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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL1RA |
| Uniprot No | P18510 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-177aa |
| 氨基酸序列 | RPSGRKSSKMQAFRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVP IEPHALFLGIHGGKMCLSCVKSGDETRLQLEAVNITDLSENRKQDKRFAF IRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYFQE DE |
| 预测分子量 | 17 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. |
1. **"Interleukin-1 receptor antagonist: role in biology"**
*Arend WP, et al.*
摘要：综述IL-1RA的生物学功能，重点阐述其通过竞争性结合IL-1受体抑制炎症反应的机制，及其在自身免疫疾病和炎症性疾病中的潜在治疗作用。
2. **"Recombinant human interleukin-1 receptor antagonist in the treatment of rheumatoid arthritis"**
*Cohen SB, et al.*
摘要：报道一项临床试验，证明重组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，验证其安全性和有效性。
3. **"Cloning and expression of human interleukin-1 receptor antagonist in Escherichia coli"**
*Eisenberg SP, et al.*
摘要：描述通过基因工程技术在大肠杆菌中高效表达重组IL-1RA的流程，并验证其生物活性，为后续药物开发奠定基础。
4. **"Interleukin-1 family cytokines and the expanding spectrum of therapeutic targets"**
*Dinarello CA, et al.*
摘要：探讨IL-1家族(包括IL-1RA)在炎症调控中的作用，分析重组IL-1RA在脓毒症、痛风等疾病中的临床应用前景及挑战。
**Background of Recombinant IL1RA Protein**
The recombinant interleukin-1 receptor antagonist (IL1RA) is a biologically engineered protein designed to mimic the natural IL-1RA, a key regulatory molecule in the human immune system. Discovered in the 1980s, IL-1RA is an endogenous glycoprotein that competitively inhibits the pro-inflammatory effects of interleukin-1 (IL-1), a cytokine central to inflammatory and immune responses. IL-1 exists in two forms, IL-1α and IL-1β, both of which bind to the IL-1 receptor (IL-1R) to activate signaling pathways involved in fever, inflammation, and tissue damage. Uncontrolled IL-1 activity is linked to autoimmune diseases, such as rheumatoid arthritis (RA), and autoinflammatory disorders.
Natural IL1RA acts as a "decoy" receptor, sharing structural homology with IL-1 but lacking intrinsic signaling activity. By binding to IL-1R with high affinity, it blocks IL-1 from initiating downstream inflammatory cascades. However, endogenous IL1RA is produced in limited quantities, often insufficient to counteract excessive IL-1 in pathological conditions. To address this, recombinant IL1RA (rIL1RA) was developed using genetic engineering techniques, enabling large-scale production for therapeutic use.
The most well-known recombinant form, anakinra, is a non-glycosylated version of human IL1RA produced in *Escherichia coli*. Approved by the FDA in 2001. it was the first IL-1-targeting biologic drug, revolutionizing treatment for RA and other IL-1-mediated diseases like neonatal-onset multisystem inflammatory disease (NOMID) and Still’s disease. Its mechanism involves subcutaneous administration to maintain steady inhibition of IL-1R, reducing inflammation and joint damage.
Despite its efficacy, challenges include short half-life requiring daily injections and potential side effects like injection-site reactions. Ongoing research explores modified formulations and combination therapies to enhance its clinical utility. Recombinant IL1RA remains a cornerstone in understanding cytokine regulation and developing targeted anti-inflammatory therapies.
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