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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RLN |
| 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3篇关于RLN(松弛素)重组蛋白研究的代表性文献摘要(内容基于领域内常见研究方向，作者名为示例)：
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1. **文献名称**：*Production and characterization of recombinant human Relaxin-2 in mammalian cell lines*
**作者**：Ross A. Bathgate, et al.
**摘要**：本研究优化了在CHO细胞中表达重组人松弛素-2(RLN2)的工艺，通过密码子优化和纯化策略提高蛋白产量，并验证其生物活性(通过cAMP信号通路测定)，为临床应用提供高质量蛋白来源。
2. **文献名称**：*Recombinant Relaxin alleviates fibrosis in experimental liver disease models*
**作者**：Chrishan S. Samuel, et al.
**摘要**：通过动物实验证明，重组RLN蛋白可显著减少肝纤维化模型中胶原沉积，其机制可能与抑制TGF-β/Smad信号通路相关，提示RLN在抗纤维化治疗中的潜力。
3. **文献名称**：*Engineering a long-acting Relaxin analog for cardiovascular therapy*
**作者**：Laura J. Parry, et al.
**摘要**：通过基因改造延长重组RLN的体内半衰期，并在心衰模型中验证其持续改善心脏血流动力学和心肌重塑的效果，为慢性心血管疾病治疗提供新策略。
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**备注**：以上文献标题和内容为模拟概括，实际文献需通过PubMed或Web of Science等平台以关键词“recombinant relaxin”或“RLN2 protein”检索获取。知名RLN研究团队包括Bathgate、Samuel、Agoulnik等课题组。
**Background of Recombinant RLN (Relaxin) Protein**
Relaxin (RLN), a pleiotropic peptide hormone belonging to the insulin superfamily, plays critical roles in reproductive, cardiovascular, and anti-fibrotic processes. It exists as multiple isoforms (e.g., RLN-1. RLN-2. RLN-3) across species, with RLN-2 being the predominant form in humans. Structurally, RLN consists of two disulfide-linked chains (A and B) processed from a prohormone, binding to G protein-coupled receptors (RXFP1/RXFP2) to activate downstream signaling pathways, including cAMP and nitric oxide production.
Recombinant RLN protein is engineered using biotechnological platforms (e.g., bacterial, yeast, or mammalian cell systems) to mimic endogenous RLN’s bioactivity. Its production involves cloning RLN-encoding genes into expression vectors, followed by purification via chromatography. Recombinant technology overcomes limitations of native RLN extraction, enabling scalable, high-purity yields for research and therapeutic use.
Therapeutic interest in recombinant RLN stems from its vasodilatory, anti-inflammatory, and extracellular matrix-remodeling properties. Preclinical and clinical studies highlight its potential in treating fibrosis (e.g., liver, lung, heart), acute heart failure, and pregnancy-related disorders. Notably, serelaxin (recombinant human RLN-2) demonstrated efficacy in phase III trials for acute heart failure, though regulatory approval remains pending due to mixed outcomes.
Current research focuses on optimizing RLN analogs for enhanced stability and tissue targeting, addressing challenges like short plasma half-life. Additionally, RLN's role in cancer and metabolic diseases is under exploration. As a versatile biologic, recombinant RLN continues to bridge translational gaps in regenerative medicine and chronic disease management.
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