| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gag |
| Uniprot No | Q9UL42 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-361aa |
| 氨基酸序列 | ALALLEDWCRIMSVDEQKSLMVTGIPADFEEAEIQEVLQETLKSLGRYRLLGKIFRKQENANAVLLELLEDTDVSAIPSEVQGKGGVWKVIFKTPNQDTEFLERLNLFLEKEGQTVSGMFRALGQEGVSPATVPCISPELLAHLLGQAMAHAPQPLLPMRYRKLRVFSGSAVPAPEEESFEVWLEQATEIVKEWPVTEAEKKRWLAESLRGPALDLMHIVQADNPSISVEECLEAFKQVFGSLESRRTAQVRYLKTYQEEGEKVSAYVLRLETLLRRAVEKRAIPRRIADQVRLEQVMAGATLNQMLWCRLRELKDQGPPPSFLELMKVIREEEEEEASFENESIEEPEERDGYGRWNHE |
| 预测分子量 | 57.1 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Gag重组蛋白的代表性文献(示例格式，非真实文献，仅供概念参考)：
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1. **文献名称**: "Assembly and structural analysis of HIV-1 Gag recombinant protein in vitro"
**作者**: Smith A, et al.
**摘要**: 研究利用大肠杆菌表达系统重组表达HIV-1 Gag蛋白，通过电子显微镜和X射线晶体学解析其自组装成病毒样颗粒(VLP)的分子机制，揭示了Gag多聚化关键结构域的作用。
2. **文献名称**: "Recombinant Gag-based virus-like particles as a vaccine platform against retroviruses"
**作者**: Zhang L, et al.
**摘要**: 开发基于重组Gag蛋白的病毒样颗粒(VLP)疫苗，通过动物实验证明其可诱导强烈的细胞免疫和中和抗体反应，为HIV和HTLV等逆转录病毒疫苗设计提供新策略。
3. **文献名称**: "Functional characterization of a truncated Gag recombinant protein for lentiviral vector production"
**作者**: Kim J, et al.
**摘要**: 通过截短Gag蛋白重组构建简化版慢病毒载体包装系统，证实其能够有效组装病毒颗粒并提高基因递送效率，同时降低细胞毒性。
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注：以上为示例内容，实际引用请根据具体研究方向查询真实文献(可参考期刊如*Journal of Virology*、*Retrovirology*或*Biotechnology and Bioengineering*中的相关研究)。
The Gag (Group-specific antigen) recombinant protein is a key structural component of retroviruses, including human immunodeficiency virus (HIV) and other lentiviruses. In native viral infection, the Gag polyprotein orchestrates viral particle assembly, budding, and maturation. It is synthesized as a precursor protein that undergoes proteolytic cleavage by viral proteases during maturation, yielding matrix (MA), capsid (CA), nucleocapsid (NC), and other smaller functional domains. These domains mediate membrane targeting, virion assembly, RNA binding, and interactions with host cell machinery.
Recombinant Gag proteins are engineered through genetic cloning, where the gag gene is inserted into expression vectors (e.g., bacterial, yeast, or mammalian systems) to produce purified proteins for research or therapeutic applications. These recombinant versions retain critical structural and functional features of native Gag, enabling studies on viral replication mechanisms, host-pathogen interactions, and drug discovery. For instance, Gag-based virus-like particles (VLPs) generated from recombinant proteins mimic authentic virions but lack genetic material, making them non-infectious tools for vaccine development or gene delivery systems.
In HIV research, recombinant Gag proteins are pivotal for investigating assembly intermediates, capsid disassembly dynamics, and immune responses. They serve as antigens in diagnostic assays to detect anti-Gag antibodies and in T-cell immunogenicity studies for vaccine design. Additionally, Gag-targeting antiretrovirals, such as maturation inhibitors, rely on recombinant proteins for mechanistic and resistance profiling.
Beyond virology, Gag recombinant proteins contribute to nanotechnology and synthetic biology due to their self-assembly properties. Their versatility underscores their importance in advancing virology, immunology, and biomedical engineering.
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