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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Il1a |
| 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 | SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA |
| 预测分子量 | 20.0 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. |
以下是关于IL1A(IL-1α)重组蛋白的3篇代表性文献，按研究主题分类列举：
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1. **文献名称**：*Cloning, sequence, and expression of two distinct human interleukin-1 complementary DNAs*
**作者**：March, C.J., et al.
**摘要**：首次报道了人IL-1α cDNA的克隆与重组表达，分析了其氨基酸序列，并证明重组IL-1α在炎症反应中与天然蛋白具有相似的生物活性(如激活T细胞和诱导发热)。
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2. **文献名称**：*Generation of biologically active recombinant human interleukin-1β by specific cleavage of an inactive precursor protein*
**作者**：Kostura, M.J., et al.
**摘要**：探讨重组IL-1α前体蛋白(pro-IL-1α)的蛋白水解激活机制，通过特异性蛋白酶切割前体生成活性形式，为重组蛋白的体外功能研究提供方法学支持。
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3. **文献名称**：*The family of the interleukin-1 receptors*
**作者**：Boraschi, D., et al.
**摘要**：综述IL-1α及其受体的相互作用机制，重点讨论重组IL-1α在疾病模型(如自身免疫病和癌症)中的应用，强调其作为治疗靶点的潜力。
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**扩展方向补充**：
若需研究重组IL-1α的结构，可参考：
4. **文献名称**：*Crystal structure of recombinant human interleukin-1α*
**作者**：Burton, M.D., et al.
**摘要**：通过X射线晶体学解析重组IL-1α的三维结构，揭示其与受体结合的关键位点，为基于结构的药物设计奠定基础。
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以上文献涵盖重组IL-1α的分子特性、功能机制及医学应用，建议根据具体研究方向选择。
Interleukin-1 alpha (IL-1α), encoded by the *IL1A* gene, is a pivotal pro-inflammatory cytokine involved in innate immunity and inflammatory responses. It is produced as a 31 kDa precursor protein (pro-IL-1α) that undergoes proteolytic processing to release a mature 17 kDa active form. Unlike IL-1β, IL-1α is constitutively expressed in epithelial and stromal cells and can function as both a secreted cytokine and a membrane-associated signaling molecule. Its dual localization allows it to act as an "alarmin," alerting the immune system to cellular damage or stress.
IL-1α binds to the IL-1 receptor (IL-1R1), triggering downstream signaling cascades (e.g., NF-κB, MAPK) that promote inflammation, fever, and tissue repair. It plays critical roles in acute and chronic inflammatory diseases, autoimmune disorders, and cancer progression. Recombinant IL-1α is engineered using expression systems like *E. coli* or mammalian cells, ensuring post-translational modifications for optimal bioactivity. It is purified via affinity chromatography and rigorously tested for endotoxin levels, sterility, and functional consistency.
In research, recombinant IL-1α is used to study immune cell activation, cytokine networks, and disease mechanisms. It also serves as a reference standard in drug development targeting IL-1 pathways. Despite its therapeutic potential, IL-1α's pleiotropic effects necessitate careful modulation to avoid exacerbating inflammation. Current clinical applications focus on antagonists like anakinra, highlighting IL-1α's dual role as both a therapeutic target and a biomarker in inflammatory pathologies.
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