CCL13 is induced by inflammatory proteins such as interleukin-1 (IL-1) and tumor necrosis factor-alpha (TNF-alpha) . The gene encoding CCL13 is located on human chromosome 17, within a large cluster of other CC chemokines . This clustering suggests a coordinated regulation and function of these chemokines in immune responses.
CCL13 functions by binding to three different G protein-coupled receptors: CCR2, CCR3, and CCR5 . These receptors are expressed on the surface of target cells and mediate the chemotactic response, leading to the directed movement of immune cells towards the site of inflammation or infection . This signaling is particularly important in the context of allergic responses and other inflammatory conditions.
The biological activity of CCL13 includes the induction of chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils . This chemotactic activity is essential for the recruitment of these immune cells to sites of inflammation, where they can exert their effector functions. The ability of CCL13 to attract a diverse range of immune cells highlights its importance in coordinating the immune response.
Human recombinant CCL13 is produced using an expression system in Escherichia coli (E. coli) . The recombinant protein is purified to a high degree of purity, typically greater than 98%, and is free from endotoxins . This high level of purity is essential for its use in research applications, where it is used to study the chemotactic properties and signaling mechanisms of CCL13.
Recombinant CCL13 is widely used in various research applications, including Western blotting, enzyme-linked immunosorbent assay (ELISA), and functional assays . These applications help researchers to understand the role of CCL13 in immune responses and to explore its potential as a therapeutic target in inflammatory and allergic diseases.