Recombinant Human Ccl6 protein

Ccl6 (chemokine (C-C motif) ligand 6), also known as MRP-1 (myeloid-related protein 1), is a small secreted protein belonging to the CC chemokine family. It plays a role in immune cell recruitment, inflammation, and tissue remodeling. Initially identified in mice, Ccl6 is primarily produced by macrophages, fibroblasts, and epithelial cells under inflammatory conditions. Its human functional homolog, CCL23. shares structural similarities but differs in gene localization and regulatory mechanisms. The protein interacts with chemokine receptors such as CCR1 and CCR3. mediating leukocyte migration, particularly monocytes, neutrophils, and T cells, to sites of infection or injury.

Ccl6 is implicated in diverse physiological and pathological processes, including chronic inflammation, fibrosis, and cancer progression. Studies highlight its dual role: while promoting tissue repair in acute settings, it may exacerbate pathological remodeling in chronic diseases. In cancer, Ccl6 contributes to tumor-associated macrophage infiltration, angiogenesis, and metastasis, making it a potential therapeutic target.

Recombinant Ccl6 protein is produced using expression systems like *E. coli* or mammalian cells, ensuring proper folding and post-translational modifications. Purification involves affinity chromatography, yielding high-purity bioactive protein for experimental applications. Researchers use it to study chemotaxis, immune cell activation, receptor-ligand interactions, and signaling pathways (e.g., MAPK/ERK, PI3K/Akt) in vitro. In vivo, it helps model disease mechanisms or test blocking antibodies/inhibitors in preclinical settings. Its structure includes a conserved CC motif and a C-terminal extended domain, critical for receptor binding and oligomerization. Despite progress, Ccl6's context-dependent functions and cross-species variability warrant further exploration to clarify its therapeutic potential.