| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PEG |
| Uniprot No | P09466 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-180aa |
| 氨基酸序列 | MDIPQTKQDLELPKLAGTWHSMAMATNNISLMATLKAPLRVHITSLLPTPEDNLEIVLHRWENNSCVEKKVLGEKTENPKKFKINYTVANEATLLDTDYDNFLFLCLQDTTTPIQSMMCQYLARVLVEDDEIMQGFIRAFRPLPRHLWYLLDLKQMEEPCRF |
| 预测分子量 | 24.8 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篇关于PEG重组蛋白的经典文献概览：
1. **《PEGylation of recombinant proteins: challenges and solutions》**
作者：Veronese FM, Pasut G.
摘要：系统综述了PEG化技术对重组蛋白药物(如干扰素、生长因子)的药代动力学优化方法，重点讨论了PEG分子量选择、偶联位点控制及减少生物活性损失的策略。
2. **《Protein PEGylation: Basic science and biological applications》**
作者：Harris JM, Chess RB.
摘要：分析了PEG修饰对重组蛋白免疫原性降低的作用机制，通过案例(如PEG-天冬酰胺酶)验证了其在延长血液循环时间及降低抗体反应中的有效性。
3. **《Site-specific PEGylation of therapeutic proteins via engineered yeast》**
作者：Li L, et al.
摘要：提出了一种基于酵母表达系统的重组蛋白定点PEG化新方法，通过基因工程引入非天然氨基酸实现单一位点修饰，显著提高了产物均一性和生物活性保留率(>90%)。
注：以上文献均聚焦于重组蛋白的聚乙二醇化技术优化与应用价值，涵盖机制研究、工艺改进及临床效果验证等领域。实际文献检索建议通过PubMed/Web of Science用关键词"PEGylated recombinant protein"查询近年更新。
**Background of PEGylated Recombinant Proteins**
PEGylated recombinant proteins are engineered biologics created by covalently attaching polyethylene glycol (PEG) polymers to recombinant proteins, a process known as PEGylation. Recombinant proteins, produced via genetic engineering in host systems like *E. coli* or mammalian cells, have revolutionized medicine since the 1980s, enabling therapies for diseases such as diabetes (insulin) and cancer (monoclonal antibodies). However, their clinical utility is often limited by short half-lives, rapid clearance, immunogenicity, and instability.
PEGylation addresses these challenges. PEG, a biocompatible, hydrophilic polymer, forms a protective "shield" around the protein, enhancing solubility, reducing enzymatic degradation, and minimizing immune recognition. By increasing molecular size, PEGylation slows renal filtration, prolonging circulation time and reducing dosing frequency. The first PEGylated drug, PEG-adenosine deaminase (approved in 1990), treated severe combined immunodeficiency, showcasing the technology’s potential.
Over 30 PEGylated therapeutics are now approved, including PEG-interferon-α for hepatitis C and PEG-G-CSF for chemotherapy-induced neutropenia. PEGylation strategies have evolved, with site-specific modifications replacing random PEG attachment to improve consistency and activity retention.
Despite successes, challenges persist. Anti-PEG antibodies, reported in some patients, may reduce efficacy or cause hypersensitivity. Long-term PEG safety and biodegradability also remain debated, driving research into alternative polymers (e.g., polysaccharides, zwitterionic coatings). Nonetheless, PEGylation remains a cornerstone in biopharmaceuticals, balancing therapeutic performance with practical clinical use. Advances in protein engineering and polymer chemistry continue to refine its applications, ensuring PEGylated proteins remain vital in treating complex diseases.
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