| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | env |
| Uniprot No | P04578 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-511aa |
| 氨基酸序列 | KLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKR |
| 预测分子量 | 69.7 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. |
以下是三篇与env重组蛋白相关的代表性文献示例，供参考：
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1. **文献名称**：Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
**作者**：McLellan JS, Pancera M, et al.
**摘要**：本研究解析了HIV-1包膜蛋白gp120的V1/V2结构域与广谱中和抗体PG9的复合物晶体结构，揭示了重组env蛋白的关键抗原表位，为基于env结构的疫苗设计提供了分子基础。
2. **文献名称**：Native-like Env trimers as a platform for HIV-1 vaccine design
**作者**：Sanders RW, Moore JP
**摘要**：文章总结了通过重组技术构建HIV-1 env蛋白三聚体模拟天然构象的策略，证明优化后的重组三聚体可诱导更强的中和抗体反应，推动了基于env的疫苗开发。
3. **文献名称**：mRNA vaccines against H10N8 and H7N9 influenza viruses elicit strong immune responses in animal models
**作者**：Pardi N, Hogan MJ, et al.
**摘要**：虽然主要针对流感病毒，但本研究展示了mRNA技术表达重组病毒蛋白(如env类似的血凝素)的潜力，为后续应用于HIV等病毒的env蛋白疫苗提供了技术参考。
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**说明**：
1. 上述文献方向覆盖env重组蛋白的**结构解析**、**疫苗设计**和**技术平台**，均为相关领域的关键研究方向。
2. 若需具体文献，建议在PubMed或Google Scholar中检索关键词："recombinant env protein HIV vaccine"或"HIV envelope glycoprotein engineering"。
3. 近年研究可关注**冷冻电镜技术优化env三聚体结构**(如BG505 SOSIP)及**mRNA/LNP递送env蛋白**的疫苗试验。
The envelope (Env) glycoprotein is a critical structural component of enveloped viruses, including HIV-1. influenza, and coronaviruses. In HIV-1. for instance, Env is a trimeric surface protein composed of gp120 and gp41 subunits, facilitating viral entry by binding to host cell receptors (CD4 and co-receptors) and mediating membrane fusion. Its structural complexity, conformational flexibility, and heavy glycosylation pose challenges for immune recognition, making it a key target for vaccine design and therapeutic interventions.
Recombinant Env proteins are engineered through genetic cloning and expression systems (e.g., mammalian, insect, or yeast cells) to mimic native viral spikes. These proteins retain antigenic features essential for eliciting neutralizing antibodies while excluding infectious elements. Since the 1980s, recombinant Env technology has advanced significantly, enabling studies on viral entry mechanisms, antibody-antigen interactions, and immune evasion strategies. For vaccine development, stabilized Env trimers (e.g., SOSIP gp140) have been designed to adopt native-like pre-fusion conformations, improving immunogenicity compared to earlier monomeric gp120 formulations.
Env recombinants are also tools for diagnostic assays, pseudovirus production, and screening broadly neutralizing antibodies (bNAbs). In HIV research, they underpin efforts like the RV144 trial and recent mRNA-based vaccine platforms. However, challenges persist, including Env's genetic diversity, glycan shielding, and instability. Ongoing work focuses on optimizing immunogen design, incorporating T-cell epitopes, and leveraging structural insights to overcome these barriers. Recombinant Env proteins thus remain central to virology and translational immunology, bridging basic science and clinical applications.
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