The gene encoding human CCL11 is located on chromosome 17 and consists of three exons . The protein itself is composed of 93 amino acids and has a calculated molecular mass of approximately 10.8 kDa. When analyzed under reducing conditions using SDS-PAGE, the apparent molecular mass is around 14 kDa .
Eotaxin exerts its effects by binding to specific G-protein-coupled receptors on the surface of target cells. The primary receptors for CCL11 are CCR2, CCR3, and CCR5 . Upon binding to these receptors, eotaxin induces the migration of eosinophils to sites of inflammation or allergic reactions. This recruitment is essential for the body’s defense mechanisms but can also contribute to the pathology of allergic diseases such as asthma.
Recombinant human eotaxin is produced using various expression systems, including Escherichia coli (E. coli) . The recombinant protein often includes a polyhistidine tag (His tag) at the N-terminus to facilitate purification. This tag allows for efficient isolation of the protein using affinity chromatography techniques.
The recombinant eotaxin protein is typically supplied in a lyophilized form and can be reconstituted in a suitable buffer for experimental use. It is crucial to store the protein under sterile conditions at -20°C to -80°C to maintain its stability and avoid repeated freeze-thaw cycles .
Recombinant eotaxin is widely used in research to study the mechanisms of eosinophil recruitment and the role of chemokines in immune responses. It is also employed in the development of therapeutic strategies for treating allergic and inflammatory diseases.