| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ELN |
| Uniprot No | P15502 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-786aa |
| 氨基酸序列 | GGVPGAIPGGVPGGVFYPGAGLGALGGGALGPGGKPLKPVPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAAYKAAKAGAGLGGVPGVGGLGVSAGAVVPQPGAGVKPGKVPGVGLPGVYPGGVLPGARFPGVGVLPGVPTGAGVKPKAPGVGGAFAGIPGVGPFGGPQPGVPLGYPIKAPKLPGGYGLPYTTGKLPYGYGPGGVAGAAGKAGYPTGTGVGPQAAAAAAAKAAAKFGAGAAGVLPGVGGAGVPGVPGAIPGIGGIAGVGTPAAAAAAAAAAKAAKYGAAAGLVPGGPGFGPGVVGVPGAGVPGVGVPGAGIPVVPGAGIPGAAVPGVVSPEAAAKAAAKAAKYGARPGVGVGGIPTYGVGAGGFPGFGVGVGGIPGVAGVPGVGGVPGVGGVPGVGISPEAQAAAAAKAAKYGAAGAGVLGGLVPGAPGAVPGVPGTGGVPGVGTPAAAAAKAAAKAAQFGLVPGVGVAPGVGVAPGVGVAPGVGLAPGVGVAPGVGVAPGVGVAPGIGPGGVAAAAKSAAKVAAKAQLRAAAGLGAGIPGLGVGVGVPGLGVGAGVPGLGVGAGVPGFGAGADEGVRRSLSPELREGDPSSSQHLPSTPSSPRVPGALAAAKAAKYGAAVPGVLGGLGALGGVGIPGGVVGAGPAAAAAAAKAAAKAAQFGLVGAAGLGGLGVGGLGVPGVGGLGGIPPAAAAKAAKYGAAGLGGVLGGAGQFPLGGVAARPGFGLSPIFPGGACLGKACGRKRK |
| 预测分子量 | 70.9 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ELN重组蛋白的3篇参考文献示例(内容基于领域常见研究方向，非真实文献，仅供格式参考)：
---
1. **文献名称**: *Recombinant Human Elastin-like Polypeptides for Tissue Engineering*
**作者**: Smith A, et al.
**摘要**: 研究利用大肠杆菌表达系统制备重组人弹性蛋白样多肽(ELPs)，验证其自组装成水凝胶的能力，并证明其支持成纤维细胞黏附与增殖，为软组织修复提供新材料。
2. **文献名称**: *ELN Gene Mutations and Arterial Disease: Functional Analysis via Recombinant Elastin*
**作者**: Johnson R, et al.
**摘要**: 通过构建携带ELN基因突变的弹性蛋白重组体，发现特定突变导致弹性纤维组装异常，揭示了遗传性主动脉狭窄(SVAS)的分子机制。
3. **文献名称**: *Thermo-Responsive ELP-Based Nanoparticles for Drug Delivery*
**作者**: Lee H, et al.
**摘要**: 开发温度敏感型重组弹性蛋白纳米颗粒，负载抗癌药物后实现肿瘤部位可控释放，体内实验显示增强的靶向性与疗效。
---
注：以上文献为模拟示例，实际研究需通过PubMed/Google Scholar等平台检索真实文献(关键词：recombinant elastin, ELN protein, ELPs)。
**Background of Recombinant Elastin (ELN) Protein**
Elastin (ELN), a critical extracellular matrix protein, provides elasticity and resilience to tissues such as skin, blood vessels, lungs, and ligaments. Its unique properties stem from a cross-linked network of tropoelastin monomers, rich in hydrophobic domains (e.g., VPGVG repeats) that enable reversible stretching. Native elastin is notoriously challenging to extract or synthesize due to its insolubility and complex post-translational modifications.
Recombinant elastin proteins, produced via genetic engineering, overcome these limitations. By expressing elastin-like polypeptides (ELPs) or tropoelastin derivatives in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells*), researchers achieve tunable molecular weights, sequences, and functionalities. These recombinant variants retain key biophysical features—thermoresponsiveness, self-assembly, and mechanical flexibility—while enabling precise customization for biomedical applications.
The development of recombinant ELN is driven by its potential in tissue engineering, drug delivery, and regenerative medicine. For instance, ELN-based hydrogels mimic native tissue mechanics, supporting cell growth in vascular grafts or skin substitutes. In drug delivery, thermoresponsive ELPs enable targeted payload release. Additionally, recombinant ELN avoids risks associated with animal-derived materials, such as immunogenicity or pathogen contamination.
Recent advances in synthetic biology and protein engineering further enhance ELN functionality. Hybrid constructs incorporating cell-binding motifs (e.g., RGD sequences) or fusion proteins improve bioactivity. Despite progress, challenges remain, including scalable production, cost-efficiency, and achieving in vivo-like cross-linking. Ongoing research focuses on optimizing expression systems, enzymatic modification strategies, and 3D bioprinting integration to unlock ELN’s full therapeutic potential.
In summary, recombinant elastin represents a versatile, biocompatible platform bridging natural material properties with modern biotechnological precision, offering transformative solutions for healthcare and material science.
×
