Description: CCL8, also known as MCP-2 (Monocyte Chemotactic Protein 2), is a member of the CC- subfamily of chemokines and is most closely related to CCL2 (MCP-1) and CCL7 (MCP-3). All three MCPs are secreted by a variety of cell types in response to inflammatory stimuli and play critical roles in the recruitment of leukocytes to areas of inflammation. While they are potent chemoattractants of monocytes and T cells, CCL7 appears to have the broadest range of activity, as it has also been demonstrated to attract activated NK cells, eosinophils, basophils, and neutrophils. CCL8 has also been demonstrated to attract NK cells, eosinophils, and basophils, but requires higher concentrations to do so. CCL8 signals via the G protein-coupled receptor CCR5, which is shared with other CC-chemokines. CCR5 is the primary co-receptor for HIV entry, which the virus binds through the gp120 envelope protein. All CCR5 ligands demonstrate potent inhibition of virus entry into the cell, both through steric hindrance of gp120-CCR5 interaction, and ligand-mediated receptor internalization.