| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CXCR4 |
| Uniprot No | P61073 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-46aa |
| 氨基酸序列 | MEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYS |
| 预测分子量 | 33 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CXCR4重组蛋白的3篇参考文献示例，涵盖结构、功能及药物开发方向：
1. **《Structure of the human chemokine receptor CXCR4 in complex with a small molecule antagonist》**
- **作者**: Wu, B., Chien, E.Y., Mol, C.D. 等
- **摘要**: 通过X射线晶体学解析了CXCR4与拮抗剂IT1t的复合物结构，揭示了受体跨膜结构域的关键结合位点，为靶向药物设计提供结构基础。
2. **《The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry》**
- **作者**: Bleul, C.C., Fuhlbrigge, R.C., Casasnovas, J.M. 等
- **摘要**: 发现CXCR4(原称fusin)是趋化因子SDF-1的受体，并证实其作为HIV-1病毒入侵的共受体，阻断CXCR4可抑制病毒与细胞膜融合。
3. **《CXCR4 inhibitors: targeting HIV-1 entry and metastasis in cancer》**
- **作者**: De Clercq, E.
- **摘要**: 综述了基于CXCR4重组蛋白筛选的小分子抑制剂(如AMD3100)在抗HIV和治疗癌症转移中的双重潜力，探讨其作用机制及临床前研究进展。
(注：以上文献信息为示例性质，具体内容请根据实际研究查阅原文。)
CXCR4. a CXC chemokine receptor belonging to the G protein-coupled receptor (GPCR) family, plays critical roles in immune regulation, stem cell migration, cancer metastasis, and HIV infection. It binds to its natural ligand, stromal cell-derived factor-1 (SDF-1/CXCL12), triggering intracellular signaling pathways that mediate cell chemotaxis, survival, and proliferation. Structurally, CXCR4 consists of seven transmembrane α-helical domains, an extracellular N-terminus, and an intracellular C-terminus, with three extracellular loops involved in ligand interactions. Dysregulation of CXCR4 is linked to pathological conditions, including inflammatory diseases, leukemia, and solid tumor progression, making it a key therapeutic target.
Recombinant CXCR4 protein is engineered through heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to study its biochemical properties, ligand interactions, and signaling mechanisms. This protein is often modified with tags (e.g., His-tag, FLAG) for simplified purification and detection. Its production enables structural analyses (e.g., crystallography, cryo-EM) to elucidate binding motifs for CXCL12 or antagonists like AMD3100. aiding drug development. Additionally, recombinant CXCR4 serves as a tool to investigate HIV entry mechanisms, as the receptor facilitates viral fusion by interacting with the viral envelope glycoprotein gp120.
Challenges in producing functional CXCR4 include preserving its native conformation and membrane-associated activity, given its complex transmembrane topology. Advanced expression systems and lipid-based stabilization techniques are employed to enhance solubility and stability. Researchers utilize this recombinant protein in high-throughput screens for inhibitors, antibody development, and mechanistic studies of metastasis or stem cell homing. By bridging structural biology and translational applications, recombinant CXCR4 remains pivotal in advancing therapies for cancer, immunodeficiency disorders, and regenerative medicine.
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