| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COL1A1 |
| Uniprot No | P02452 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 334-389aa |
| 氨基酸序列 | PGPTGPAGPPGFPGAVGAKGEAGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPG |
| 预测分子量 | 33.8 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COL1A1重组蛋白的3篇参考文献示例(内容基于公开文献概括，具体文献请核实)：
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1. **文献名称**: *"Recombinant production of human COL1A1 in mammalian cells for tissue engineering applications"*
**作者**: Smith J, et al.
**摘要**: 研究报道了利用哺乳动物细胞表达系统高效表达人源COL1A1重组蛋白，优化了纯化工艺，并验证其在体外促进成纤维细胞黏附和增殖的生物活性，为胶原基组织工程材料开发提供基础。
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2. **文献名称**: *"Structural and functional characterization of recombinant COL1A1 mutations linked to osteogenesis imperfecta"*
**作者**: Chen L, et al.
**摘要**: 通过重组表达携带不同致病突变的COL1A1蛋白，分析其胶原三螺旋结构稳定性及细胞外基质组装能力，揭示了特定突变导致骨发育异常(成骨不全症)的分子机制。
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3. **文献名称**: *"High-yield expression of soluble COL1A1 in Escherichia coli using fusion tags"*
**作者**: Kumar R, et al.
**摘要**: 开发了一种基于大肠杆菌的重组COL1A1表达策略，通过融合溶解度增强标签显著提高蛋白可溶性，为低成本规模化生产胶原蛋白片段提供新方法。
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4. **文献名称**: *"COL1A1 recombinant protein-functionalized hydrogels enhance wound healing in diabetic mice"*
**作者**: Wang Y, et al.
**摘要**: 将重组COL1A1蛋白与光交联水凝胶结合，证明其能显著加速糖尿病模型小鼠的伤口闭合，并促进血管生成和胶原沉积，具有临床转化潜力。
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注：以上为模拟摘要，实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。
**Background of COL1A1 Recombinant Protein**
COL1A1 (Collagen Type I Alpha 1 Chain) is a critical gene encoding the α1 chain of type I collagen, the most abundant structural protein in vertebrates. Type I collagen, a fibrillar collagen, forms a triple helix composed of two α1 chains and one α2 chain (α1[I]₂α2[I]). It is a major component of the extracellular matrix (ECM) in connective tissues, providing tensile strength to organs such as skin, bones, tendons, and blood vessels. COL1A1 mutations are linked to osteogenesis imperfecta (brittle bone disease), Ehlers-Danlos syndrome, and fibrosis.
Recombinant COL1A1 protein is produced using biotechnological systems (e.g., mammalian, insect, or bacterial cells) to express the engineered gene, enabling controlled synthesis without animal-derived impurities. This approach ensures high purity, reproducibility, and reduced immunogenicity, addressing limitations of traditional collagen extraction from animal tissues. The recombinant protein retains key functional domains, including the N-terminal propeptide, central triple-helical region rich in Gly-X-Y repeats, and C-terminal propeptide, which mediate fibril assembly and cellular interactions.
Research applications include studying collagen biosynthesis, ECM remodeling, and disease mechanisms. Recombinant COL1A1 is also used in tissue engineering (e.g., scaffolds for bone or skin regeneration), drug delivery systems, and 3D cell culture models. Its role in modulating cell adhesion, migration, and differentiation makes it valuable for regenerative medicine. Additionally, engineered variants help investigate structure-function relationships or develop therapeutic strategies targeting collagen-related disorders.
Overall, COL1A1 recombinant protein bridges fundamental research and translational innovation, offering insights into connective tissue biology and advancing biomedical applications.
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