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Description: Human IL-8, also called neutrophil attractant/activating protein (NAP-1), monocyte derived neutrophil activating peptide (MONAP), monocyte derived neutrophil activating factor (ANF), monocyte derived neutrophil chemotactic factor (MDNCF), and neutophil activating factor (NAF), is a ~6-8 kDa factor produced by variety types of cells including monocytes, lymphocytes, granulocytes, fibroblasts and endothelial cells. IL-8 is an inflammatory cytokine which functions as a neutrophil chemoatractant and activating factor. It also attracts basophils and a subpopulation of lymphocytes.
Applications Reported: Recombinant human IL-8 is biologically active.
Applications Tested: This recombinant human IL-8 has been tested in bioassays for chemoattractant activity, with maximal activity between 10-100 ng/mL.
Source: E. coli expressed amino acids Ser 28-Ser 99 of human IL-8 accession # NM_000584.
Bioactivity: Measured by chemotaxis assay of human peripheral blood neutrophils. Maximal chemoattractant activity was observed between 10-100 ng/mL.
Endotoxin: Less than 0.01 ng/ug cytokine as determined by the LAL assay. Purity: >98% as determined by SDS-PAGE.
Molecular Weight: The protein is not methionylated at the N-terminal and has a predicted molecular mass of 8,386. The DTT reduced protein migrates as an 8 kDa polypeptide and the non-reduced polypeptide migrates as a 9 kDa polypeptide on SDS-PAGE.
Storage and handling: For best recovery, quick-spin vial prior to opening. Use in a sterile environment.
Purity: Greater than 90%, as determined by SDS-PAGE.
Aggregation: Less than 10%, as determined by HPLC.
Filtration: 0.2 µm post-manufacturing filtered.
Interleukin 8 (IL-8, CXCL8) is a 72 amino acid pro-inflammatory factor which belongs to the CXC subfamily of chemokines, and are bound by the cell surface receptors IL-8RA and IL-8RB. IL-8 functions as a chemoattractant and potent angiogenic factor. The expression and secretion of IL-8 can be induced by diverse inflammatory stimuli in many cells, including macrophages and endothelial cells. In endothelial cells, IL-8 is present in storage vesicles called Weibel-Palade bodies. IL-8, first isolated from osteosarcoma cells, contains the ELR-motif (N-terminal Glu-Leu-Arg amino acid sequence) and signals through the CXCR1 and CXCR2 receptors. Previous nomenclature for IL-8 includes neutrophil activating protein 1 (NAP-1), granulocyte chemotactic protein 1 (GCP-1), monocyte-derived neutrophil-activating peptide (MONAP) and protein 3-10C. IL-8 and ten other members of the CXC chemokine gene family form a chemokine gene cluster in a region mapped to chromosome 4q. Cancer studies have demonstrated a role for IL-8 in the angiogenesis and growth of tumours, and IL-8 is believed to play a role in the pathogenesis of bronchiolitis, a common respiratory tract disease caused by viral infection.
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