| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LTF |
| Uniprot No | P02788 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-711aa |
| 氨基酸序列 | MKLVFLVLLFLGALGLCLAGRRRRSVQWCAVSQPEATKCFQWQRNMRKVC GPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAE VYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGRRRTAGWNVPIG TLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENK CAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELL CPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGK DKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQN LRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDC IALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDR PVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQT GSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTG AFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKR KPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDK FCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTS PLLEACEFLRK |
| 预测分子量 | 105 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篇关于重组乳铁蛋白(LTF)的虚构参考文献示例(仅供格式参考，非真实文献)：
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1. **文献名称**: "Efficient Expression and Purification of Recombinant Human Lactoferrin in *E. coli*"
**作者**: Wang, X. et al.
**摘要**: 研究通过优化大肠杆菌表达系统，成功实现重组人乳铁蛋白的高效可溶性表达。经离子交换层析纯化后，蛋白表现出与天然LTF相似的铁结合能力，并证实对金黄色葡萄球菌具有显著抑菌活性。
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2. **文献名称**: "Functional Characterization of Yeast-Expressed Bovine Lactoferrin"
**作者**: Kim, S. & Lee, J.
**摘要**: 利用毕赤酵母系统表达牛源重组LTF，通过糖基化修饰分析发现其免疫调节功能优于原核表达产物。动物实验表明该蛋白能有效缓解肠道炎症，提示其在功能性食品中的应用潜力。
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3. **文献名称**: "Structural Optimization of Recombinant Lactoferrin for Enhanced Antiviral Activity"
**作者**: Gupta, R. et al.
**摘要**: 通过定点突变改造重组LTF的N端结构域，显著提升其抑制HSV-1病毒进入宿主细胞的能力。晶体结构解析揭示了关键氨基酸残基与病毒包膜蛋白的相互作用机制。
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4. **文献名称**: "Large-Scale Production of Recombinant Porcine Lactoferrin and Its Application in Weaned Piglets"
**作者**: Müller, T. et al.
**摘要**: 开发CHO细胞规模化生产重组猪乳铁蛋白的工艺，临床实验证实添加该蛋白的饲料可降低断奶仔猪腹泻发生率，并促进肠道菌群平衡，验证其替代抗生素的可行性。
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**提示**：实际研究中建议通过PubMed、Web of Science等平台，以关键词"recombinant lactoferrin"+"expression"/"function"检索近五年文献，重点关注《International Journal of Biological Macromolecules》《Biotechnology Progress》等期刊。
**Background of Recombinant Lactoferrin (LTF)**
Lactoferrin (LTF), an iron-binding glycoprotein belonging to the transferrin family, is naturally found in mammalian secretions such as milk, saliva, and tears. It plays multifaceted roles in innate immunity, including antimicrobial, antiviral, and anti-inflammatory activities, largely attributed to its ability to sequester iron or interact with pathogens and host cells. Traditionally, lactoferrin is isolated from bovine or human milk, but limitations in yield, cost, and ethical concerns drive the development of recombinant lactoferrin (rLTF) through genetic engineering.
Recombinant DNA technology enables the production of rLTF in heterologous host systems like bacteria, yeast, plants, or mammalian cells. This approach overcomes scalability issues and ensures pathogen-free production. For instance, yeast systems (e.g., *Pichia pastoris*) are favored for their ability to perform post-translational modifications, enhancing protein functionality comparable to native LTF. Bacterial systems, while cost-effective, often yield non-glycosylated forms, which may affect bioactivity.
rLTF retains the core functions of natural lactoferrin, making it valuable in pharmaceuticals, nutraceuticals, and cosmetics. It is explored as an antimicrobial agent, immune modulator, and iron supplement. In food industries, rLTF serves as a natural preservative or nutritional enhancer. Recent research also highlights its potential in treating infections, cancer, and metabolic disorders.
Despite progress, challenges persist in optimizing expression systems, purification processes, and ensuring consistent bioactivity. Regulatory approvals and cost-effective large-scale production remain critical hurdles. Advances in synthetic biology and precision fermentation may further refine rLTF applications, positioning it as a sustainable alternative to meet growing demand across health and industrial sectors.
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