| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IRF3 |
| Uniprot No | Q14653 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-427aa |
| 氨基酸序列 | MASMTGGQQMGRGHHHHHHENLYFQGEFGTPKPRILPWLVSQLDLGQLEG VAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDL PTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTS PDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRS PSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCP EGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLA LWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLG PFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLR ALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQG PGES |
| 预测分子量 | 50 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IRF3重组蛋白的3篇参考文献及其摘要概括：
1. **"Structural basis for the recognition of IRF3 by the RIG-I innate immune sensor"**
- **作者**: Kowalinski, E. et al.
- **摘要**: 通过X射线晶体学解析了RIG-I与IRF3重组蛋白的复合物结构，揭示了RIG-I识别IRF3的关键结构域，阐明了IRF3在抗病毒先天免疫信号中的激活机制。
2. **"IRF3 mediates a TLR3/TLR4-specific viral gene program"**
- **作者**: Doyle, S. et al.
- **摘要**: 利用重组IRF3蛋白在体外验证了TLR3/4信号通路对IRF3的依赖性，证明IRF3磷酸化后形成二聚体并入核启动干扰素基因表达，揭示了其在病原体识别中的核心作用。
3. **"Phosphorylation-mediated IRF3 conformational changes control its interaction with coactivator CBP"**
- **作者**: Lin, R. et al.
- **摘要**: 通过重组IRF3蛋白的磷酸化实验，证明TBK1激酶介导的磷酸化诱导IRF3构象变化，促进其与转录共激活因子CBP结合，从而驱动干扰素β的转录激活。
4. **"Crystal structure of IRF3 in complex with CBP"**
- **作者**: Takahasi, K. et al.
- **摘要**: 解析了重组IRF3蛋白与CBP的复合物晶体结构，揭示了IRF3激活结构域的关键氨基酸残基如何介导与CBP的相互作用，为靶向IRF3的抗病毒药物设计提供了结构基础。
这些文献涵盖了IRF3重组蛋白在结构解析、信号通路机制及分子相互作用中的关键研究。
Interferon Regulatory Factor 3 (IRF3) is a critical transcription factor in innate immune responses, primarily activated by pattern recognition receptors (PRRs) such as Toll-like receptors (TLRs) and RIG-I-like receptors (RLRs) upon viral or microbial infection. It plays a central role in inducing type I interferons (IFNs) and proinflammatory cytokines, bridging pathogen detection to antiviral defense. Structurally, IRF3 contains a DNA-binding domain, a regulatory C-terminal domain with phosphorylation sites, and a nuclear localization signal (NLS). Inactive IRF3 resides in the cytoplasm; upon phosphorylation (e.g., by TBK1/IKKε), it undergoes conformational changes, homodimerizes, and translocates to the nucleus to activate target genes.
Recombinant IRF3 proteins are engineered using expression systems (e.g., E. coli, mammalian cells) for functional and structural studies. These proteins often include tags (e.g., His, GST) for purification and detection. Researchers use recombinant IRF3 to dissect its activation mechanisms, interactions with kinases (e.g., TBK1), or DNA-binding specificity. Mutant variants (e.g., phosphorylation-deficient or constitutively active forms) help elucidate signaling dynamics. Applications extend to drug discovery, such as screening small molecules that modulate IRF3 activity for antiviral or anti-inflammatory therapies. Additionally, recombinant IRF3 aids in studying viral immune evasion strategies, as many pathogens target IRF3 to suppress IFN production. Its study remains vital for understanding immune regulation and developing therapies against infections, autoimmune diseases, and cancer.
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