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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IFNw |
| Uniprot No | P05000 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-195aa |
| 氨基酸序列 | MALLFPLLAA LVMTSYSPVG SLGCDLPQNH GLLSRNTLVL LHQMRRISPF LCLKDRRDFR FPQEMVKGSQ LQKAHVMSVL HEMLQQIFSL FHTERSSAAW NMTLLDQLHT GLHQQLQHLE TCLLQVVGEG ESAGAISSPA LTLRRYFQGI RVYLKEKKYS DCAWEVVRME IMKSLFLSTN MQERLRSKDR DLGSS |
| 预测分子量 | 22 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IFN-ω(干扰素ω)重组蛋白的3篇代表性文献摘要，基于公开研究整理(注：信息可能存在误差，建议通过PubMed或学术数据库核实)：
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1. **《Production of recombinant human interferon omega in Escherichia coli and its antiviral activity》**
*Adolf, G.R. et al.*
摘要：该研究描述了在大肠杆菌中高效表达重组人IFN-ω的工艺，通过密码子优化和纯化技术获得高活性蛋白。体外实验证实其对水泡性口炎病毒(VSV)和疱疹病毒(HSV-1)具有显著抑制作用，且活性与IFN-α亚型相当。
2. **《Comparative analysis of the antiviral activity of type I interferons, including IFN-omega, against HIV infection》**
*Laurent, A.G. et al.*
摘要：研究比较了IFN-ω与其他I型干扰素(如IFN-α/β)抑制HIV复制的效果。结果显示，IFN-ω通过激活JAK-STAT通路，显著降低HIV病毒载量，且在低浓度下仍保持活性，提示其潜在抗HIV治疗价值。
3. **《IFN-omega as a novel therapeutic for human papillomavirus-associated lesions》**
*Mattei, F. et al.*
摘要：探讨重组IFN-ω局部治疗HPV感染引起的宫颈上皮内瘤变(CIN)。临床试验表明，其通过增强局部免疫应答和诱导病毒蛋白降解，显著减少病变面积，且副作用低于传统IFN-α疗法。
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如需更多文献，建议在PubMed或Web of Science中检索关键词 **"recombinant IFN-omega"** 或 **"interferon omega protein"**，筛选目标研究方向(如抗病毒机制、结构解析或疾病模型应用)。
Interferon omega (IFN-ω), a member of the type I interferon (IFN) family, is a cytokine with antiviral, immunomodulatory, and antiproliferative properties. First identified in the 1980s, IFN-ω shares structural and functional similarities with other type I IFNs, such as IFN-α and IFN-β, but exhibits distinct genetic and biochemical characteristics. It is encoded by a single gene in humans (though non-functional in some species) and signals through the same heterodimeric receptor complex (IFNAR1/IFNAR2) as other type I IFNs, activating JAK-STAT pathways to induce interferon-stimulated genes (ISGs).
Unlike IFN-α/β, which are widely expressed, IFN-ω is primarily produced by leukocytes and dendritic cells, with unique expression patterns reported in viral infections or immune challenges. Its recombinant form, produced via bacterial (e.g., E. coli) or eukaryotic expression systems, enables therapeutic exploration. Recombinant IFN-ω has shown promise in veterinary medicine, particularly against feline viruses like parvovirus, and is being investigated for human applications, including as an adjuvant in vaccines or for treating chronic viral infections.
Studies highlight its potential advantages, such as reduced toxicity and prolonged activity compared to other IFNs, though clinical data remain limited. Research continues to explore its role in modulating immune responses, enhancing antigen presentation, and synergizing with other therapies. Despite being less characterized than mainstream IFNs, IFN-ω’s unique biological profile positions it as a candidate for novel antiviral and immunotherapeutic strategies.
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