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| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL-1α |
| Uniprot No | P01583 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 113-271aa |
| 氨基酸序列 | SAPFSFLSNV KYNFMRIIKY EFILNDALNQ SIIRANDQYL TAAALHNLDE AVKFDMGAYK SSKDDAKITV ILRISKTQLY VTAQDEDQPV LLKEMPEIPK TITGSETNLL FFWETHGTKN YFTSVAHPNL FIATKQDYWV CLAGGPPSIT DFQILENQA |
| 预测分子量 | 18.0 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3篇与IL-1伪重组蛋白相关的文献摘要(内容基于真实研究方向简化概括)：
1. **"Production and characterization of recombinant human IL-1 receptor antagonist"**
- 作者：Eisenberg, S.P. 等
- 摘要：该研究描述了大肠杆菌中重组人IL-1受体拮抗剂(IL-1Ra)的高效表达与纯化方法，验证其能够有效阻断IL-1α和IL-1β与受体的结合，并在动物模型中展示抗炎活性。
2. **"Interleukin-1 receptor antagonist: role in biology"**
- 作者：Dinarello, C.A.
- 摘要：综述IL-1Ra的分子机制及病理生理作用，强调重组IL-1Ra蛋白在调控过度炎症反应中的治疗潜力，并讨论其在类风湿性关节炎等疾病中的临床试验结果。
3. **"Treatment of rheumatoid arthritis with recombinant human interleukin-1 receptor antagonist"**
- 作者：Bresnihan, B. 等
- 摘要：临床研究证实皮下注射重组IL-1Ra(Anakinra)可显著缓解类风湿性关节炎患者的关节症状和炎症指标，验证其作为IL-1信号通路抑制剂的治疗价值。
注：以上文献标题和内容方向参考自IL-1研究领域经典论文，具体细节需通过学术数据库(如PubMed)检索原文确认。IL-1伪重组蛋白通常指通过基因工程表达的IL-1通路调控蛋白(如拮抗剂或突变体)。
Interleukin-1 (IL-1) pseudo-recombinant proteins are engineered molecules designed to modulate IL-1 signaling, a critical pathway in inflammation and immune responses. The IL-1 family comprises key cytokines like IL-1α and IL-1β, which bind to IL-1 receptors (IL-1R1 and IL-1R2) to regulate pro-inflammatory processes. Dysregulation of this pathway is implicated in autoimmune diseases, chronic inflammation, and cytokine storm syndromes. Traditional IL-1 inhibitors, such as recombinant IL-1 receptor antagonists (e.g., anakinra) or neutralizing antibodies, have therapeutic limitations, including short half-life or immunogenicity.
IL-1 pseudo-recombinant proteins are hybrid molecules combining functional domains of IL-1 receptors or binding proteins with stabilizing elements (e.g., Fc regions). For example, constructs may fuse the extracellular domain of IL-1R1 or IL-1R2 (which binds IL-1 cytokines) to immunoglobulin Fc fragments to enhance pharmacokinetics. These proteins act as decoy receptors, competitively inhibiting IL-1α/β from engaging native receptors, thereby suppressing downstream NF-κB and MAPK signaling. Unlike natural inhibitors, pseudo-recombinant variants are optimized for prolonged serum stability and reduced clearance.
Their development leverages recombinant DNA technology, often using mammalian expression systems to ensure proper post-translational modifications. Applications span therapeutic research (e.g., rheumatoid arthritis, sepsis) and mechanistic studies of IL-1-driven pathologies. Challenges include balancing high-affinity binding with minimal off-target effects and ensuring proper dimerization for functional activity. Ongoing research aims to refine specificity and delivery methods, positioning IL-1 pseudo-recombinant proteins as versatile tools for both clinical and experimental immunology.
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