CCL8, also known as MCP-2, is a beta chemokine initially isolated from human MG-63 osteosarcoma cells that are stimulated with IL-1β. CCL8 (MCP-2) has a structure and function that is similar with both MCP-1 and MCP-3. It is often co-induced with those chemokines in mononuclear cells. IFNγ is a strong inducer of CCL8 (MCP-2) in monocytes and fibroblasts. CCL8 (MCP-2) in monocytes and fibroblasts and can be processed and secreted as a truncated chemokine CCL8 (6-75). This isoform does not chemo attract monocytes, but it binds to the CCR2 receptor and induces its internalization. As a result, CCL8 (MCP-2) inhibits MCP-1 (CCL2) and MCP-2 (CCL8) ERK signaling and antagonizes the chemotactic activity of several CCR2 ligands (MCP-1/CCL2, MCP-2/CCL8, MCP-3/CCL7). CCL8 (MCP-2) is highly expressed in the skin, and it serves as an agonist for the chemokine receptor CCR8, but not for CCR2. Therefore, it has been speculated that the CCL8-CCR8 interaction is a crucial regulator of the Th2 homing, which drives IL-5 mediated chronic allergic inflammation. In addition, CCL8 (MCP-2) binds the CCR5 receptor with a high affinity and inhibits the replication of human immunodeficiency virus type 1. CCL8 (MCP-2) is highly expressed in different human diseases, and it is a potential biomarker for the diagnosis of graft-versus-host diseases and tuberculosis.
Size
4 pack
Concentration
n/a
Applications
ELISA
Other Names
Monocyte chemotactic protein2, MCP-2; Small inducible cytokine subfamily A, member 8, SCYA8