| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COL1 |
| Uniprot No | Q07092 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1604aa |
| 氨基酸序列 | MWVSWAPGLWLLGLWATFGHGANTGAQCPPSQQEGLKLEHSSSLPANVTGFNLIHRLSLMKTSAIKKIRNPKGPLILRLGAAPVTQPTRRVFPRGLPEEFALVLTLLLKKHTHQKTWYLFQVTDANGYPQISLEVNSQERSLELRAQGQDGDFVSCIFPVPQLFDLRWHKLMLSVAGRVASVHVDCSSASSQPLGPRRPMRPVGHVFLGLDAEQGKPVSFDLQQVHIYCDPELVLEEGCCEILPAGCPPETSKARRDTQSNELIEINPQSEGKVYTRCFCLEEPQNSEVDAQLTGRISQKAERGAKVHQETAADECPPCVHGARDSNVTLAPSGPKGGKGERGLPGPPGSKGEKGARGNDCVRISPDAPLQCAEGPKGEKGESGALGPSGLPGSTGEKGQKGEKGDGGIKGVPGKPGRDGRPGEICVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGDKGSSGIPGKEGPGGKPGKPGVKGEKGDPCEVCPTLPEGFQNFVGLPGKPGPKGEPGDPVPARGDPGIQGIKGEKGEPCLSCSSVVGAQHLVSSTGASGDVGSPGFGLPGLPGRAGVPGLKGEKGNFGEAGPAGSPGPPGPVGPAGIKGAKGEPCEPCPALSNLQDGDVRVVALPGPSGEKGEPGPPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGTTGRPGLSGEPGVQGPAGPKGEKGDGCTACPSLQGTVTDMAGRPGQPGPKGEQGPEGVGRPGKPGQPGLPGVQGPPGLKGVQGEPGPPGRGVQGPQGEPGAPGLPGIQGLPGPRGPPGPTGEKGAQGSPGVKGATGPVGPPGASVSGPPGRDGQQGQTGLRGTPGEKGPRGEKGEPGECSCPSQGDLIFSGMPGAPGLWMGSSWQPGPQGPPGIPGPPGPPGVPGLQGVPGNNGLPGQPGLTAELGSLPIEQHLLKSICGDCVQGQRAHPGYLVEKGEKGDQGIPGVPGLDNCAQCFLSLERPRAEEARGDNSEGDPGCVGSPGLPGPPGLPGQRGEEGPPGMRGSPGPPGPIGPPGFPGAVGSPGLPGLQGERGLTGLTGDKGEPGPPGQPGYPGATGPPGLPGIKGERGYTGSAGEKGEPGPPGSEGLPGPPGPAGPRGERGPQGNSGEKGDQGFQGQPGFPGPPGPPGFPGKVGSPGPPGPQAEKGSEGIRGPSGLPGSPGPPGPPGIQGPAGLDGLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKTGHPGLPGPKGDCGKPGPPGSTGRPGAEGEPGAMGPQGRPGPPGHVGPPGPPGQPGPAGISAVGLKGDRGATGERGLAGLPGQPGPPGHPGPPGEPGTDGAAGKEGPPGKQGFYGPPGPKGDPGAAGQKGQAGEKGRAGMPGGPGKSGSMGPVGPPGPAGERGHPGAPGPSGSPGLPGVPGSMGDMVNYDEIKRFIRQEIIKMFDERMAYYTSRMQFPMEMAAAPGRPGPPGKDGAPGRPGAPGSPGLPGQIGREGRQGLPGVRGLPGTKGEKGDIGIGIAGENGLPGPPGPQGPPGYGKMGATGPMGQQGIPGIPGPPGPMGQPGKAGHCNPSDCFGAMPMEQQYPPMKTMKGPFG |
| 预测分子量 | 157 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篇与COL1重组蛋白相关的参考文献摘要：
1. **"Recombinant human type I collagen produced in mammalian cells"**
- **作者**: Yang C. et al. (2014)
- **摘要**: 该研究报道了利用HEK293哺乳动物细胞系统高效表达重组人源I型胶原蛋白(rhCOL1)，并通过质谱和圆二色光谱验证其正确折叠的三螺旋结构，证明其与天然胶原相似的生物活性。
2. **"Baculovirus-mediated production of human collagen type I in insect cells"**
- **作者**: Fertala A. et al. (2001)
- **摘要**: 文章描述了利用杆状病毒-昆虫细胞系统表达重组人COL1.优化了蛋白纯化流程，并证明重组蛋白具有促进成纤维细胞粘附和增殖的能力，为大规模生产提供了可行方案。
3. **"Engineered recombinant collagen scaffolds for 3D cell culture models"**
- **作者**: Lee P. et al. (2019)
- **摘要**: 研究开发了基于重组COL1的水凝胶支架，通过调整交联密度调控力学性能，成功构建了仿生3D肿瘤模型，证实其支持癌细胞侵袭和药物筛选的潜力。
注：以上文献信息为示例性质，实际引用时请核对具体论文来源及发表细节。如需精准文献，建议通过PubMed或Google Scholar以关键词"recombinant collagen type I"、"COL1 expression"等检索近期研究。
**Background of COL1 Recombinant Protein**
Collagen type I (COL1), the most abundant extracellular matrix protein in vertebrates, is a key structural component of connective tissues, including skin, bone, tendons, and ligaments. It is composed of two α1 chains and one α2 chain, forming a triple-helical structure that provides mechanical strength and stability. Traditionally, collagen is isolated from animal sources (e.g., bovine or porcine tissues), but concerns over pathogen transmission, immunogenicity, and batch variability have driven the development of recombinant collagen production.
Recombinant COL1 is engineered using heterologous expression systems, such as mammalian cells (e.g., HEK293), yeast, or bacteria, to produce humanized collagen with controlled purity and consistency. The gene sequences encoding α1 and α2 chains are cloned into expression vectors, enabling precise modification of functional domains (e.g., integrin-binding sites) or incorporation of non-natural amino acids for enhanced stability or bioactivity. Unlike animal-derived collagen, recombinant COL1 avoids religious and ethical restrictions, reduces allergenicity risks, and allows customization for specific biomedical applications.
Its applications span tissue engineering (e.g., skin grafts, bone scaffolds), drug delivery systems, and 3D cell culture models. Recombinant COL1 also serves as a critical tool in studying collagen-related diseases, such as fibrosis and osteogenesis imperfecta. Challenges remain in scaling production, achieving proper post-translational modifications (e.g., hydroxylation of proline/lysine), and replicating native fibril assembly. Advances in synthetic biology and bioprocessing continue to optimize its functional fidelity, positioning recombinant COL1 as a safer, scalable alternative to traditional collagen sources in regenerative medicine and biomanufacturing.
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