| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PPL |
| Uniprot No | O60437 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 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. |
以下为模拟的参考文献示例(非真实文献，供格式参考)：
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1. **"Efficient Expression and Purification of Recombinant PPL in Escherichia coli"**
*Authors: Zhang, L.; Chen, W.; Wang, Y.*
*摘要：* 本研究优化了Pseudomonas putida脂肪酶(PPL)在大肠杆菌中的重组表达条件，采用His标签纯化系统获得高活性酶，为工业生物催化应用提供高效生产方案。
2. **"Yeast-Based Platform for Scalable Production of Therapeutic PPL Fusion Proteins"**
*Authors: Müller, S.; Schmidt, H.; Braun, F.*
*摘要：* 通过毕赤酵母表达系统实现人源化PPL重组蛋白的可控分泌表达，验证其在代谢疾病模型中的治疗潜力，证明其稳定性与生物活性优于传统制备方法。
3. **"CRISPR/Cas9-Mediated Engineering of PPL in Mammalian Cells for Biomedical Applications"**
*Authors: Gupta, R.; Lee, T.; Park, J.H.*
*摘要：* 利用CRISPR技术对哺乳动物细胞系进行基因编辑，实现重组PPL的定向修饰与功能增强，显著提升其在靶向药物递送系统中的效率。
4. **"Structural and Functional Analysis of Recombinant PPL Mutants for Industrial Biocatalysis"**
*Authors: Silva, M.; Costa, R.; Oliveira, P.*
*摘要：* 通过理性设计获得耐高温、耐有机溶剂的PPL突变体，解析其晶体结构并评估其在生物柴油生产中的催化性能，为酶工程改造提供理论依据。
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如需真实文献，建议在PubMed、Web of Science等平台检索关键词“recombinant PPL protein”、“Pseudomonas lipase production”或结合具体应用方向(如“PPL enzyme engineering”)。
PPL (Pichia-produced recombinant human lactoferrin) is a biotechnologically engineered protein derived from the expression of the human lactoferrin gene in the yeast *Pichia pastoris*. Lactoferrin, a multifunctional glycoprotein naturally found in mammalian secretions (e.g., milk, tears), plays critical roles in immune modulation, iron metabolism, and antimicrobial activity. Traditional extraction from natural sources (e.g., bovine milk) faces challenges like low yield, ethical concerns, and potential allergenicity. Recombinant production addresses these limitations by enabling scalable, cost-effective, and animal-free manufacturing.
The choice of *Pichia pastoris* as an expression host offers advantages such as high protein yield, post-translational modifications (e.g., glycosylation), and compatibility with large-scale fermentation. PPL retains structural and functional equivalence to native human lactoferrin, including iron-binding capacity and antimicrobial properties. This has driven its applications in nutraceuticals, infant formula (mimicking breast milk benefits), biomedical products (wound healing, antiviral therapies), and functional foods. Regulatory approvals (e.g., GRAS status in the U.S.) further support its commercial viability.
Research continues to optimize PPL's production efficiency and explore novel applications, such as drug delivery systems or anti-inflammatory agents. However, challenges remain in ensuring consistent glycosylation patterns and meeting stringent regulatory standards across global markets. Overall, PPL exemplifies the convergence of synthetic biology and industrial biotechnology to meet growing demand for sustainable, high-value protein therapeutics.
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