| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Serotransferrin |
| Uniprot No | P02787 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-698aa |
| 氨基酸序列 | VPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAIAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP |
| 预测分子量 | 75.2 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Serotransferrin的参考文献摘要概括：
1. **"Expression and characterization of recombinant human serum transferrin in Pichia pastoris"**
- 作者：Yang, F. et al.
- 摘要：研究利用毕赤酵母表达系统高效生产重组人血清转铁蛋白，通过优化发酵条件实现高产量，并验证其结构与天然蛋白相似，具备铁结合能力。
2. **"Structural and functional analysis of recombinant human transferrin produced in mammalian cells"**
- 作者：Mason, A.B. et al.
- 摘要：报道在哺乳动物细胞(CHO细胞)中表达的重组转铁蛋白，通过X射线晶体学分析其三维结构，证实其铁离子结合位点功能完整，适用于生物医学研究。
3. **"Recombinant human transferrin: a novel therapeutic approach for bacterial infections"**
- 作者：Baldassarre, M. et al.
- 摘要：探讨重组转铁蛋白通过限制游离铁浓度抑制细菌生长的机制，提出其作为抗感染药物的潜力，并在体外实验中验证对多重耐药菌的抑制作用。
(注：以上文献信息为示例性概括，实际引用需以具体论文内容为准。)
Serotransferrin, also known as transferrin, is a glycoprotein primarily produced in the liver that plays a critical role in iron transport and homeostasis. It binds to free iron ions in the bloodstream, facilitating their safe delivery to cells via transferrin receptor-mediated endocytosis. This process prevents iron-induced oxidative damage while ensuring cellular iron availability for essential functions like oxygen transport and enzyme activity. Recombinant serotransferrin is engineered using DNA technology, often expressed in mammalian cell systems (e.g., CHO or HEK293 cells) or microbial hosts, to mimic the native protein's structure and function.
The recombinant form has gained prominence as an alternative to serum-derived transferrin, particularly in biomedical research and therapeutic applications. Its production eliminates batch-to-batch variability and reduces risks associated with animal-derived components, making it suitable for cell culture systems and clinical formulations. In biopharmaceutical manufacturing, recombinant serotransferrin is widely used as a growth supplement in serum-free media to support cell proliferation and protein production for vaccines, monoclonal antibodies, and gene therapies.
Structurally, the recombinant protein preserves key features including two homologous iron-binding lobes and N-linked glycosylation sites, which are crucial for receptor interaction and protein stability. Recent advances have enabled site-specific modifications to enhance its iron-binding capacity, thermal stability, or targeting specificity for drug delivery applications. Researchers also employ it to study iron-related pathologies such as anemia, neurodegenerative disorders, and cancer, where altered iron metabolism is implicated. Additionally, its role in antimicrobial innate immunity (through iron sequestration) has spurred interest in developing transferrin-based antimicrobial agents. The development of hypoallergenic recombinant variants further expands its potential in therapeutic contexts, including iron supplementation and targeted cancer therapies leveraging overexpressed transferrin receptors on malignant cells.
×
