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| 纯度 | >98%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL17 |
| Uniprot No | Q16552 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-155aa |
| 氨基酸序列 | MIVKAGITIP RNPGCPNSED KNFPRTVMVN LNIHNRNTNT NPKRSSDYYN RSTSPWNLHR NEDPERYPSV IWEAKCRHLG CINADGNVDY HMNSVPIQQE ILVLRREPPH CPNSFRLEKI LVSVGCTCVT PIVHHVA |
| 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. |
以下是关于IL17重组蛋白的3篇参考文献示例(注：文献信息为示例，实际引用时请核对原文)：
1. **《Production and characterization of recombinant human IL-17A in Escherichia coli》**
- 作者：Smith A, et al.
- 摘要：研究通过大肠杆菌表达系统高效制备重组人IL-17A蛋白，优化纯化工艺并验证其生物活性(如诱导炎性细胞因子分泌)。
2. **《IL-17F recombinant protein exacerbates autoimmune arthritis in murine models》**
- 作者：Jones R, et al.
- 摘要：利用重组IL-17F蛋白注射小鼠，揭示其在类风湿关节炎模型中增强中性粒细胞浸润和骨侵蚀的作用机制。
3. **《Therapeutic potential of IL-17 neutralizing recombinant fusion protein in psoriasis》**
- 作者：Wang L, et al.
- 摘要：开发靶向IL-17的重组融合蛋白，通过阻断IL-17信号通路显著改善银屑病动物模型的皮肤炎症及病理损伤。
4. **《Structural and functional analysis of glycosylated IL-17A recombinant protein》**
- 作者：Kim S, et al.
- 摘要：对比哺乳动物细胞(CHO)表达的重组IL-17A糖基化修饰对蛋白稳定性及受体结合能力的影响，揭示糖基化对其功能的关键作用。
(提示：以上为虚拟文献，建议通过PubMed或Web of Science检索真实文献，关键词如“recombinant IL-17 protein”、“IL-17 expression”等。)
Interleukin-17 (IL-17) is a pro-inflammatory cytokine primarily produced by Th17 cells, γδ T cells, and other immune cells. It plays a pivotal role in host defense against extracellular pathogens but is also implicated in autoimmune and chronic inflammatory diseases, such as psoriasis, rheumatoid arthritis, and inflammatory bowel disease. The IL-17 family consists of six members (IL-17A to IL-17F), with IL-17A (commonly referred to as IL-17) and IL-17F being the most studied due to their overlapping functions in promoting neutrophil recruitment and tissue inflammation via induction of chemokines and antimicrobial peptides.
Recombinant IL-17 proteins are engineered using genetic modification techniques, typically expressed in mammalian (e.g., HEK293. CHO cells) or bacterial systems. These proteins retain the biological activity of native IL-17 and are widely utilized in research to study signaling pathways, immune responses, and therapeutic targets. For instance, recombinant IL-17 is critical in elucidating its interaction with the IL-17 receptor (IL-17R), which activates NF-κB and MAPK pathways, driving inflammatory gene expression.
In drug development, recombinant IL-17 serves as a tool for screening inhibitors or neutralizing antibodies. Therapeutics targeting the IL-17/IL-17R axis, such as secukinumab and ixekizumab (anti-IL-17A monoclonal antibodies), have been approved for autoimmune diseases, highlighting the translational relevance of recombinant IL-17 in preclinical studies. However, challenges remain in optimizing protein stability, post-translational modifications, and scalable production. Recent advances in protein engineering and quality control (e.g., HPLC, mass spectrometry) ensure high-purity recombinant IL-17 for reliable experimental and clinical applications, accelerating both mechanistic research and biopharmaceutical innovation.
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