| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TFR |
| Uniprot No | P02786 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 89-760aa |
| 氨基酸序列 | CKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF |
| 预测分子量 | 76.5 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. |
以下是关于TFR(转铁蛋白受体)重组蛋白研究的示例参考文献(注：部分文献信息为示例性概括，实际引用时请核实具体来源)：
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1. **标题**：*Structural insights into the human transferrin receptor-mediated cellular iron uptake*
**作者**：Cheng, Y., Zak, O., Aisen, P.
**年份**：2004
**摘要**：通过X射线晶体学解析人源转铁蛋白受体(TFR1)与其配体转铁蛋白的复合物结构，揭示了TFR介导铁离子内吞的分子机制，为靶向TFR的药物设计提供结构基础。
2. **标题**：*Recombinant TFR-conjugated nanoparticles for targeted drug delivery across the blood-brain barrier*
**作者**：Zhang, L., et al.
**年份**：2015
**摘要**：开发了一种重组TFR修饰的纳米颗粒，利用TFR的跨血脑屏障转运能力，显著提高了药物在脑组织中的靶向递送效率，为神经疾病治疗提供新策略。
3. **标题**：*Optimizing recombinant TFR production in mammalian expression systems for therapeutic applications*
**作者**：Smith, J.R., Gupta, S., Lee, K.
**年份**：2020
**摘要**：系统比较了HEK293和CHO细胞中重组TFR的表达条件，优化了糖基化修饰和纯化工艺，获得高活性TFR蛋白，适用于抗体偶联药物开发。
4. **标题**：*Functional characterization of a soluble recombinant TFR variant in iron metabolism disorders*
**作者**：Wang, H., et al.
**年份**：2018
**摘要**：构建了一种可溶性重组TFR蛋白(sTFR)，证实其可通过竞争性结合转铁蛋白调节细胞铁摄取，为遗传性铁过载疾病的体外治疗研究提供工具。
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**注意**：以上文献信息为基于领域内典型研究方向生成的示例，实际文献可能需要通过PubMed、Web of Science等数据库检索确认。若需真实文献，可补充具体研究方向(如结构、疾病应用等)进一步筛选。
**Background of Recombinant Transferrin Receptor (TfR) Protein**
The transferrin receptor (TfR), primarily known as TfR1 (CD71), is a transmembrane glycoprotein critical for cellular iron uptake. It binds to iron-loaded transferrin, facilitating its internalization via clathrin-mediated endocytosis. This process ensures regulated iron delivery, essential for numerous physiological functions, including oxygen transport, DNA synthesis, and cellular metabolism. Dysregulation of TfR expression is linked to iron-related disorders (e.g., anemia, hemochromatosis) and cancers, where proliferating cells overexpress TfR to meet elevated iron demands.
Recombinant TfR proteins are engineered using biotechnological platforms, such as bacterial, yeast, or mammalian expression systems. These systems enable large-scale production of purified, functional TfR variants for research and therapeutic applications. Recombinant TfR retains the ability to bind transferrin and interact with antibodies or ligands, making it valuable for studying iron metabolism, receptor trafficking, and drug delivery mechanisms.
In therapeutics, TfR-targeted strategies exploit its overexpression in cancer cells. Recombinant TfR proteins serve as tools to design antibody-drug conjugates (ADCs) or nanoparticle-based systems for targeted drug delivery. Additionally, TfR is explored in diagnostic assays to detect iron deficiency or monitor cancer progression.
Recent advances include structural studies of TfR-ligand interactions using recombinant proteins, aiding in the rational design of inhibitors or mimetics. Challenges remain in optimizing expression yields, ensuring proper post-translational modifications, and minimizing immunogenicity in clinical applications. Nonetheless, recombinant TfR continues to bridge basic research and translational innovation, offering insights into iron biology and novel therapeutic avenues.
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