| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COL2A1 |
| Uniprot No | P02458-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1242-1487aa |
| 氨基酸序列 | DQAAGGLRQH DAEVDATLKS LNNQIESIRS PEGSRKNPAR TCRDLKLCHP EWKSGDYWID PNQGCTLDAM KVFCNMETGE TCVYPNPANV PKKNWWSSKS KEKKHIWFGE TINGGFHFSY GDDNLAPNTA NVQMTFLRLL STEGSQNITY HCKNSIAYLD EAAGNLKKAL LIQGSNDVEI RAEGNSRFTY TALKDGCTKH TGKWGKTVIE YRSQKTSRLP IIDIAPMDIG GPEQEFGVDI GPVCFL |
| 预测分子量 | 30 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COL2A1重组蛋白的3篇代表性文献的简要总结(注：内容基于公开研究领域知识整合，非真实文献直接引用)：
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1. **文献名称**：Recombinant human type II collagen induces chondrogenic differentiation of mesenchymal stem cells
**作者**：Smith et al., 2015
**摘要**：研究通过哺乳动物表达系统重组表达人源COL2A1蛋白，并证明其可诱导间充质干细胞向软骨细胞分化，为关节软骨修复提供了潜在生物材料。
2. **文献名称**：Expression and characterization of COL2A1 in insect cells for osteoarthritis therapy
**作者**：Chen & Lee, 2018
**摘要**：利用杆状病毒-昆虫细胞系统高效表达重组COL2A1蛋白，验证其结构与天然II型胶原相似性，并在体外模型中显示其抑制骨关节炎炎症反应的能力。
3. **文献名称**：COL2A1 mutations and recombinant protein rescue in zebrafish models
**作者**：Wang et al., 2020
**摘要**：通过斑马鱼模型研究COL2A1基因突变导致的软骨发育异常，发现外源性重组COL2A1蛋白可部分恢复突变体表型，提示其在遗传性软骨疾病中的治疗潜力。
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**备注**：以上内容为领域知识概括，实际文献需通过PubMed、Google Scholar等平台以“COL2A1 recombinant protein”为关键词检索获取原文。
The COL2A1 gene encodes the alpha-1 chain of type II collagen, a critical structural component of cartilage and essential for skeletal and joint development. As the primary collagen in hyaline cartilage, it forms a triple-helical structure through the assembly of three identical α1(II) chains, stabilized by post-translational modifications like hydroxylation. This fibrillar protein provides tensile strength to extracellular matrices, supporting tissue integrity in articular cartilage, intervertebral discs, and the vitreous body of the eye.
Recombinant COL2A1 protein is produced using expression systems (e.g., mammalian, insect, or yeast cells) to study its biological roles and therapeutic potential. Its applications span disease modeling, drug screening, and regenerative medicine, particularly in osteoarthritis research where cartilage degradation involves COL2A1 abnormalities. Mutations in COL2A1 are linked to genetic disorders such as Stickler syndrome (characterized by ocular, auditory, and skeletal defects) and achondrogenesis type II, highlighting its developmental significance.
In tissue engineering, recombinant COL2A1 serves as a scaffold material for cartilage repair strategies. Researchers also investigate its interactions with proteoglycans and signaling molecules to decipher cartilage homeostasis mechanisms. Current challenges include maintaining the protein's native conformation during recombinant production and addressing immunogenicity concerns in therapeutic contexts. Ongoing studies focus on optimizing expression systems and exploring engineered variants for improved stability and bioactivity in clinical applications.
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