| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PINP |
| Uniprot No | A0A0K3AVY3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-164aa |
| 氨基酸序列 | MGVFSSPMSTLRWVTLFAALLSLLEWGTAHEDIVMDGDQVVQQQGRSCDPQRLSACRDYLQRRREQPSERCCEELQRMSPHCRCRAIERALDQSQSYDSSTDSDSQDGAPLNQRRRRRGEGRGREEEEAVERAEELPNRCNLRESPRRCDIRRHSRYSIIGGSD |
| 预测分子量 | 18,9 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PINP重组蛋白相关的文献摘要示例：
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1. **"Development of a monoclonal antibody-based ELISA for detection of human procollagen type I N-terminal propeptide in serum"**
*H. Orum et al. (1993)*
该研究开发了一种基于单克隆抗体的ELISA方法，利用重组人PINP作为标准品，用于检测血清中的PINP水平，提高了骨代谢评估的特异性。
2. **"Clinical utility of bone turnover markers in osteoporosis management"**
*M.J. Seibel (2009)*
综述讨论了PINP作为骨形成标志物的临床意义，并指出重组PINP蛋白在标准化检测方法中的关键作用，以减少不同实验室间的检测变异。
3. **"Standardization of PINP immunoassays: The role of recombinant antigens"**
*A.R. Eastell et al. (2017)*
研究提出通过重组PINP蛋白统一校准品，解决不同检测系统间结果不一致的问题，强调重组蛋白对提高临床数据可比性的重要性。
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注：以上文献为示例，实际引用需核实具体来源及细节。如需准确文献，建议通过PubMed或Web of Science以“recombinant PINP protein”为关键词检索。
PINP (Procollagen I Intact N-Terminal Propeptide) recombinant protein is a engineered form of a natural biomarker involved in collagen synthesis. As a cleavage product of type I procollagen, PINP reflects the rate of collagen type I formation, which constitutes ~90% of bone organic matrix and is critical in connective tissue remodeling.
In physiological contexts, PINP is released during the extracellular processing of procollagen to collagen fibrils. Its serum/plasma levels correlate with bone formation activity, making it a key clinical biomarker for bone metabolic disorders like osteoporosis, Paget's disease, and bone metastasis monitoring. However, natural PINP isolation from biological fluids faces challenges in purity and scalability.
Recombinant PINP technology addresses these limitations through genetic engineering. By expressing PINP-coding sequences in bacterial (e.g., E. coli) or mammalian cell systems, researchers produce standardized, high-purity PINP proteins. This enables consistent quality for diagnostic applications, including ELISA calibration and quality control reagents. Recent advances also explore its therapeutic potential in tissue engineering, particularly in scaffolds for bone regeneration where collagen matrix deposition requires precise regulation.
Current research focuses on optimizing post-translational modifications (critical for antibody recognition in assays) and developing mutant variants to study collagen maturation pathways. As personalized medicine evolves, recombinant PINP serves as both a diagnostic tool and a research reagent for understanding bone biology and developing targeted therapies.
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