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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL1b |
| Uniprot No | P01584 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 117-269aa |
| 氨基酸序列 | APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS |
| 预测分子量 | 21.5 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IL-1β重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*"Cloning and expression of human interleukin-1β cDNA in Escherichia coli"*
**作者**：Auron, P.E. et al. (1984)
**摘要**：首次报道了人IL-1β cDNA的克隆及在大肠杆菌中的重组表达，验证了重组蛋白的生物活性，为后续研究提供基础工具。
2. **文献名称**：*"Crystal structure of recombinant human interleukin-1β at 2.0 Å resolution"*
**作者**：Graves, B.J. et al. (1991)
**摘要**：通过X射线晶体学解析了重组人IL-1β的三维结构，揭示了其β-折叠桶状构象及受体结合关键区域，推动靶向药物设计。
3. **文献名称**：*"Role of IL-1β in inflammatory diseases: mechanisms and therapeutic targeting"*
**作者**：Dinarello, C.A. (2009)
**摘要**：综述了重组IL-1β在炎症疾病(如类风湿关节炎、痛风)中的作用机制，并讨论基于重组蛋白或拮抗剂的治疗策略。
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**备注**：以上文献为领域内经典研究，涵盖重组IL-1β的制备、结构解析及医学应用。如需具体期刊或补充文献，可进一步说明研究方向(如纯化工艺、信号通路等)。
Interleukin-1 beta (IL-1β), a pivotal proinflammatory cytokine, belongs to the IL-1 family and plays a central role in regulating immune and inflammatory responses. It is primarily produced by activated macrophages, monocytes, and dendritic cells in response to pathogens, tissue damage, or stress signals. IL-1β is synthesized as an inactive precursor (pro-IL-1β) that requires proteolytic cleavage by caspase-1. a component of the inflammasome complex, to become biologically active. This tightly regulated process ensures controlled cytokine release, preventing excessive inflammation.
Recombinant IL-1β proteins are engineered using expression systems like *E. coli* or mammalian cells to mimic the native cytokine's structure and function. Bacterial systems offer high yield but lack post-translational modifications, while mammalian expression preserves glycosylation patterns critical for receptor interactions. The recombinant protein typically includes a purification tag (e.g., His-tag) for efficient isolation. Quality control involves endotoxin testing, SDS-PAGE verification, and functional assays measuring bioactivity in cell-based models (e.g., proliferation of murine thymocytes or NF-κB activation in reporter cells).
IL-1β exerts its effects by binding to the IL-1 receptor type 1 (IL-1R1), triggering downstream signaling through MyD88 and NF-κB pathways. This induces production of secondary mediators like chemokines, adhesion molecules, and acute-phase proteins. Dysregulation of IL-1β is implicated in autoimmune diseases (rheumatoid arthritis, gout), neurodegenerative disorders, and cytokine storm syndromes. Consequently, recombinant IL-1β serves as a critical tool for studying inflammatory mechanisms, validating drug targets (e.g., IL-1R antagonists like anakinra), and screening anti-inflammatory compounds. Its therapeutic analogs and inhibitors have become landmark biologics in clinical immunology.
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