Recombinant Mouse CCL9 protein

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.