| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COIL |
| Uniprot No | P38432 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-576aa |
| 氨基酸序列 | MAASETVRLRLQFDYPPPATPHCTAFWLLVDLNRCRVVTDLISLIRQRFGFSSGAFLGLYLEGGLLPPAESARLVRDNDCLRVKLEERGVAENSVVISNGDINLSLRKAKKRAFQLEEGEETEPDCKYSKKHWKSRENNNNNEKVLDLEPKAVTDQTVSKKNKRKNKATCGTVGDDNEEAKRKSPKKKEKCEYKKKAKNPKSPKVQAVKDWANQRCSSPKGSARNSLVKAKRKGSVSVCSKESPSSSSESESCDESISDGPSKVTLEARNSSEKLPTELSKEEPSTKNTTADKLAIKLGFSLTPSKGKTSGTTSSSSDSSAESDDQCLMSSSTPECAAGFLKTVGLFAGRGRPGPGLSSQTAGAAGWRRSGSNGGGQAPGASPSVSLPASLGRGWGREENLFSWKGAKGRGMRGRGRGRGHPVSCVVNRSTDNQRQQQLNDVVKNSSTIIQNPVETPKKDYSLLPLLAAAPQVGEKIAFKLLELTSSYSPDVSDYKEGRILSHNPETQQVDIEILSSLPALREPGKFDLVYHNENGAEVVEYAVTQESKITVFWKELIDPRLIIESPSNTSSTEPA |
| 预测分子量 | 62,6 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COIL重组蛋白的示例参考文献(内容为模拟，非真实文献)：
1. **"Engineering Recombinant Coiled-Coil (COIL) Proteins for Enhanced Stability"**
*作者：Zhang, Y. et al.*
**摘要**：研究通过理性设计优化COIL结构域的重组蛋白稳定性，利用点突变和分子动力学模拟，证明改造后的重组蛋白在高温和极端pH条件下仍保持结构完整性。
2. **"Expression and Functional Characterization of COIL-Fusion Antigens in Vaccine Development"**
*作者：Rodriguez, M. & Kumar, S.*
**摘要**：报道在大肠杆菌中高效表达含有COIL结构域的重组融合抗原，验证其诱导特异性免疫反应的能力，为疫苗载体设计提供新策略。
3. **"COIL-Mediated Self-Assembly of Recombinant Protein Nanoparticles"**
*作者：Lee, J. et al.*
**摘要**：利用COIL结构域的自组装特性，构建基于重组蛋白的纳米颗粒，并证明其在靶向药物递送系统中的高效负载和控释性能。
4. **"Structural and Biophysical Analysis of Recombinant COIL Domains in Protein-Protein Interactions"**
*作者：Wei, X. et al.*
**摘要**：通过冷冻电镜和表面等离子体共振技术，解析重组COIL蛋白与配体结合的分子机制，揭示其介导特异性相互作用的关键残基。
如需真实文献，建议在PubMed或Web of Science中搜索关键词“recombinant coiled-coil protein”或“COIL domain expression”获取近期研究。
COIL (clusters of regularly interspaced coiled-coil motifs) recombinant proteins are engineered biomolecules inspired by naturally occurring coiled-coil structural domains. Coiled-coil motifs, characterized by intertwined alpha-helices stabilized by hydrophobic interactions, are ubiquitous in proteins like collagen, myosin, and viral fusion peptides. These motifs confer mechanical stability, modularity, and programmable self-assembly properties, making them attractive for synthetic biology applications.
The development of COIL recombinant proteins leverages advances in genetic engineering and computational design. Researchers modify coiled-coil sequences to control folding, stability, and interaction specificity. For instance, altering heptad repeat patterns (typical 7-residue sequences in coiled coils) can tune oligomerization states (dimers, trimers, etc.) or environmental responsiveness to pH or temperature. Such precision enables custom-designed protein architectures for nanotechnology, drug delivery, and biomaterials.
Applications span multiple fields. In vaccine development, COIL proteins serve as antigen-display platforms, mimicking viral capsid geometries to enhance immune responses. In tissue engineering, they form tunable hydrogels through reversible coiled-coil interactions. Their modularity also facilitates fusion with functional domains (e.g., enzymes, targeting peptides), creating multifunctional biologics.
Production typically involves expression in microbial systems (E. coli, yeast), though mammalian cells are used for complex post-translational modifications. Challenges include optimizing solubility, preventing aggregation, and ensuring proper folding. Recent innovations in machine learning-assisted design and high-throughput screening have accelerated the engineering of COIL proteins with desired properties.
As a bridge between synthetic biology and materials science, COIL recombinant proteins represent a versatile toolkit for creating programmable biomaterials, with ongoing research focusing on smart therapeutics, biosensors, and sustainable alternatives to synthetic polymers.
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艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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