| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HIV1 |
| Uniprot No | P03367 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 501-599aa |
| 氨基酸序列 | PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGI GGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF |
| 预测分子量 | 11 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篇关于HIV-1重组蛋白的经典参考文献及摘要概括：
1. **文献名称**：Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
**作者**：McLellan JS, Pancera M, Carrico C, et al.
**摘要内容**：该研究通过X射线晶体学解析了HIV-1包膜蛋白gp120的V1/V2结构域与广谱中和抗体PG9的复合物结构，揭示了PG9通过靶向gp120四聚体界面保守的糖基化表位实现中和作用的机制，为疫苗设计提供结构学依据。
2. **文献名称**：Crystal structure of a soluble cleaved HIV-1 envelope trimer
**作者**：Julien JP, Cupo A, Sok D, et al.
**摘要内容**：作者成功表达并纯化了一种稳定的HIV-1重组包膜蛋白三聚体(BG505 SOSIP.664)，并通过冷冻电镜和晶体学解析其近天然构象，证明该重组蛋白能模拟病毒表面刺突结构，成为疫苗开发的重要抗原候选。
3. **文献名称**：Recombinant HIV-1 envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex
**作者**：Sanders RW, Derking R, Cupo A, et al.
**摘要内容**：研究利用重组HIV-1三聚体蛋白进行免疫原性测试，发现其能优先诱导靶向三聚体顶端(如V2/V3区)的广谱中和抗体，表明重组三聚体蛋白在模拟天然构象及激发有效免疫应答方面具有优势。
(注：以上为简化摘要，实际文献需通过PubMed或期刊官网获取完整内容。)
Human immunodeficiency virus type 1 (HIV-1) recombinant proteins are engineered versions of viral components produced through genetic modification in heterologous expression systems, such as bacteria, yeast, or mammalian cells. These proteins play a pivotal role in HIV research, diagnostics, and therapeutic development. Key targets include structural proteins like Env (envelope glycoproteins gp120 and gp41), Gag (capsid protein p24), and Pol (enzymes like reverse transcriptase, integrase, and protease), which are critical for viral entry, replication, and assembly.
Recombinant HIV-1 proteins are designed to mimic native viral antigens while eliminating infectious risks. For example, soluble gp140 trimers (engineered Env proteins) are widely used in vaccine studies to induce neutralizing antibodies. Similarly, recombinant p24 is employed in diagnostic assays to detect HIV-specific immune responses. Advances in structural biology and glycoengineering have improved the fidelity of these proteins, enabling better antigenic presentation and functional studies.
The development of recombinant proteins addresses challenges posed by HIV-1’s genetic diversity and immune evasion mechanisms. Subtype-specific or consensus sequences are often used to broaden immune coverage. Additionally, recombinant enzymes like reverse transcriptase and integrase serve as targets for antiretroviral drug screening. Recent efforts also explore mosaic proteins combining epitopes from multiple strains to enhance vaccine efficacy.
Despite progress, obstacles remain, including conformational instability of Env proteins and glycosylation pattern discrepancies. Ongoing research focuses on stabilizing native-like trimeric structures (e.g., SOSIP variants) and optimizing expression systems for scalability. Recombinant proteins also underpin novel therapeutic strategies, such as broadly neutralizing antibody (bNAb) discovery and mRNA-based vaccine platforms. Their versatility continues to drive innovations in understanding HIV-1 pathogenesis and advancing prevention/treatment tools.
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