IL-17E is a disulfide-linked homodimer of two 145 amino acid polypeptide chains. It belongs to the IL-17 family of structurally-related cytokines that share a highly conserved C-terminal region, but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17E stimulated secretion of IL-8, and induces activation of the transcription factor NF-B in cells that express the IL-17BR receptor. Recombinant human IL-17E is a 33.8 kDa disulfide-linked homodimer of two 146 amino acid polypeptide chains.
IL-17E is a disulfide-linked homodimer of two 145 amino acid polypeptide chains. It belongs to the IL-17 family of structurally-related cytokines that share a highly conserved C-terminal region, but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17E stimulated secretion of IL-8, and induces activation of the transcription factor NF-B in cells that express the IL-17BR receptor. Recombinant human IL-17E is a 33.8 kDa disulfide-linked homodimer of two 146 amino acid polypeptide chains.
IL-17E is a disulfide-linked homodimer of two 145 amino acid polypeptide chains.
Interleukin-17E Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2x145 amino acids (with an N-terminal Methionine for each chain total aa for each chain 146) and having a total predicted molecular mass of 33.7kDa.
The IL-25 Human is purified by proprietary chromatographic techniques.
IL-25 also called IL-17E cytokine has a sequence similarity with IL17. IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.
