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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL28B |
| Uniprot No | Q8IZI9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-196aa |
| 氨基酸序列 | MTGDCMPVLV LMAAVLTVTG AVPVARLRGA LPDARGCHIA QFKSLSPQEL QAFKRAKDAL EESLLLKDCK CRSRLFPRTW DLRQLQVRER PVALEAELAL TLKVLEATAD TDPALGDVLD QPLHTLHHIL SQLRACIQPQ PTAGPRTRGR LHHWLHRLQE APKKESPGCL EASVTFNLFR LLTRDLNCVA SGDLCV |
| 预测分子量 | 21 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IL28B重组蛋白的3篇参考文献示例(内容基于假设文献整理)：
1. **文献名称**：*"Recombinant IL28B induces potent antiviral responses in vitro and enhances HCV clearance"*
**作者**：Ge D, Fellay J, Thompson AJ, et al.
**摘要**：研究报道了IL28B重组蛋白在大肠杆菌中的高效表达与纯化，并证实其在体外模型中显著抑制丙型肝炎病毒(HCV)复制，揭示了IL28B多态性与干扰素治疗应答的关联性。
2. **文献名称**：*"IL28B recombinant protein modulates JAK-STAT signaling and suppresses HBV replication in hepatocytes"*
**作者**：Thomas DL, Thio CL, Martin MP, et al.
**摘要**：通过哺乳动物细胞系统表达IL28B重组蛋白，发现其通过激活JAK-STAT通路诱导干扰素刺激基因(ISGs)，并在肝细胞模型中抑制乙型肝炎病毒(HBV)的复制。
3. **文献名称**：*"Structural and functional characterization of recombinant human IL28B: Implications for therapeutic design"*
**作者**：Zhang L, Jilg N, Shao RX, et al.
**摘要**：利用X射线晶体学解析IL28B重组蛋白的三维结构，结合功能实验验证其与受体IL28Rα的结合模式，为基于IL28B的靶向药物开发提供结构基础。
4. **文献名称**：*"IL28B recombinant protein as a novel adjuvant for hepatitis B vaccination"*
**作者**：Gad HH, Paul F, Hamming OJ, et al.
**摘要**：评估IL28B重组蛋白作为疫苗佐剂的潜力，实验表明其可增强小鼠模型中乙肝表面抗原(HBsAg)的免疫原性，提示其在疫苗开发中的应用前景。
注：以上文献标题和作者为示例性虚构内容，实际研究中需根据具体文献数据库(如PubMed)检索真实论文。
IL28B recombinant protein, also known as interferon lambda 3 (IFN-λ3), is a cytokine belonging to the type III interferon family. Discovered in 2003. type III interferons (IFN-λ1. λ2. λ3. and λ4) share structural and functional similarities with type I interferons but signal through a distinct receptor complex composed of IL-28Rα and IL-10Rβ. The IL28B gene, located on human chromosome 19. encodes the IL28B protein, which plays a critical role in innate immune responses, particularly against viral infections. It activates the JAK-STAT signaling pathway, leading to the induction of interferon-stimulated genes (ISGs) that inhibit viral replication and modulate immune cell activity.
Recombinant IL28B is produced using genetic engineering techniques, often expressed in bacterial (e.g., E. coli) or mammalian cell systems to ensure proper folding and post-translational modifications. Its therapeutic potential has been extensively studied in viral hepatitis, especially hepatitis C virus (HCV) infection. Landmark studies revealed that IL28B polymorphisms (e.g., rs12979860) strongly correlate with spontaneous HCV clearance and treatment response, highlighting its role in personalized medicine. Unlike type I interferons, IFN-λ3 exhibits tissue-specific receptor expression, primarily targeting epithelial cells and hepatocytes, which may reduce systemic side effects.
Beyond virology, IL28B recombinant protein is explored in oncology for its antitumor and immunomodulatory effects, particularly in cancers with viral etiology or interferon-sensitive pathways. Preclinical studies suggest its efficacy in enhancing antigen presentation and suppressing tumor growth. Additionally, it is investigated in chronic inflammatory diseases, such as multiple sclerosis, due to its ability to regulate Th1/Th17 responses. Despite promising applications, challenges remain in optimizing delivery systems and minimizing off-target effects. Overall, IL28B recombinant protein represents a versatile tool for both research and therapeutic development, bridging immunology, virology, and precision medicine.
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