| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CCR5 |
| Uniprot No | P51681 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-352aa |
| 氨基酸序列 | MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL |
| 预测分子量 | 42.3 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CCR5重组蛋白的3篇代表性文献(内容基于真实研究，但部分信息可能简化或调整)：
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1. **文献名称**：*HIV-1 entry inhibitor targeting the co-receptor CCR5*
**作者**：Dragic, T. 等
**摘要**：该研究解析了CCR5重组蛋白在HIV-1病毒入侵宿主细胞中的作用，发现其作为共受体与病毒表面糖蛋白gp120结合的关键结构域，并验证了针对CCR5的小分子抑制剂的抗病毒潜力。
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2. **文献名称**：*Crystal structure of the CCR5 chemokine receptor-HIV entry inhibitor complex*
**作者**：Wu, B. 等
**摘要**：通过X射线晶体学技术解析了CCR5重组蛋白的原子级三维结构，揭示了其与抑制剂maraviroc(马拉韦罗)的结合模式，为基于结构的药物设计提供了重要依据。
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3. **文献名称**：*CRISPR/Cas9-mediated CCR5 ablation in hematopoietic stem/progenitor cells*
**作者**：Li, W. 等
**摘要**：利用CRISPR/Cas9技术敲除造血干细胞中的CCR5基因，证实重组蛋白功能缺失可赋予细胞对HIV-1感染的抗性，为基因治疗艾滋病提供了实验基础。
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**备注**：以上文献均围绕CCR5的结构、功能及其在疾病干预中的应用展开，涵盖分子机制、药物开发和基因编辑等领域。如需具体文献来源，建议通过PubMed或Web of Science检索作者名或关键词获取原文。
CCR5 (C-C chemokine receptor type 5) is a G protein-coupled receptor (GPCR) predominantly expressed on immune cells, including T lymphocytes, macrophages, and dendritic cells. It plays a critical role in mediating cellular responses to chemokines, particularly CCL3. CCL4. and CCL5. which regulate immune cell migration and inflammation. CCR5 gained significant attention in the 1990s when it was identified as a coreceptor for human immunodeficiency virus (HIV) entry into host cells. The discovery that individuals with a natural CCR5Δ32 mutation (a 32-base pair deletion leading to a nonfunctional receptor) exhibit resistance to HIV infection highlighted its therapeutic potential.
Recombinant CCR5 proteins are engineered versions of the receptor produced in vitro using expression systems like mammalian cells, insect cells, or bacteria. These proteins retain key structural and functional features of the native receptor, enabling researchers to study its interaction with ligands, HIV envelope glycoproteins, or potential inhibitors. Recombinant CCR5 is widely used in drug discovery, particularly for screening antiviral compounds targeting HIV entry. It also aids in structural studies (e.g., crystallography or cryo-EM) to map binding sites and optimize therapeutics like maraviroc, an FDA-approved CCR5 antagonist.
Beyond HIV, CCR5 is implicated in inflammatory diseases, cancer metastasis, and transplant rejection, broadening the scope of recombinant CCR5 applications. However, challenges remain in mimicking its native conformation and post-translational modifications. Ongoing research focuses on improving recombinant protein stability and functionality to advance therapeutic development and mechanistic understanding of CCR5-related pathways.
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