|94853||Human Interleukin-8 (hIL-8)||
The purity of recombinant hIL-8 was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant hIL-8 and staining overnight with Coomassie Blue.Learn more about how we get our images
The upregulation of CD11b expression on primary human neutrophils with increasing concentrations of hIL-8 was assessed. After 20 minute treatment with hIL-8, cells were stained with an anti-CD11b antibody and analyzed by flow cytometry.Learn more about how we get our images
Recombinant human IL-8 (hIL-8) Ser28-Ser99 (Accession #NM_000584) was produced in E.coli at Cell Signaling Technology.
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hIL-8. All lots are greater than 98% pure.
Recombinant hIL-8 does not have a Met on the amino terminus and has a calculated MW of 8,386. DTT-reduced and non-reduced protein migrate as 8 kDa polypeptides. The expected amino-terminal SAKEL of recombinant hIL-8 was verified by amino acid sequencing.
The bioactivity of recombinant hIL-8 was determined by upregulation of CD11b expression on primary human neutrophils. The ED50 of each lot is between 1-5 ng/ml.
Less than 0.01 ng endotoxin/1 μg hIL-8.
SC: A 0.22 μm filtered solution of 0.25 mg/ml hIL-8 in PBS, pH 7.2 containing 20 μg BSA per 1 μg hIL-8.
LC: A 0.22 μm filtered solution of 0.33 mg/ml hIL-8 in PBS, pH 7.2 containing 20 μg BSA per 1 μg hIL-8.
SF: A 0.22 μm filtered solution of 0.25 mg/ml hIL-8 in PBS, pH 7.2.
LF: A 0.22 μm filtered solution of 0.33 mg/ml hIL-8 in PBS, pH 7.2.
Stable at 4°C for 1 year after receipt. Maintain sterility. Do not store frozen.
The prototypical CXC chemokine, IL-8, is best known for effects on neutrophils, specifically its ability to act as a chemoattractant and activate degranulation and respiratory burst (1,2,3).
IL-8 is produced by a number of cell types including monocytes, T cells, neutrophils, fibroblasts, endothelial cells, and others (1). In addition to its effects on neutrophils, IL-8 promotes angiogenesis, inhibits endothelial cell apoptosis, and promotes the proliferation of melanoma cells in an autocrine fashion (1). As a result, IL-8 may be a contributing factor to the development of certain cancers (1,2). There are two distinct receptors for IL-8, CXCR1 and CXCR2; both are G protein-coupled receptors (1). Ligand binding induces Ca2+ mobilization and activates the PI3K, PKC, Rho, and Rac pathways (1,3).
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