGRELV RAQIAICGMS TWS |
| 预测分子量 | 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RLN1重组蛋白的3篇参考文献及其摘要概括：
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1. **标题**: "Production of recombinant human relaxin 1 in Escherichia coli and its structural characterization"
**作者**: Smith A, et al.
**摘要**: 该研究通过大肠杆菌表达系统成功制备了重组人松弛素1(RLN1)，并利用质谱和圆二色谱分析验证了其正确折叠和二硫键结构。结果显示重组蛋白具有与天然RLN1相似的生物活性，适用于体外细胞实验。
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2. **标题**: "Recombinant relaxin-1 alleviates cardiac fibrosis via inhibition of TGF-β/Smad2 signaling in a mouse model"
**作者**: Chen L, et al.
**摘要**: 研究者通过哺乳动物细胞表达系统获得高纯度重组RLN1蛋白，并在小鼠心脏纤维化模型中验证其疗效。实验表明，重组RLN1通过抑制TGF-β/Smad2通路显著减少胶原沉积，为纤维化疾病治疗提供潜在策略。
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3. **标题**: "Engineering a stable form of human relaxin-1 for enhanced therapeutic potential"
**作者**: Johnson R, et al.
**摘要**: 本研究通过定点突变技术改良重组RLN1的稳定性，延长其半衰期。体外活性实验显示，改造后的蛋白在促进宫颈成纤维细胞松弛的活性上优于天然RLN1.提示其在产科或组织修复中的应用前景。
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注：以上文献信息为示例性质，实际引用时需以真实文献为准。建议通过PubMed或Web of Science以关键词“recombinant RLN1/relaxin-1”检索最新研究。
**Background of RLN1 Recombinant Protein**
Relaxin-1 (RLN1) is a peptide hormone belonging to the relaxin family, which plays critical roles in reproductive and connective tissue remodeling processes. Initially identified for its role in pregnancy—where it promotes uterine relaxation, cervical softening, and mammary gland development—RLN1 has broader physiological implications. It binds to the relaxin family peptide receptor 1 (RXFP1), triggering signaling pathways that regulate collagen metabolism, angiogenesis, and anti-fibrotic responses. Structurally, RLN1 is a heterodimeric protein consisting of two chains (A and B) linked by disulfide bonds, resembling insulin-like growth factors.
Recombinant RLN1 is produced using biotechnological methods, such as *E. coli* or mammalian cell expression systems, to ensure proper folding and post-translational modifications. Its production addresses the limited availability of native RLN1 from biological sources and enables standardized research and therapeutic applications. Recombinant RLN1 retains the bioactivity of the native hormone, making it invaluable for studying its role in tissue repair, cardiovascular function, and reproductive health.
Research on RLN1 recombinant protein has expanded into potential clinical applications. Preclinical studies highlight its anti-fibrotic effects in liver, lung, and kidney diseases, as well as its cardioprotective properties in heart failure models. Additionally, RLN1 is being explored for its anti-inflammatory actions and role in cancer biology, where it may influence tumor microenvironment dynamics. Despite progress, challenges remain in optimizing delivery methods and understanding long-term effects. RLN1 recombinant protein thus represents a promising yet underexplored therapeutic agent bridging reproductive biology and systemic disease management.
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