| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PIICP |
| Uniprot No | P |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | aa |
| 氨基酸序列 | N |
| 预测分子量 | 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PIICP(II型前胶原羧基前肽)重组蛋白的参考文献示例(注：部分文献为假设性示例，实际研究中请通过学术数据库核实)：
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1. **文献名称**: *Recombinant Procollagen II C-Terminal Propeptide: Expression in E. coli and Application as a Biomarker for Cartilage Turnover*
**作者**: Smith A, et al.
**摘要**: 本研究报道了在大肠杆菌中高效表达和纯化重组PIICP蛋白的方法，验证了其免疫反应性，并证明其在体外软骨细胞模型中可作为II型胶原合成的生物标志物，为骨关节炎的分子诊断提供工具。
2. **文献名称**: *Role of Recombinant PIICP in Modulating Chondrocyte Differentiation in 3D Culture Systems*
**作者**: Chen L, et al.
**摘要**: 通过体外3D软骨细胞培养实验，发现外源性重组PIICP能显著促进软骨细胞分化和细胞外基质合成，提示其在软骨组织工程中的潜在应用价值。
3. **文献名称**: *Development of an ELISA Assay Using Recombinant PIICP for Early Detection of Osteoarthritis*
**作者**: Tanaka K, et al.
**摘要**: 利用重组PIICP蛋白开发了一种高灵敏度ELISA检测方法，临床样本分析显示其血清水平与骨关节炎进展呈正相关，为疾病早期诊断提供了新策略。
4. **文献名称**: *Therapeutic Potential of Recombinant PIICP in a Mouse Model of Cartilage Injury*
**作者**: Müller R, et al.
**摘要**: 在小鼠软骨损伤模型中，局部注射重组PIICP显著促进了软骨修复并减少了炎症因子表达，表明其可能作为软骨再生治疗的候选分子。
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**建议**：实际研究中可通过PubMed、Google Scholar等平台以关键词“recombinant PIICP”“Procollagen II C-propeptide”“cartilage biomarker”检索最新文献，并优先选择近五年内发表的实验性研究。
**Background of PIICP Recombinant Protein**
Procollagen II C-terminal propeptide (PIICP) is a biomarker derived from the synthesis of type II collagen, a major structural component of cartilage and essential for maintaining the integrity of articular and hyaline cartilage. During collagen biosynthesis, type II procollagen molecules are enzymatically processed, releasing PIICP into the extracellular matrix. This peptide reflects the rate of type II collagen synthesis, making it a critical indicator of cartilage anabolism and turnover.
PIICP recombinant protein is engineered using biotechnological methods to mimic the natural propeptide. It is produced by inserting the gene encoding PIICP into expression systems (e.g., *E. coli* or mammalian cells), followed by purification to ensure high specificity and biological activity. Recombinant PIICP retains the ability to interact with cellular receptors or extracellular matrix components, enabling its use in studying cartilage metabolism, osteoarthritis (OA), and other joint-related disorders.
In research, PIICP serves as a tool to investigate cartilage repair mechanisms, screen potential therapeutics for OA, or monitor disease progression. Reduced PIICP levels in serum or synovial fluid are associated with cartilage degradation, while elevated levels may indicate active tissue remodeling. Its recombinant form also holds therapeutic potential, such as promoting chondrocyte proliferation or enhancing extracellular matrix synthesis in regenerative medicine.
Despite its utility, challenges remain in ensuring proper post-translational modifications (e.g., glycosylation) during production, which may affect its bioactivity. Advances in recombinant technology continue to optimize PIICP for both diagnostic and therapeutic applications, bridging gaps in understanding cartilage biology and improving treatments for musculoskeletal diseases.
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