IL-8 (human):Fc (human) (rec.) (nonlytic)

Unfortunately, most cytokines have short circulating half-lives. With the creation of a group of new immunoglobulin- based cytokine fusion proteins, in which a cytokine sequence had been genetically fused to the hinge, CH2 and CH3 regions of an immunoglobulin, these cytokine fusion proteins possess both the biological functions of the cytokine moiety and the prolonged circulating half-life determined by the Fc domain. Interleukin-8 (IL-8) was originally discovered as a neutrophil chemotactic and activating factor and is a member of the alpha (CXC) subfamily of chemokines (including also platelet factor 4, GRO, IP-10, etc.). Many cell types, including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, keratinocytes, hepatocytes, chondrocytes and various tumor cell lines, produce IL-8 in response to a wide variety of proinflammatory stimuli such as exposure to IL-1, TNF, LPS and viruses. IL-8 has a wide range of other proinflammatory effects. It is a potent chemoattractant for neutrophils and causes degranulation of neutrophil specific granules and azurophilic granules. IL-8 induces expression of the cell adhesion molecules CD11/CD18 and enhances the adherence of neutrophils to endothelial cells and subendothelial matrix proteins. Besides neutrophils, IL-8 is also chemotactic for basophils, T cells and eosinophils. IL-8 has been reported to be a co-mitogen for keratinocytes and was also shown to be an autocrine growth factor for melanoma cells. IL-8 was also reported to be angiogenic both in vivo and in vitro.