Interleukin-8, also known as CXCL8, a chemokine with a characteristic CXC amino acid sequence that was originally investigated for its leukocyte chemotactic activity, is now recognized to have tumorogenic and proangiogenic properties. In response to inflammatory stimuli, this cytokine is produced by a range of cell types, including monocytes/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, and various tumor cell lines. IL-8 is highly produced and secreted in human gliomas both in vitro and in vivo, suggesting that it is important to glial tumor neovascularity and progression. High levels of IL-8 correlate with histologic grades in glial neoplasms, but the most malignant kind, glioblastoma, exhibits the greatest expression of pseudopalisading cells around necrosis, suggesting that hypoxia/anoxia may drive gene expression. Interleukin (IL)-8/CXCL8 is a potent neutrophil chemotactic factor. Various types of cells have been shown to produce a significant amount of IL-8/CXCL8 in response to a variety of stimuli, including proinflammatory cytokines, microorganisms and their products, and environmental changes such as hypoxia, reperfusion, and hyperoxia. IL-8/CXCL8 has been shown in numerous studies to be a key participant in neutrophil-mediated acute inflammation, as it has a powerful effect on neutrophils. However, several lines of evidence indicate that IL-8/CXCL8 has a variety of effects on a wide range of cell types, including lymphocytes, monocytes, endothelial cells, and fibroblasts, in addition to neutrophils. The identification of these biological activities implies that IL-8/CXCL8 has critical functions in a number of disease processes including chronic inflammation and cancer. For example, the anti-inflammatory cytokine IL-8 has been linked to tumor angiogenesis, metastasis, and poor outcome in breast cancer. IL-8 may present a novel therapeutic target for estrogen driven breast carcinogenesis and tumor progression. Human IL-8/CXCL8 Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.
The 72 amino acid residue form (Ser 28-Ser 99) of mature human IL8 (NP_000575.1) was expressed and purified.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
8.5 kDa
AP Mol Mass:
12 kDa
Formulation:
Lyophilized from sterile 100mM NaCl, 50mM Tris, pH 7.5
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
