CX3CL1 ELISA Kits

CX3CL1 consists of a chemokine domain linked to a transmembrane domain via an extended mucin-rich stalk of an extracellular domain. The chemokine is synthesized as membrane-anchored form and may be cleaved in the soluble form by different metalloprotease. The membrane-anchored CX3CL1 form functions as an adhesion molecule promoting retention of leucocytes to endothelial cells under physiological flow conditions. The soluble CX3CL1 form is released following constitutive shedding operated by A Disintegrin And Metalloprotease (ADAM)10, whereas shedding under inflammatory conditions is mediated primarily by ADAM17. CX3CL1 cleavage is also mediated by the lysosomal cysteine protease Cathepsin S. Soluble CX3CL1 resembles a conventional chemokine exhibiting efficient chemotactic activity for human monocytes, NK cells, T cells, dendritic cells. CX3CL1 expression has been reported in many cell types of hematopoietic or nonhematopoietic origin, such as endothelial and epithelial cells, lymphocytes, neurons, microglial cells, and osteoblasts.

CX3CL1-driven chemotaxis and adhesion are mediated by CX3CR1 that is expressed on different cell types such as NK cells, CD14+ monocytes, cytotoxic effector T cells, B cells, neurons, microglia, smooth muscle cells, and tumor cells. CX3CL1 is involved in leukocyte recruitment associated with numerous inflammatory disorders and in tumorigenesis process in which the chemokine show pro- and antitumoral properties. The different roles of CX3CL1 make it an attractive candidate for the development of therapeutic strategies. promotes the accumulation of immune cells that express CX3CR1, generating a vascular gateway for cytotoxic effector cells and being detrimental in several inflammatory diseases.