Recombinant Human CCL8 protein

CCL8 (C-C motif chemokine ligand 8), also known as monocyte chemoattractant protein-2 (MCP-2), is a small secretory protein belonging to the CC chemokine family. It plays a critical role in immune regulation by recruiting leukocytes, including monocytes, lymphocytes, eosinophils, and basophils, to sites of inflammation or infection. CCL8 is produced by various cell types, such as monocytes, fibroblasts, and endothelial cells, in response to pro-inflammatory stimuli like TNF-α, IL-1β, or viral components. Its activity is mediated through binding to chemokine receptors, primarily CCR1. CCR2. CCR3. and CCR5. which are expressed on target immune cells.

Recombinant CCL8 protein is engineered using biotechnology platforms (e.g., E. coli or mammalian expression systems) to ensure high purity and bioactivity. It typically retains the conserved structure of natural CCL8. including a signal peptide and a mature protein domain with characteristic disulfide bonds critical for receptor interaction. Researchers utilize recombinant CCL8 to study chemokine-mediated immune responses, inflammatory diseases (e.g., rheumatoid arthritis, asthma), cancer progression (via tumor microenvironment modulation), and viral infections (e.g., HIV, as CCR5 is a co-receptor). It is also employed in in vitro assays to evaluate cell migration, receptor signaling pathways, and potential therapeutic inhibitors. Quality-controlled batches are validated using techniques like HPLC, SDS-PAGE, and functional cell-based migration assays to ensure consistency for experimental reproducibility.