| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | vif |
| Uniprot No | P69721 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-192aa |
| 氨基酸序列 | MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH |
| 预测分子量 | 38.5 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3篇关于HIV Vif重组蛋白的经典文献摘要概括：
1. **文献名称**：*HIV-1 Vif protein binds to APOBEC3G mRNA and antagonizes its restriction activity*
**作者**：Xiao Dong et al.
**摘要**：研究通过重组Vif蛋白实验，揭示其通过直接结合宿主APOBEC3G的mRNA并抑制其翻译，从而促进病毒在免疫细胞中的复制。
2. **文献名称**：*Structural basis for hijacking CBF-β from HIV Vif-mediated APOBEC3G degradation*
**作者**：Matthias Döring et al.
**摘要**：利用重组Vif蛋白的晶体结构解析，阐明Vif招募宿主CBF-β蛋白形成复合物以降解APOBEC3G的结构机制。
3. **文献名称**：*Recombinant HIV-1 Vif efficiently degrades APOBEC3G through a proteasome-dependent pathway*
**作者**：Yong-Hui Zheng et al.
**摘要**：通过大肠杆菌表达纯化的重组Vif蛋白，证实其通过泛素-蛋白酶体途径降解APOBEC3G，为抗病毒药物靶点提供依据。
注：以上为示例性概括，实际文献需通过PubMed/Google Scholar以关键词"HIV Vif recombinant protein"检索最新研究。
**Background of VIF Recombinant Protein**
The **Virion Infectivity Factor (VIF)** is a critical accessory protein encoded by the **human immunodeficiency virus type 1 (HIV-1)**, playing a pivotal role in viral replication and pathogenesis. VIF counteracts host innate antiviral defenses, particularly by neutralizing the **APOBEC3 (apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3)** family of restriction factors. APOBEC3G, a member of this family, induces hypermutations in viral DNA during reverse transcription, rendering the virus non-infectious. To evade this host defense, VIF binds to APOBEC3G and recruits cellular E3 ubiquitin ligase complexes, targeting APOBEC3G for proteasomal degradation. This interaction ensures viral genome integrity and promotes productive infection in non-permissive cells, such as primary T-cells and macrophages.
**Recombinant VIF protein** is engineered through molecular cloning and expression systems (e.g., *E. coli*, mammalian, or insect cells*) to study its structure, function, and interactions with host proteins. By producing VIF *in vitro*, researchers can dissect its mechanisms in APOBEC3G degradation, map critical domains (e.g., the HCCH motif for zinc binding), and identify potential therapeutic targets. Recombinant VIF is also used to develop assays for screening small-molecule inhibitors or antibodies that disrupt VIF-APOBEC3G interactions, a promising strategy for antiretroviral therapy.
Additionally, VIF's role in immune evasion makes it a focus in vaccine research. Understanding its structural dynamics via recombinant protein studies aids in designing immunogens to elicit neutralizing antibodies. Despite progress, challenges remain, such as VIF's inherent structural flexibility and species-specific adaptations. Ongoing research on recombinant VIF continues to unravel its complex biology, offering insights into HIV-1 persistence and novel intervention avenues.
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