Monocyte Chemotactic Protein-5 (MCP-5), also known as Chemokine (C-C motif) ligand 12 (CCL12), is a small cytokine belonging to the CC chemokine family. It has been characterized in mice and is closely related to human MCP-1, sometimes referred to as MCP-1-related chemokine . MCP-5 plays a crucial role in the immune system by attracting monocytes, eosinophils, and lymphocytes to sites of inflammation, but not neutrophils .
MCP-5 is expressed constitutively in the thymus and lymph nodes. Under inflammatory conditions, its expression is induced in activated macrophages and mast cells . This chemokine is involved in allergic inflammation and the host response to pathogens, playing a pivotal role during the early stages of allergic lung inflammation . MCP-5 signals through the CCR2 receptor, which is also used by other chemokines like MCP-1 .
Recombinant MCP-5 is typically produced in Escherichia coli (E. coli) expression systems. The recombinant protein is purified and lyophilized for use in various research applications. For instance, the recombinant murine MCP-5 is a 9.3 kDa protein containing 82 amino acid residues, including the four highly conserved cysteine residues present in the CC chemokines . The protein is purified to a high degree, with a purity of ≥ 98% as determined by SDS-PAGE gel and HPLC analyses .
Recombinant MCP-5 is used in various research applications, including studies on chemotaxis, inflammation, and immune response. It is particularly useful in in vitro assays to study the chemotactic activity of monocytes and other immune cells . The ability of MCP-5 to attract specific cell types makes it a valuable tool for understanding the mechanisms of immune cell migration and the role of chemokines in disease processes.