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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IFNa9 |
| Uniprot No | P09235 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-190aa |
| 氨基酸序列 | CDLPQTH NLRNKKILTL LAQMRRLSPL SCLKDRKDFG FPQEKVDAQQ IQEAQAIPVL SELTQQILTL FTSKDSSAAW NATLLDSFCT GLHQLLNDLQ GCLMQLVGMK ELPLTQEDSQ LAMKKYFHRI TVYLREKKHS PCAWEVVRAE VWRALSSSVN LLARLSEEKE |
| 预测分子量 | 21,6 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IFNa9重组蛋白的模拟参考文献示例(注：文献信息为虚构，仅供示例参考)：
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1. **标题**: "Expression and purification of recombinant human IFNα9 in Escherichia coli"
**作者**: Zhang L, et al.
**摘要**: 研究通过大肠杆菌系统高效表达IFNα9重组蛋白，优化了包涵体复性条件，并验证其具有抗病毒活性(如抑制VSV复制)，为大规模生产提供技术基础。
2. **标题**: "IFNα9 exhibits distinct immunomodulatory effects compared to IFNα2 in chronic hepatitis B models"
**作者**: Kim S, et al.
**摘要**: 对比IFNα9与IFNα2在慢性乙肝小鼠模型中的疗效，发现IFNα9通过激活JAK-STAT通路更强效抑制HBV DNA复制，且副作用更低，提示其潜在临床应用优势。
3. **标题**: "Structural basis of IFNα9 receptor binding specificity revealed by mutagenesis"
**作者**: Müller R, et al.
**摘要**: 通过点突变和分子对接分析IFNα9与IFNAR受体的相互作用，鉴定出关键氨基酸残基，阐明其与IFNα亚型差异结合的分子机制。
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**说明**：以上文献为模拟内容，实际研究需通过PubMed、Web of Science等平台检索关键词“IFNα9 recombinant protein”或“Interferon alpha-9”获取真实数据。
Interferon alpha-9 (IFNα9) is a member of the type I interferon (IFN-I) family, a group of cytokines critical in mediating innate immune responses against viral infections and modulating adaptive immunity. Discovered in the 1980s, IFNα9 is encoded by the *IFNA9* gene in humans and shares structural homology with other IFNα subtypes, featuring a conserved core of five alpha-helices. Unlike ubiquitously expressed IFNα subtypes like IFNα2. IFNα9 exhibits distinct expression patterns, primarily in virus-infected leukocytes or dendritic cells, and demonstrates unique receptor-binding affinities that influence downstream signaling dynamics.
Recombinant IFNα9 protein is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems, enabling large-scale purification for research or therapeutic applications. Its biological activity hinges on binding to the IFNα/β receptor (IFNAR), activating JAK-STAT signaling pathways to induce antiviral, antiproliferative, and immunomodulatory genes. Studies highlight its potent antiviral effects against RNA viruses, including hepatitis C and influenza, though its efficacy varies compared to other IFNα subtypes due to differential receptor interaction kinetics.
Clinically, recombinant IFNα9 has been explored as a therapeutic agent for viral diseases and cancers, leveraging its ability to enhance immune cell activation and inhibit tumor growth. However, challenges persist, such as optimizing its pharmacokinetics, minimizing systemic toxicity, and understanding subtype-specific signaling outcomes. Current research focuses on engineering IFNα9 variants with improved stability or targeted delivery, aiming to harness its unique properties while mitigating limitations associated with conventional IFN therapies.
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