Recombinant dog IL-8 protein is a Dog Full Length protein, in the 23 to 101 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS, HPLC.
View Alternative Names
IL8, CXCL8, Interleukin-8, IL-8, C-X-C motif chemokine 8, Chemokine (C-X-C motif) ligand 8
Complementary Products
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
IL-8 functions as a chemoattractant for neutrophils and lymphocytes facilitating their movement towards the site of infection or injury. It does not form part of a larger protein complex but operates individually to enhance immune cell migration. IL-8 possesses unique binding motifs allowing it to interact with specific receptors namely CXCR1 and CXCR2 on target cells. This binding triggers cellular responses leading to effective immune surveillance and response to inflammatory stimuli.
Pathways
IL-8 operates within important inflammatory and immune response pathways. It forms a part of the NF-κB signaling cascade which activates in response to stress signals promoting the expression of other inflammatory mediators. Additionally it engages in the mitogen-activated protein kinase (MAPK) pathway influencing cellular responses such as proliferation and differentiation. The interaction of IL-8 with these pathways highlights its role in modulating immune responses and highlights its interaction with other proteins such as TNF-α and IL-1β.
Specifications
Form
Lyophilized
Additional notes
ab200269 is > 95 % pure as assessed by SDS-PAGE and HPLC analyses.
General info
Function
Chemotactic factor that mediates inflammatory response by attracting neutrophils, basophils, and T-cells to clear pathogens and protect the host from infection. Also plays an important role in neutrophil activation. Released in response to an inflammatory stimulus, exerts its effect by binding to the G-protein-coupled receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes and endothelial cells. G-protein heterotrimer (alpha, beta, gamma subunits) constitutively binds to CXCR1/CXCR2 receptor and activation by IL8 leads to beta and gamma subunits release from Galpha (GNAI2 in neutrophils) and activation of several downstream signaling pathways including PI3K and MAPK pathways.
Sequence similarities
Belongs to the intercrine alpha (chemokine CxC) family.
Post-translational modifications
Citrullination at Arg-27 prevents proteolysis, and dampens tissue inflammation, it also enhances leukocytosis, possibly through impaired chemokine clearance from the blood circulation.
Target data
Product promise
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