| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | col |
| Uniprot No | P18000 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 74-180aa |
| 氨基酸序列 | LAKNKGKIPGLKIDQKIRGQMPERGWTEDDIKNTVSNGATGTSFDKRSPKKTPPDYLGRNDPATVYGSPGKYVVVNDRTGEVTQISDKTDPGWVDDSRIQWGNKNDQ |
| 预测分子量 | 24.8 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. |
以下是关于重组胶原蛋白(COL)的3篇代表性文献摘要整理：
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1. **文献名称**：Production of recombinant human type III collagen in Escherichia coli
**作者**：Yu, Z., et al.
**摘要**：该研究开发了利用大肠杆菌表达系统高效生产重组人源III型胶原蛋白的方法。通过密码子优化和温度调控策略，实现了可溶性蛋白的高产量表达，产物经纯化后显示出与天然胶原相似的三螺旋结构和生物相容性，为规模化生产奠定了基础。
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2. **文献名称**：Recombinant collagen-based scaffolds for tissue engineering applications
**作者**：Rho, K.S., et al.
**摘要**：研究团队将重组COL1A1蛋白与壳聚糖复合，制备出具有多孔结构的三维支架。体外实验显示该材料能显著促进成纤维细胞增殖和细胞外基质沉积，动物实验中成功应用于皮肤再生，证实其在组织修复领域的潜力。
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3. **文献名称**：High-level expression of recombinant human collagen in Pichia pastoris
**作者**：Zhang, Y., et al.
**摘要**：采用毕赤酵母表达系统，通过多拷贝整合策略实现重组人胶原蛋白的高效分泌表达。优化后的发酵工艺使产量达到5.8 g/L，产物经质谱验证具有完整羟脯氨酸修饰，力学测试显示其纤维强度优于哺乳动物细胞来源的胶原蛋白。
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注：以上文献为虚拟示例，实际研究中建议通过PubMed或Web of Science检索关键词“recombinant collagen”、“COL expression”等获取具体文献。如需特定研究方向(如医学应用、结构分析)，可进一步限定检索范围。
Collagen (COL) recombinant proteins are engineered versions of collagen, a critical structural protein found in extracellular matrices in animals. Naturally, collagen provides tensile strength and elasticity to tissues like skin, bones, tendons, and cartilage. It consists of three polypeptide chains forming a triple helix, with over 28 types identified in humans (e.g., COL I, II, III), each with distinct tissue-specific roles. However, natural collagen extraction from animal or human sources faces challenges, including immunogenicity, batch variability, and ethical concerns.
Recombinant collagen production addresses these limitations. Using genetic engineering, collagen-encoding genes (e.g., COL1A1. COL1A2) are inserted into host systems like bacteria, yeast, or mammalian cells. These systems synthesize collagen chains, which are purified and assembled into functional triple helices. Modifications, such as incorporating non-natural amino acids or fusion tags, enhance stability, solubility, or bioactivity. Recombinant collagen also allows customization of sequence domains to mimic specific collagen types or engineer novel functions.
Applications span biomedicine and biotechnology. In tissue engineering, recombinant COL proteins serve as scaffolds for regenerating skin, cartilage, or bone. They are used in wound dressings, drug delivery systems, and cosmetic formulations due to their biocompatibility and low immunogenic risk. Additionally, recombinant collagen enables precise studies of collagen-related diseases (e.g., osteogenesis imperfecta) and cell-matrix interactions. Challenges remain in scaling production, achieving proper post-translational modifications (e.g., hydroxylation), and replicating the mechanical properties of native collagen. Ongoing advances in synthetic biology and bioprocessing aim to optimize cost, yield, and functionality for broader clinical adoption.
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