首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL3 |
| Uniprot No | P08700 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-152aa |
| 氨基酸序列 | APMTQTTSLKTSWVNCSNMIDEIITHLKQPPLPLLDFNNLNGEDQDILME NNLRRPNLEAFNRAVKSLQNASAIESILKNLLPCLPLATAAPTRHPIHIK DGDWNEFRRKLTFYLKTLENAQAQQTTLSLAIF |
| 预测分子量 | 15 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IL-3重组蛋白的3篇参考文献及其摘要概括：
1. **《Expression of human interleukin-3 (IL-3) in E. coli: IL-3-mediated hematopoietic activity in vitro》**
- **作者**：Yang, Y.C., et al.
- **摘要**：该研究首次报道了人源IL-3基因在大肠杆菌中的重组表达，验证了重组蛋白在体外促进造血祖细胞增殖和分化的活性，为后续IL-3的临床应用奠定基础。
2. **《Purification and characterization of recombinant human interleukin-3 produced in mammalian cells》**
- **作者**：Kaushansky, K., et al.
- **摘要**：通过哺乳动物细胞表达系统(如CHO细胞)纯化IL-3重组蛋白，分析了其糖基化修饰对蛋白稳定性和功能的影响，证明其与天然IL-3具有相似的受体结合活性。
3. **《IL-3 in the treatment of chemotherapy-induced myelosuppression: Phase I clinical trial》**
- **作者**：Ganser, A., et al.
- **摘要**：一项针对化疗后骨髓抑制患者的I期临床试验，证实重组IL-3可显著提升中性粒细胞和血小板水平，初步验证其治疗骨髓衰竭的安全性及有效性。
4. **《Structural and functional analysis of IL-3 using site-directed mutagenesis》**
- **作者**：López, A.F., et al.
- **摘要**：通过定点突变技术研究IL-3重组蛋白的关键功能域，揭示了其受体结合位点及信号激活机制，为开发改良型IL-3类似物提供理论支持。
(注：以上文献信息为示例性概括，实际引用需核对原文。)
**Background on IL-3 Recombinant Protein**
Interleukin-3 (IL-3) is a multifunctional cytokine first identified in the 1980s for its role in regulating hematopoiesis. Produced primarily by activated T cells, mast cells, and stromal cells, IL-3 binds to the IL-3 receptor (IL-3R), a heterodimer composed of a unique α-subunit (CD123) and a shared β-subunit common to receptors for IL-5 and GM-CSF. This interaction activates downstream signaling pathways, such as JAK-STAT, MAPK, and PI3K, promoting the survival, proliferation, and differentiation of hematopoietic stem and progenitor cells (HSPCs) into myeloid lineages, including granulocytes, macrophages, and dendritic cells.
Recombinant IL-3 is engineered using genetic cloning techniques, where the *IL3* gene is inserted into expression systems like *E. coli*, yeast, or mammalian cells (e.g., CHO cells). Bacterial systems offer cost-effective production but lack post-translational modifications, while mammalian systems ensure proper glycosylation and bioactivity. The purified protein is extensively characterized for purity, stability, and functionality via SDS-PAGE, ELISA, and cell-based assays.
In research, recombinant IL-3 is pivotal for studying hematopoiesis, immune responses, and diseases like leukemia, where CD123 is often overexpressed. Clinically, it has been explored to accelerate hematopoietic recovery post-chemotherapy or bone marrow transplantation. However, its therapeutic use remains limited due to risks of inflammation and off-target effects. Recent advances focus on engineered IL-3 variants or antibody-cytokine conjugates to enhance specificity and reduce toxicity.
Overall, IL-3 recombinant protein serves as a critical tool in both basic science and translational medicine, with ongoing efforts to refine its applications in regenerative and cancer therapies.
×
