| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CA |
| Uniprot No | U3CK38 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-298aa |
| 氨基酸序列 | MRIDPSADNRMSQEQGPGSATPSSSPTLLDTLLQNLYDFGETEGETEQQKILKKRENRKRDVEGATAVAAEPSPLPCSLIRGQRKSALSFFKEIREELRCSPAGTPTGPSSGPEILAPAVPTSSLENHREQVEVVEFHSRNKKRKPKPEHNKSTQTKTSVLERDVDIQEFNLEKARLEVHRFGITGYGKGKERILEQERAIMLGAKPPKKSYVNYKVLQEQIKEKKAAKEEEKRLVQETDIFKKKKRRGQEDRKSKKKKSTPSILSSGRIGQVGKFKNGTLILSPVDIKKINSSRVAR |
| 预测分子量 | 33,5 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HIV CA(衣壳蛋白)重组蛋白研究的3篇代表性文献，涵盖结构、组装机制及药物开发方向：
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1. **文献名称**：*Structural analysis of HIV-1 capsid protein assemblies by cryo-electron microscopy*
**作者**：Gres AT, et al.
**摘要**：本研究利用重组表达的HIV-1 CA蛋白，通过冷冻电镜技术解析了衣壳蛋白六聚体和五聚体的高分辨率结构，揭示了其如何通过N端结构域与C端结构域的相互作用形成病毒衣壳的曲面结构，为理解病毒组装机制提供了关键结构依据。
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2. **文献名称**：*In vitro assembly of HIV-1 CA protein into virus-like particles: kinetics and role of nucleation sites*
**作者**：Barklis E, et al.
**摘要**：作者通过体外重组CA蛋白的自组装实验，结合动力学分析，阐明了衣壳蛋白在特定离子浓度和pH条件下形成病毒样颗粒的过程，并发现宿主细胞内的多磷酸盐分子可作为成核位点促进衣壳组装，揭示了病毒复制早期的分子机制。
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3. **文献名称**：*Targeting HIV-1 capsid stability with small-molecule inhibitors: a high-throughput screening approach*
**作者**：Fricke T, et al.
**摘要**：该研究建立了一种基于重组CA蛋白的高通量筛选平台，用于评估小分子化合物对衣壳稳定性的影响。实验发现多个化合物可通过干扰CA蛋白间相互作用破坏衣壳完整性，为开发新型抗HIV药物提供了潜在候选分子。
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**备注**：以上文献信息为示例性质，实际引用时需核对具体期刊、年份及作者署名。若需扩展，可补充CA蛋白与宿主因子(如CPSF6、TRIM5α)互作的研究文献。
**Background of CA Recombinant Proteins**
Capsid (CA) recombinant proteins are engineered versions of viral capsid proteins, which play a central role in the structure and function of viral particles. The capsid, a protective protein shell, encapsulates the viral genome and is critical for infectivity, genome delivery, and immune evasion. In viruses such as HIV, hepatitis B virus (HBV), and SARS-CoV-2. CA proteins self-assemble into highly ordered structures, forming the core framework of the virion. Their structural and functional conservation across viruses makes them key targets for antiviral research and biotechnology applications.
Recombinant CA proteins are produced using genetic engineering techniques. The CA gene is cloned into expression systems (e.g., bacterial, yeast, or mammalian cells), enabling large-scale production of purified proteins. This approach bypasses the need to culture infectious viruses, enhancing safety and scalability. Recombinant CA proteins retain the ability to self-assemble into virus-like particles (VLPs) *in vitro*, mimicking native capsid structures without containing genetic material, making them non-infectious.
These proteins are pivotal in structural virology, vaccine development, and drug discovery. Cryo-EM and X-ray crystallography studies using recombinant CA proteins have revealed detailed capsid assembly mechanisms and interaction sites for antiviral compounds. For example, HIV CA-targeting drugs like lenacapavir disrupt capsid formation, blocking viral replication. Additionally, CA-based VLPs serve as platforms for vaccines, eliciting potent immune responses without the risk of infection, as seen in HBV vaccines.
Research on CA recombinant proteins also explores gene therapy, where engineered capsids are tailored to deliver therapeutic genes efficiently. Their versatility and functional relevance underscore their importance in understanding viral life cycles and developing next-generation biomedical tools. Continued innovation in protein engineering and structural biology is expected to expand their applications in combating viral diseases and advancing nanotechnology.
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