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Fractalkine (CX3CL1) is a unique chemokine belonging to the CX3C family, and is characterized by a C-X3-C cysteine motif within the chemokine domain, near the amino terminus of the protein (Bazan et al.). The chemokine domain is connected to an extended mucin-like stalk, followed by a transmembrane region, and a C-terminal intracellular domain (Imai et al.; Jones et al.). The protein signals through 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).
Subtype
Cytokines
Alternative Names
C3Xkine, Chemokine (C-X3-C motif) ligand 1, FKN, Neurotactin, NTN, NTT, SCYD1, Small inducible cytokine subfamily D member 1
Cell Type
Dendritic Cells, Endothelial Cells, Macrophages, Monocytes, NK Cells, T Cells
(A) The biological activity of Human Recombinant Fractalkine (CX3CL1) was tested by its ability to mobilize Ca2+ in CHO-K1/Gα15/hCX3CR1 (human Gα15 and human CX3CR1 stably expressed in CHO-K1 cells) cells. Ca2+ mobilization was measured using a fluorometric assay method. The EC50 is defined as the effective concentration of the growth factor at which Ca2+ mobilization is at 50% of maximum. The EC50 in the example above is less than 1.5 μg/mL.
(B) 2 μg of Human Recombinant Fractalkine (CX3CL1) was resolved with SDS-PAGE under reducing (+) and non-reducing (-) conditions and visualized by Coomassie Blue staining. Human Recombinant Fractalkine (CX3CL1) has a predicted molecular mass of 50 - 75 kDa.
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