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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL11 |
| Uniprot No | P20809 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-199aa |
| 氨基酸序列 | PGPPPGPPRV SPDPRAELDS TVLLTRSLLA DTRQLAAQLR DKFPADGDHN LDSLPTLAMS AGALGALQLP GVLTRLRADL LSYLRHVQWL RRAGGSSLKT LEPELGTLQA RLDRLLRRLQ LLMSRLALPQ PPPDPPAPPL APPSSAWGGI RAAHAILGGL HLTLDWAVRG LLLLKTRL |
| 预测分子量 | 19 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IL11重组蛋白的3篇参考文献的简要信息：
1. **文献名称**: *"Recombinant human interleukin-11 (IL-11) improves thrombocytopenia and reduces platelet transfusion requirements in patients with non-myeloid malignancies"*
**作者**: Gordon MS, et al.
**摘要**: 该研究报道了重组人IL-11在治疗化疗引起的血小板减少症中的作用，通过促进巨核细胞分化提升血小板水平，减少患者对输血的依赖。
2. **文献名称**: *"IL-11 is a crucial determinant of cardiovascular fibrosis"*
**作者**: Widjaja AA, et al.
**摘要**: 研究发现IL-11通过激活ERK信号通路，促进心脏成纤维细胞活化，导致心肌纤维化和心力衰竭，为靶向IL-11治疗心血管疾病提供了依据。
3. **文献名称**: *"Interleukin-11 receptor signaling promotes adenocarcinoma development in the lung"*
**作者**: Ng B, et al.
**摘要**: 揭示IL-11/IL-11Rα轴通过STAT3和MAPK通路驱动肺腺癌进展，抑制该信号可减少肿瘤生长，提示其作为癌症治疗靶点的潜力。
如需具体文献年份或期刊名称，可补充说明进一步检索。
Interleukin-11 (IL-11) is a pleiotropic cytokine first identified in 1990 for its ability to stimulate megakaryocyte proliferation and platelet production. It belongs to the IL-6 family of cytokines, sharing structural homology and signaling pathways mediated through the gp130 receptor subunit. IL-11 is primarily secreted by stromal cells, fibroblasts, osteoblasts, and certain epithelial cells, playing critical roles in hematopoiesis, tissue repair, and immune modulation. Its biological effects are mediated by binding to a specific IL-11 receptor alpha chain (IL-11Rα), which recruits gp130 to activate downstream JAK/STAT, MAPK, and PI3K pathways.
Recombinant IL-11 proteins are engineered using expression systems like *E. coli* or mammalian cells to mimic natural IL-11 activity. These proteins retain the functional epitopes required for receptor interaction and signaling. Clinically, recombinant human IL-11 (rhIL-11. Oprelvekin) was approved to prevent chemotherapy-induced thrombocytopenia by promoting platelet recovery. However, its use is limited due to side effects like fluid retention and cardiac arrhythmias.
Beyond hematopoiesis, IL-11 is implicated in pathological processes, including fibrosis, inflammation, and cancer progression. Studies highlight its role in epithelial cell survival, extracellular matrix remodeling, and tumor microenvironment modulation, making it a therapeutic target in diseases like pulmonary fibrosis and gastrointestinal cancers. Research-grade recombinant IL-11 is widely utilized *in vitro* and *in vivo* to dissect its signaling mechanisms and evaluate therapeutic interventions. Ongoing studies aim to engineer modified IL-11 variants with improved specificity or reduced toxicity for clinical applications.
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