| 纯度 | >90%SDS-PAGE. |
| 种属 | Drosophila |
| 靶点 | resilin |
| Uniprot No | Q9V7U0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 342-620aa |
| 氨基酸序列 | PAKYEFNYQVEDAPSGLSFGHSEMRDGDFTTGQYNVLLPDGRKQIVEYEADQQGYRPQIRYEGDANDGSGPSGPGGPGGQNLGADGYSSGRPGNGNGNGNGGYSGGRPGGQDLGPSGYSGGRPGGQDLGAGGYSNGKPGGQDLGPGGYSGGRPGGQDLGRDGYSGGRPGGQDLGASGYSNGRPGGNGNGGSDGGRVIIGGRVIGGQDGGDQGYSGGRPGGQDLGRDGYSSGRPGGRPGGNGQDSQDGQGYSSGRPGQGGRNGFGPGGQNGDNDGSGYRY |
| 预测分子量 | 34.9 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3篇关于重组resilin蛋白的经典文献摘要概览：
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1. **标题**: *Synthesis and properties of crosslinked recombinant pro-resilin*
**作者**: Elvin, C.M. et al.
**摘要**: 该研究首次成功克隆并表达了果蝇resilin基因的重组蛋白，通过大肠杆菌系统生产。交联后的材料展现出卓越的弹性(回弹率>97%)，为仿生弹性材料开发奠定基础。
2. **标题**: *Recombinant resilin-based biohybrid tailorable hydrogels*
**作者**: Qin, G. et al.
**摘要**: 提出将重组resilin与蚕丝蛋白结合，构建可调控力学性能的水凝胶。材料兼具高延展性(>500%应变)与生物相容性，适用于柔性生物传感器设计。
3. **标题**: *Resilin-like polypeptide hydrogel engineering for stem cell niches*
**作者**: Su, R.S. et al.
**摘要**: 开发了光交联重组resilin水凝胶作为干细胞培养支架，证实其支持间充质干细胞的粘附与分化，在软骨组织工程中展现潜力。
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*注：以上文献发表于2005-2015年间，近年研究可能涉及基因编辑优化表达(如CRISPR修饰宿主)或3D生物打印应用。如需更新文献建议检索近年期刊如《ACS Biomaterials Science & Engineering》。*
Resilin is a remarkable elastomeric protein first identified in insect cuticles, where it plays a critical role in energy storage and resilience. Natural resilin, found in specialized structures like the jumping organs of fleas and wing hinges of flies, exhibits exceptional elasticity, efficiency (>90% energy return), and fatigue resistance. These properties stem from its unique molecular architecture—a network of randomly coiled polypeptide chains cross-linked by di- and tri-tyrosine bonds formed via enzymatic oxidation.
The interest in recombinant resilin emerged from the need to replicate these biomechanical traits for biomedical and material science applications. Early studies focused on cloning resilin-like sequences (e.g., the *Drosophila* resilin gene *CG15920*), revealing repetitive motifs rich in glycine, proline, and tyrosine. Advances in genetic engineering enabled the production of resilin-based proteins in heterologous systems like *E. coli*, yeast, or insect cells. Recombinant resilin variants often include modular domains to enhance functionality—for instance, cell-binding motifs for tissue engineering or cross-linking sites for tunable mechanical properties.
Recombinant resilin has shown promise in creating biocompatible, elastic biomaterials. Potential applications include vascular grafts, cartilage repair scaffolds, and dynamic drug delivery systems. Its biodegradability and non-toxic degradation products further support its use in vivo. Challenges remain in precisely mimicking native resilin's mechanical performance, as synthetic cross-linking methods and purification processes can alter network dynamics. Current research explores hybrid materials combining resilin with synthetic polymers or other structural proteins to optimize strength and elasticity.
Overall, resilin-inspired proteins represent a frontier in bioengineered materials, merging evolutionary optimization with modern biotechnological precision to address needs in regenerative medicine and soft robotics.
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