首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RLN2 |
| Uniprot No | P04090 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-185aa |
| 氨基酸序列 | MGSSHHHHHHMGSSHHHHHHSSGLVPRGSHMGSDSWMEEVIKLCGRELVR AQIAICGMSTWSKRSLSQEDAPQTPRPVAEIVPSFINKDTETINMMSEFV ANLPQELKLTLSEMQPALPQLQQHVPVLKDSSLLFEEFKKLIRNRQSEAA DSSPSELKYLGLDTHSRKKRQLYSALANKCCHVGCTKRSLARFC |
| 预测分子量 | 21 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RLN2(松弛素-2)重组蛋白的示例参考文献(内容为虚构示例，仅用于格式参考)：
1. **文献名称**：Recombinant Human Relaxin-2 (RLN2) Attenuates Cardiac Fibrosis via TGF-β Signaling Inhibition
**作者**：Smith A, et al.
**摘要**：研究利用重组RLN2蛋白在心肌纤维化模型中的作用，发现其通过抑制TGF-β/Smad通路减少胶原沉积，为心血管疾病治疗提供新策略。
2. **文献名称**：High-Yield Production of RLN2 in E. coli: Optimization and Functional Characterization
**作者**：Zhang L, et al.
**摘要**：报道通过大肠杆菌表达系统高效生产重组RLN2.优化纯化工艺并验证其生物活性，为规模化制备奠定基础。
3. **文献名称**：RLN2 Recombinant Protein Promotes Angiogenesis in Ischemic Tissue Repair
**作者**：Chen Y, et al.
**摘要**：验证重组RLN2通过激活VEGF通路促进缺血组织血管新生，提示其在组织再生中的潜在应用价值。
4. **文献名称**：Structural Insights into RLN2 Receptor Binding by Cryo-EM Analysis
**作者**：Johnson R, et al.
**摘要**：利用冷冻电镜解析重组RLN2与其受体RXFP1的复合物结构，揭示其分子互作机制，助力靶向药物设计。
---
注：以上文献为示例，实际研究中请通过PubMed或Google Scholar检索真实文献(关键词：recombinant RLN2. relaxin-2. RXFP1)。
Relaxin-2 (RLN2), a member of the relaxin peptide family, is a pleiotropic hormone with critical roles in reproductive, cardiovascular, and connective tissue remodeling processes. Initially identified for its role in pregnancy—mediating uterine relaxation, cervical softening, and systemic hemodynamic adaptations—RLN2 has gained broader scientific interest due to its potent antifibrotic, anti-inflammatory, and vasodilatory properties. Structurally, it consists of two peptide chains (A and B) linked by disulfide bonds and signals primarily through the G protein-coupled receptor RXFP1.
Recombinant RLN2 is engineered using biotechnological platforms, often expressed in *E. coli* or mammalian cell systems to ensure proper folding and post-translational modifications. Its production addresses the limitations of natural RLN2 extraction, which is scarce and impractical for therapeutic use. The recombinant form retains bioactivity comparable to endogenous RLN2. enabling scalable production for research and clinical applications.
Preclinical studies highlight RLN2's therapeutic potential in fibrosis-related disorders (e.g., liver, lung, and kidney fibrosis), heart failure, and vascular diseases. It promotes extracellular matrix degradation by modulating matrix metalloproteinases and inhibiting collagen deposition. Additionally, its angiogenic and cardioprotective effects are being explored in ischemic conditions. Despite promising results, clinical translation remains limited, with only a few Phase II/III trials (e.g., serelaxin for acute heart failure) showing mixed outcomes, underscoring the need for further mechanistic and dosing studies.
Current research focuses on optimizing delivery systems, understanding receptor dynamics, and exploring combination therapies. RLN2's multifaceted biology positions it as a compelling candidate for addressing complex multifactorial diseases, though challenges in pharmacokinetics and tissue-specific targeting persist.
×
