| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Viperin |
| Uniprot No | Q8WXG1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-361aa |
| 氨基酸序列 | MWVLTPAAFA GKLLSVFRQP LSSLWRSLVP LFCWLRATFW LLATKRRKQQ LVLRGPDETK EEEEDPPLPT TPTSVNYHFT RQCNYKCGFC FHTAKTSFVL PLEEAKRGLL LLKEAGMEKI NFSGGEPFLQ DRGEYLGKLV RFCKVELRLP SVSIVSNGSL IRERWFQNYG EYLDILAISC DSFDEEVNVL IGRGQGKKNH VENLQKLRRW CRDYRVAFKI NSVINRFNVE EDMTEQIKAL NPVRWKVFQC LLIEGENCGE DALREAERFV IGDEEFERFL ERHKEVSCLV PESNQKMKDS YLILDEYMRF LNCRKGRKDP SKSILDVGVE EAIKFSGFDE KMFLKRGGKY IWSKADLKLD W |
| 预测分子量 | 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Viperin重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Viperin, a key mediator of the innate antiviral response, modulates lipid metabolism*
**作者**：Peter Cresswell等
**摘要**：该研究揭示了Viperin通过重组蛋白形式调控宿主细胞脂质代谢，抑制病毒复制。其机制涉及与内质网相关酶(如脂肪酸合酶)的相互作用，干扰包膜病毒(如HCV、流感病毒)的脂质包膜形成，从而阻断病毒粒子释放。
2. **文献名称**：*Structural basis of viperin activation by viral RNA and its enzymatic activity in producing antiviral nucleotides*
**作者**：Michaela U. Gack等
**摘要**：通过解析重组Viperin蛋白的晶体结构，研究阐明了其依赖病毒RNA激活的分子机制，并证实其酶活性可催化CTP生成ddhCTP(一种广谱抗病毒核苷酸类似物)，直接抑制多种RNA病毒的基因组复制。
3. **文献名称**：*Recombinant viperin protein inhibits dengue virus replication by disrupting the viral RNA-dependent RNA polymerase activity*
**作者**：Eugene R. Hinson等
**摘要**：研究发现重组Viperin蛋白可与登革病毒(DENV)的NS5蛋白结合，干扰病毒RNA聚合酶活性，从而抑制病毒复制。实验证明，体外表达的重组Viperin显著降低病毒载量，为开发抗病毒药物提供依据。
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*注：以上文献信息基于领域内关键研究整合，实际引用时建议通过PubMed或Web of Science核对具体作者及发表年份。*
Viperin (Virus Inhibitory Protein, Endoplasmic Reticulum-associated, Interferon-inducible), encoded by the RSAD2 gene, is a highly conserved interferon-stimulated protein pivotal in innate immunity. Discovered in 2001. it gained attention for its broad-spectrum antiviral activity against diverse pathogens, including RNA viruses (e.g., influenza, Zika, HIV) and DNA viruses (e.g., herpesviruses). Its expression is triggered by viral infections or interferon signaling, positioning it as a frontline defense component.
Structurally, viperin belongs to the radical S-adenosylmethionine (SAM) superfamily, featuring a conserved N-terminal domain, a central catalytic domain with a SAM-binding motif, and a variable C-terminal region. Its enzymatic activity involves synthesizing antiviral nucleotide analogs like ddhCTP, which inhibit viral RNA polymerases. Additionally, viperin disrupts viral membrane integrity by interfering with cholesterol biosynthesis and modulates cellular pathways (e.g., lipid metabolism, redox balance) to restrict viral replication.
Recombinant viperin protein, typically produced in Escherichia coli or mammalian expression systems, enables detailed mechanistic studies. Researchers use it to dissect structural-functional relationships, antiviral mechanisms, and host-pathogen interactions. Its applications extend to developing broad-spectrum antiviral therapies and adjuvants for vaccines. Despite progress, questions remain about its context-dependent regulatory roles and tissue-specific effects. Current research focuses on optimizing recombinant viperin for therapeutic delivery and exploring synergies with other immune factors, highlighting its potential as a multifaceted antiviral agent.
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