首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CSF2 |
| Uniprot No | P04141 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-144aa |
| 氨基酸序列 | APARSPSPST QPWEHVNAIQ EARRLLNLSR DTAAEMNETV EVISEMFDLQ EPTCLQTRLE LYKQGLRGSL TKLKGPLTMM ASHYKQHCPP TPETSCATQT ITFESFKENL KDFLLVIPFD CWEPVQE |
| 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CSF2(粒细胞-巨噬细胞集落刺激因子，GM-CSF)重组蛋白的3篇代表性文献示例(注：文献信息为模拟概括，仅供参考)：
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1. **文献名称**：*Optimized Expression and Purification of Recombinant Human GM-CSF in E. coli for Clinical Applications*
**作者**：Ye, J., et al.
**摘要**：本研究报道了一种在大肠杆菌中高效表达重组人GM-CSF的优化方法，通过密码子优化和纯化工艺改进，显著提高了蛋白产量和生物活性，为规模化生产奠定了基础。
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2. **文献名称**：*Recombinant GM-CSF Enhances Neutrophil Recovery in Chemotherapy-Induced Myelosuppression: A Phase II Clinical Trial*
**作者**：Johnson, R.W., et al.
**摘要**：通过一项II期临床试验，验证了重组GM-CSF在化疗导致的中性粒细胞减少症中的治疗效果，证明其能显著缩短恢复时间并降低感染风险。
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3. **文献名称**：*Structural and Functional Analysis of Glycosylated vs. Non-glycosylated Recombinant GM-CSF*
**作者**：Lee, S., & Smith, T.P.
**摘要**：比较了真核(糖基化)与原核(非糖基化)系统生产的重组GM-CSF的结构差异，发现糖基化修饰影响蛋白稳定性但未显著改变其体外促造血活性。
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如需真实文献，建议通过PubMed或Web of Science检索关键词(如“recombinant GM-CSF”或“CSF2 protein”)，并筛选近年高被引研究或权威期刊论文。
**Background of CSF2 Recombinant Protein**
Colony-stimulating factor 2 (CSF2), also known as granulocyte-macrophage colony-stimulating factor (GM-CSF), is a cytokine critical for regulating immune responses and hematopoiesis. It stimulates the proliferation, differentiation, and functional activation of granulocytes, macrophages, and dendritic cells. CSF2 binds to a heterodimeric receptor complex (GM-CSFRα and βc subunits), activating downstream signaling pathways such as JAK/STAT, MAPK, and PI3K, which mediate its biological effects.
Recombinant CSF2 protein is produced using genetic engineering techniques, often in mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications. The recombinant form retains the native protein's functional properties, including promoting leukocyte production, enhancing antigen presentation, and modulating inflammation.
Clinically, CSF2 recombinant protein has therapeutic applications in treating neutropenia, accelerating hematopoietic recovery after chemotherapy or bone marrow transplantation, and boosting immune responses in cancer immunotherapy. It is also explored as an adjuvant in vaccines to improve efficacy by activating dendritic cells. Research continues to investigate its role in autoimmune diseases, infectious diseases, and chronic inflammatory conditions, though its dual pro-inflammatory and immunosuppressive functions require careful dose and context optimization.
Despite its therapeutic potential, challenges remain, such as managing cytokine release syndrome or tissue inflammation. Ongoing studies aim to refine delivery methods and explore engineered variants to enhance specificity and reduce off-target effects.
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