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 | Mouse |
| 靶点 | CCL9 |
| Uniprot No | P51670 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-122aa |
| 氨基酸序列 | QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q |
| 预测分子量 | 11.6 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. |
以下是与CCL9重组蛋白相关的3篇文献，简要列举如下：
1. **文献名称**：*CCL9/CCR1轴通过招募CD11b+Gr1+髓系细胞促进肿瘤转移*
**作者**：Kitamura T, et al.
**摘要**：该研究揭示肿瘤细胞分泌的CCL9通过结合受体CCR1.募集CD11b+Gr1+髓系细胞至肿瘤微环境，促进侵袭和转移。实验中利用重组CCL9蛋白验证其对髓系细胞迁移和肿瘤生长的调控作用。
2. **文献名称**：*CCL9(MIP-1γ)通过诱导破骨细胞前体融合调节骨代谢*
**作者**：Kukita T, et al.
**摘要**：研究发现重组CCL9蛋白可直接刺激破骨细胞前体细胞融合，并通过与CCR1受体结合激活下游信号通路，揭示其在骨吸收和骨质疏松中的潜在作用。
3. **文献名称**：*CCL9通过调控巨噬细胞趋化性影响炎症反应*
**作者**：Lu Y, et al.
**摘要**：本文通过体外迁移实验证明，重组CCL9蛋白显著增强巨噬细胞的趋化能力，并依赖MAPK信号通路，提示其在炎症性疾病中的关键功能。
(注：以上文献信息为示例性概括，具体内容建议通过PubMed或期刊数据库核实原文。)
CCL9 (C-C motif chemokine ligand 9), also known as macrophage inflammatory protein-1γ (MIP-1γ) or myeloid progenitor inhibitory factor-2 (MRP-2), is a small secretory protein belonging to the CC chemokine family. It plays a critical role in immune regulation by mediating leukocyte migration and activation through interaction with its primary receptor CCR1. Initially identified in mice, CCL9 is functionally analogous to human CCL23. sharing structural homology and overlapping roles in inflammatory responses. It is predominantly produced by stromal cells, macrophages, and certain tumor cells, influencing both innate and adaptive immunity.
Structurally, CCL9 contains four conserved cysteine residues forming two disulfide bonds, a hallmark of CC chemokines. Its recombinant form is typically produced using bacterial (e.g., E. coli) or mammalian expression systems, followed by purification via chromatography to ensure high purity and bioactivity. Recombinant CCL9 retains the ability to bind CCR1 and induce chemotaxis in target cells like monocytes, dendritic cells, and neutrophils. This makes it a valuable tool for studying immune cell trafficking, inflammatory pathways, and tumor microenvironment interactions.
Research applications of recombinant CCL9 span in vitro assays (e.g., cell migration studies) and in vivo models to explore its role in diseases such as chronic inflammation, cancer progression, and autoimmune disorders. Emerging evidence also highlights its dual role in cancer biology, acting as either a promoter or suppressor depending on context, which underscores its therapeutic potential. Additionally, recombinant CCL9 aids in drug discovery efforts targeting chemokine-receptor interactions. Despite progress, species-specific differences between murine CCL9 and human CCL23 warrant careful interpretation in translational studies.
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