IL8 GST
Escherichia Coli.
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
Sterile Filtered clear solution.
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Description
Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.
Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.
Product Specs
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
Escherichia Coli.
Product Science Overview
Interleukin-8 (IL-8), also known as CXCL8, is a pro-inflammatory chemokine belonging to the CXC subfamily. It plays a crucial role in the immune response by acting as a chemoattractant for neutrophils and other immune cells. IL-8 is produced by various cell types, including macrophages, epithelial cells, and endothelial cells, in response to inflammatory stimuli .
IL-8 is a 72 amino acid protein with a molecular weight of approximately 8.4 kDa . It contains an ELR motif (Glu-Leu-Arg) near its N-terminus, which is essential for its angiogenic properties . The protein signals through the CXCR1 and CXCR2 receptors, which are expressed on the surface of target cells .
Recombinant IL-8 (1-72) is typically produced using an expression system in Escherichia coli (E. coli). The gene encoding IL-8 is cloned into a plasmid vector, which is then introduced into E. coli cells. The bacteria are cultured, and the recombinant protein is expressed and purified. The GST (Glutathione S-transferase) tag is often used to facilitate the purification process, as it allows for affinity purification using glutathione agarose beads .
IL-8 functions as a potent chemoattractant and activator of neutrophils. It induces the migration of neutrophils to sites of infection or injury, where they can perform their immune functions. Additionally, IL-8 has angiogenic properties, promoting the formation of new blood vessels, which is important in wound healing and tumor growth .
