Human Recombinant Fractalkine (CX3CL1)

Fractalkine. The chemokine domain is connected to an extended mucin-like stalk, followed by a transmembrane region, and a C-terminal intracellular domain. The protein signals thro μgh interaction with a single receptor, CX3CR1, expressed on monocytes, natural killer cells, T cells, microglia, and smooth muscle cells. Fractalkine is upregulated in endothelial cells by inflammatory signals and is synthesized as a membrane-bound molecule that mediates cell migration and adhesion (White & Greaves). Cleavage at the base of the stalk by metalloproteinases generates a soluble chemokine, which functions as a potent chemoattractant of target cells (Garton et al.; Apostolakis & Spandidos). Fractalkine has been implicated in pathology of inflammatory diseases, such as atherosclerosis and other vascular diseases, and has anti-apoptotic functions (White & Greaves).