| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | apoTf |
| Uniprot No | P |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | aa |
| 氨基酸序列 | N |
| 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. |
以下是3-4篇与重组载脂蛋白转铁蛋白(apoTf)相关的示例文献(内容为示例，请根据实际文献查证)：
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1. **文献名称**: *Recombinant human apotransferrin: Expression, purification, and structural characterization*
**作者**: Wally J, Buchanan SK
**摘要**: 研究通过大肠杆菌表达系统重组生产人源apoTf，优化纯化条件并利用光谱学方法分析其结构与铁结合能力，证实重组蛋白与天然apoTf功能一致。
2. **文献名称**: *Apo-transferrin-targeted nanoparticles for enhanced drug delivery to tumors*
**作者**: Yang T, et al.
**摘要**: 探索重组apoTf作为靶向配体修饰纳米颗粒，用于肿瘤药物递送，实验表明其通过转铁蛋白受体介导的内吞作用显著提高药物在癌细胞中的富集。
3. **文献名称**: *Apolactoferrin in cell culture: Role in serum-free media supplementation*
**作者**: Chen L, et al.
**摘要**: 评估重组apoTf在无血清哺乳动物细胞培养中的应用，证实其能有效促进细胞增殖并替代动物源性转铁蛋白，降低培养污染风险。
4. **文献名称**: *Crystal structure of recombinant apotransferrin reveals conformational flexibility*
**作者**: Mizutani K, et al.
**摘要**: 通过X射线晶体学解析重组apoTf的三维结构，揭示其铁结合域的动态构象变化，为理解其金属离子结合机制提供结构基础。
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注：以上为模拟文献，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
**Background of Apo-Transferrin (apoTf) Recombinant Protein**
Apo-transferrin (apoTf) is the iron-free form of transferrin, a glycoprotein critical for iron transport and homeostasis in vertebrates. Transferrin binds two ferric ions (Fe³⁺) with high affinity in a pH-dependent manner, facilitating iron uptake into cells via receptor-mediated endocytosis. The "apo" state refers to its iron-unbound conformation, which plays a regulatory role in cellular iron metabolism by modulating receptor binding and release.
Structurally, apoTf is a monomeric protein (~80 kDa) composed of two homologous lobes (N-lobe and C-lobe), each capable of binding one Fe³⁺ ion. Its iron-binding capacity requires a synergistic anion, typically bicarbonate. Recombinant apoTf is produced using biotechnological platforms, such as bacterial, yeast, or mammalian expression systems, followed by purification to remove endogenous iron and contaminants. Mammalian systems (e.g., CHO cells) are often preferred to ensure proper post-translational modifications, including glycosylation, which affects stability and function.
Recombinant apoTf has broad applications in biomedical research and therapeutics. In cell culture, it serves as an iron carrier in serum-free media, avoiding iron toxicity while supporting cellular growth. It is also studied for its role in drug delivery, as transferrin receptors are overexpressed in certain cancer cells, enabling targeted therapies. Additionally, apoTf is used to investigate iron-related disorders (e.g., anemia, hemochromatosis) and neurodegenerative diseases linked to metal ion dysregulation.
The development of recombinant apoTf addresses challenges associated with plasma-derived transferrin, such as batch variability and pathogen risks. Its consistent quality and scalability make it a vital tool in biotechnology, pharmaceuticals, and basic science, underscoring its importance in both industrial and academic settings.
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