| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL17RB |
| Uniprot No | Q9NRM6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-502aa |
| 氨基酸序列 | MSLVLLSLAALCRSAVPREPTVQCGSETGPSPEWMLQHDLIPGDLRDLRVEPVTTSVATGDYSILMNVSWVLRADASIRLLKATKICVTGKSNFQSYSCVRCNYTEAFQTQTRPSGGKWTFSYIGFPVELNTVYFIGAHNIPNANMNEDGPSMSVNFTSPGCLDHIMKYKKKCVKAGSLWDPNITACKKNEETVEVNFTTTPLGNRYMALIQHSTIIGFSQVFEPHQKKQTRASVVIPVTGDSEGATVQLTPYFPTCGSDCIRHKGTVVLCPQTGVPFPLDNNKSKPGGWLPLLLLSLLVATWVLVAGIYLMWRHERIKKTSFSTTTLLPPIKVLVVYPSEICFHHTICYFTEFLQNHCRSEVILEKWQKKKIAEMGPVQWLATQKKAADKVVFLLSNDVNSVCDGTCGKSEGSPSENSQDLFPLAFNLFCSDLRSQIHLHKYVVVYFREIDTKDDYNALSVCPKYHLMKDATAFCAELLHVKQQVSAGKRSQACHDGCCSL |
| 预测分子量 | 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IL17RB重组蛋白的参考文献示例(注：内容为模拟示例，非真实文献)：
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1. **文献名称**：*Expression and Functional Characterization of Recombinant Human IL17RB in Inflammatory Signaling*
**作者**：Zhang Y, Wang L, Chen X
**摘要**：该研究通过哺乳动物表达系统成功制备了重组人IL17RB蛋白，并验证其与配体IL-25的结合能力。实验表明，IL17RB在激活NF-κB通路中起关键作用，促进Th2型细胞因子的释放，提示其在过敏性疾病中的潜在机制。
2. **文献名称**：*Structural Insights into IL17RB Ligand Interaction via Recombinant Protein Crystallography*
**作者**：Lee S, Kim H, Tanaka K
**摘要**：通过昆虫细胞系统表达并纯化重组IL17RB胞外域，利用X射线晶体学解析其与IL-25复合物的三维结构。研究揭示了IL17RB的独特结合界面，为设计靶向该受体的抑制剂提供了结构基础。
3. **文献名称**：*Recombinant IL17RB Fusion Protein Attenuates Pancreatic Cancer Progression in Vivo*
**作者**：Smith J, Patel R, Garcia M
**摘要**：构建重组IL17RB-Fc融合蛋白，发现其可通过阻断IL-25信号通路抑制肿瘤微环境中的炎症反应，显著减缓胰腺癌小鼠模型的肿瘤生长，表明其作为新型治疗策略的潜力。
4. **文献名称**：*Development of Neutralizing Antibodies Against IL17RB Using Recombinant Protein Immunization*
**作者**：Chen T, Liu Z, Wang Q
**摘要**：以重组IL17RB蛋白免疫小鼠，筛选获得高亲和力单克隆抗体。体外实验证实这些抗体能有效抑制IL-25诱导的炎症反应，为治疗哮喘等Th2相关疾病提供了候选药物。
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以上示例结合了IL17RB在信号传导、结构解析、疾病模型及治疗应用中的典型研究方向，供参考格式与内容框架。实际文献需通过学术数据库检索获取。
Interleukin-17 receptor B (IL-17RB), also known as IL-17Rh1 or IL-17BR, is a member of the IL-17 receptor family, which plays a critical role in mediating inflammatory and immune responses. Structurally, IL-17RB is a type I transmembrane protein comprising an extracellular domain with fibronectin III-like motifs, a single transmembrane region, and a cytoplasmic SEF/IL-17R (SEFIR) domain essential for downstream signaling. It primarily binds to IL-17B and IL-17E (IL-25), triggering signaling cascades involving NF-κB and MAPK pathways, which regulate proinflammatory cytokine production and immune cell recruitment.
IL-17RB is implicated in both protective immunity and pathological conditions. It contributes to host defense against parasites and mucosal immunity but is also linked to chronic inflammatory diseases, such as asthma, atopic dermatitis, and autoimmune disorders. Notably, IL-17RB's interaction with IL-25 amplifies type 2 immune responses, promoting eosinophil activation and Th2-associated pathologies. In cancer, IL-17RB overexpression correlates with poor prognosis in pancreatic, breast, and liver cancers, where it facilitates tumor growth, angiogenesis, and metastasis through mechanisms involving cross-talk with oncogenic pathways.
Recombinant IL-17RB proteins are engineered to study receptor-ligand interactions, signaling mechanisms, and therapeutic targeting. Produced via mammalian or insect cell systems, these proteins retain post-translational modifications critical for functional studies. They serve as tools for developing IL-17RB antagonists, monoclonal antibodies, or decoy receptors to block pathogenic signaling in inflammation and cancer. Additionally, recombinant IL-17RB aids in structural studies to map binding epitopes and optimize drug design, highlighting its dual role as a biomarker and therapeutic target in translational research.
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