| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PIIINP |
| 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PIIINP(III型前胶原氨基端肽)重组蛋白的模拟参考文献示例，内容基于领域内常见研究方向概括，仅供参考：
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1. **标题**: *"Recombinant PIIINP as a Serum Biomarker for Liver Fibrosis Staging"*
**作者**: Smith, J. et al.
**摘要**: 研究通过重组技术表达PIIINP蛋白，验证其在肝纤维化患者血清中的浓度与组织病理学分期的相关性，证明其作为非侵入性生物标志物的潜力。
2. **标题**: *"Therapeutic Efficacy of Recombinant PIIINP in Attenuating Pulmonary Fibrosis in Murine Models"*
**作者**: Lee, H. et al.
**摘要**: 在小鼠肺纤维化模型中，外源性重组PIIINP通过调节胶原代谢平衡，显著降低肺组织纤维化面积，提示其治疗纤维化疾病的可能机制。
3. **标题**: *"Development of a High-Sensitivity ELISA Using Recombinant PIIINP for Early Fibrosis Detection"*
**作者**: Garcia, R. et al.
**摘要**: 利用重组PIIINP建立新型ELISA检测方法，与传统检测相比灵敏度提升3倍，可早期识别肝硬化及心血管疾病患者的纤维化进程。
4. **标题**: *"Molecular Interaction Between Recombinant PIIINP and TGF-β Signaling Pathways"*
**作者**: Chen, L. et al.
**摘要**: 通过体外实验揭示重组PIIINP与TGF-β1受体的竞争性结合机制，为干预纤维化关键信号通路提供理论依据。
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**注**：以上文献为示例性内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。
**Background of PIIINP Recombinant Protein**
PIIINP (Procollagen Type III N-Terminal Propeptide) is a biologically active peptide fragment released during the synthesis of type III collagen, a major component of the extracellular matrix (ECM). Type III collagen is predominantly produced by fibroblasts and plays a critical role in maintaining tissue structure, particularly in organs such as the liver, skin, and blood vessels. During collagen maturation, the precursor molecule procollagen undergoes enzymatic cleavage, releasing PIIINP into bodily fluids. Elevated levels of PIIINP in serum or plasma are strongly associated with active fibrogenesis, making it a well-established biomarker for diagnosing and monitoring fibrotic diseases, such as liver cirrhosis, pulmonary fibrosis, and systemic sclerosis.
The recombinant form of PIIINP is generated using genetic engineering techniques, often expressed in microbial or mammalian cell systems. This approach ensures high purity, consistency, and scalability compared to native PIIINP isolated from biological samples. Recombinant PIIINP retains the immunogenic and structural properties of the natural peptide, enabling its use in immunoassays (e.g., ELISA) to quantify collagen turnover in clinical or research settings. It serves as a critical reference standard for calibrating diagnostic kits and validating experimental models of fibrosis.
Beyond diagnostics, PIIINP recombinant protein is utilized in mechanistic studies to investigate ECM remodeling, fibroblast activation, and the efficacy of antifibrotic therapies. Its role in fibrosis pathways has also sparked interest in drug development, targeting collagen synthesis or degradation.
In summary, PIIINP recombinant protein bridges clinical diagnostics and biomedical research, offering a reliable tool to understand and address fibrotic disorders, which affect millions globally and lack definitive therapies. Its production and application highlight the convergence of biotechnology and translational medicine.
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