MCP-2 Protein/CCL8

CCL8, also known as monocyte chemotactic protein 2 ( MCP2), is a small cell factor belonging to the CC chemokine family. First identified in human osteosarcoma cells, it is a protein encoded by the CCL8 gene located on human chromosome 17. CCL8 is mainly expressed in small intestine and peripheral blood cells. CCL8 can bind to several different chemokine cell surface receptors, such as CCR1, CCR2B, CCR3 and CCR5. CCL8 can act as a chemoattractant, attracting chemokines such as monocytes, lymphocytes, basophils and eosinophils to mediate inflammatory host responses. On the one hand, CCL8 contributes to the spread of breast cancer and promotes the migration and invasion of esophageal squamous cell carcinoma. On the other hand, it has also been reported that CCL8 inhibits cervical cancer tumor growth and exhibits anti-tumor metastatic effects in melanoma. cCL8 significantly activates ERK1/2 phosphorylation in glioblastoma cells and significantly reduces the invasiveness of glioma cells by neutralizing antibody blockade of tama-secreted CCL8. At the same time, CCL8 can act as a potent HIV1 inhibitor with high affinity for the receptor CCR5, which is one of the major co-receptors for HIV1[1][2].