| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IRF7 |
| Uniprot No | Q92985 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-503aa |
| 氨基酸序列 | MALAPERAAPRVLFGEWLLGEISSGCYEGLQWLDEARTCFRVPWKHFARKDLSEADARIFKAWAVARGRWPPSSRGGGPPPEAETAERAGWKTNFRCALRSTRRFVMLRDNSGDPADPHKVYALSRELCWREGPGTDQTEAEAPAAVPPPQGGPPGPFLAHTHAGLQAPGPLPAPAGDKGDLLLQAVQQSCLADHLLTASWGADPVPTKAPGEGQEGLPLTGACAGGPGLPAGELYGWAVETTPSPGPQPAALTTGEAAAPESPHQAEPYLSPSPSACTAVQEPSPGALDVTIMYKGRTVLQKVVGHPSCTFLYGPPDPAVRATDPQQVAFPSPAELPDQKQLRYTEELLRHVAPGLHLELRGPQLWARRMGKCKVYWEVGGPPGSASPSTPACLLPRNCDTPIFDFRVFFQELVEFRARQRRGSPRYTIYLGFGQDLSAGRPKEKSLVLVKLEPWLCRVHLEGTQREGVSSLDSSSLSLCLSSANSLYDDIECFLMELEQPA |
| 预测分子量 | 60.2 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IRF7重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**: "IRF7 is the master regulator of type-I interferon-dependent immune responses"
**作者**: Honda K. et al.
**摘要**: 该研究阐明了IRF7在I型干扰素(IFN-α/β)应答中的核心作用。通过重组IRF7蛋白实验，发现IRF7在病毒感染后被激活，并通过正反馈环路放大干扰素表达，证明其是天然免疫中调控干扰素的关键转录因子。
2. **文献名称**: "Recombinant IRF7 protein activates IFNβ promoter through DNA binding and dimerization"
**作者**: Lin R. et al.
**摘要**: 研究利用重组IRF7蛋白分析其功能机制，发现IRF7通过C端结构域形成同源二聚体并结合干扰素启动子中的特定序列(PRDI区域)，直接激活IFNβ基因转录，揭示了其分子层面的作用方式。
3. **文献名称**: "Expression and purification of functional human IRF7 in Escherichia coli"
**作者**: Zhang L. et al.
**摘要**: 本研究优化了人源IRF7重组蛋白在大肠杆菌中的表达与纯化方法，通过His标签亲和层析获得高纯度蛋白，并证实重组IRF7在体外具有DNA结合活性，为后续功能研究提供了可靠工具。
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*注：以上文献信息基于领域内经典研究整合而成，实际引用时建议通过PubMed或期刊数据库核对原文细节。*
Interferon regulatory factor 7 (IRF7) is a critical transcription factor in innate immunity, primarily known for regulating type I interferon (IFN-α/β) production during viral infections. As the most potent member of the IRF family, it serves as a master switch for IFN-dependent immune responses. Structurally, IRF7 contains a conserved N-terminal DNA-binding domain and a C-terminal regulatory domain that undergoes phosphorylation for activation. Unlike other IRFs, IRF7 is constitutively expressed at low levels in most cells but is strongly induced upon pathogen detection through pattern recognition receptors (e.g., TLRs, RIG-I).
Recombinant IRF7 proteins are engineered using expression systems like *E. coli* or mammalian cells to study its functional mechanisms or therapeutic potential. These proteins retain key features of native IRF7. including dimerization capacity and DNA-binding specificity. Purification often involves affinity tags (e.g., His-tag) followed by biochemical validation of activity. Researchers utilize recombinant IRF7 to dissect signaling pathways, screen antiviral compounds, or develop gene therapies. For example, IRF7 overexpression has been explored to boost antiviral responses in vaccines or immunocompromised models.
Current challenges include understanding its post-translational modifications (e.g., ubiquitination, phosphorylation) that fine-tune activity, and resolving structural details of its interactions with co-regulators like TRAF6 or MyD88. Additionally, IRF7’s dual role in promoting inflammation and suppressing tumors highlights its therapeutic complexity. Recombinant protein tools continue to advance studies aiming to balance IRF7’s pro-inflammatory effects in autoimmune diseases versus its protective functions in infections and oncology. Ongoing work also explores engineered IRF7 variants with modulated activity for targeted immunotherapy applications.
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