Recombinant mouse CXCL16 protein

CXCL16 is a unique member of the CXC chemokine family, functioning both as a chemotactic cytokine and a transmembrane scavenger receptor. It exists in two forms: a membrane-bound protein expressed on antigen-presenting cells (e.g., dendritic cells, macrophages) and epithelial cells, and a soluble form released through proteolytic cleavage. The membrane-bound CXCL16 mediates cell adhesion by interacting with its sole receptor, CXCR6. expressed on T cells, natural killer T (NKT) cells, and activated CD8+ T cells. The soluble form acts as a chemoattractant, directing the migration of CXCR6-expressing immune cells to inflammatory or tumor sites. Structurally, CXCL16 contains a chemokine domain, a mucin-like stalk, a transmembrane domain, and a cytoplasmic tail, distinguishing it from other chemokines.

Recombinant CXCL16 protein is produced using genetic engineering techniques, typically in mammalian expression systems to ensure proper post-translational modifications. This purified protein retains biological activity, enabling researchers to study CXCL16-CXCR6 signaling pathways, immune cell recruitment mechanisms, and its dual roles in inflammation and immune surveillance. Studies highlight its involvement in diseases such as atherosclerosis (via oxidized LDL uptake), cancer progression (modulating tumor microenvironment), and autoimmune disorders (e.g., rheumatoid arthritis). Recombinant CXCL16 is widely used in in vitro assays (e.g., cell migration, receptor binding) and animal models to explore therapeutic targeting. Its scavenger receptor function in pathogen clearance (e.g., bacteria, viruses) further underscores its immunological relevance. Research continues to unravel its context-dependent roles, balancing pro-inflammatory and homeostatic functions, making it a potential biomarker or therapeutic target in chronic diseases.