Cytokines & Chemokines

Mouse interleukin 13 (mIL-13) is a pleiotropic cytokine produced by activated Th2 cells. IL-13 induces B cell proliferation and immunoglobin production. It contains a four helical bundle with two internal disulfide bonds. Mouse IL13 shares 58% sequence identity with human protein and exhibits cross-species activity. IL13 signals via receptor IL13R (type2, IL4R) and activates STAT-6. IL13 initially binds IL-13Rα1 with low affinity and triggers association of IL4Rα, generating a high affinity heterodimeric receptor IL13R and eliciting downstream signals. IL13 also binds IL-13Rα2 with high affinity, which plays a role in a negative feedback system of IL13 signaling. IL13 is an important mediator of allergic inflammation and disease.

Interleukin-17F (IL-17F) exists in a disulfide-linked heterodimer that belongs to the IL-17 family. IL-17F is expressed in activated, but not resting, CD4+ T-cells and activated monocytes. Mouse and human IL-17F share 55% sequence identity.IL-17F has been shown to stimulate the production of several other cytokines, including IL-6, IL-8, and granulocyte colony-stimulating factor. IL-17F can regulate cartilage matrix turnover and stimulates PBMC and T-cell proliferation. IL-17F is also found to inhibit the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. Defects in IL-17F are the cause of familial candidiasis type 6 (CANDF6).

Interleukin-4 (IL-4) is a pleiotropic cytokine that regulates diverse T and B cell responses including cell proliferation, survival and gene expression. IL-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of naive CD4+ T cells into helper Th2 cells, characterized by their cytokine-secretion profile that includes secretion of IL-4, IL-5, IL-6, IL-10, and IL-13, which favor a humoral immune response. Another dominant function of IL-4 is the regulation of immunoglobulin class switching to the IgG1 and IgE isotypes. Excessive IL-4 production by Th2 cells has been associated with elevated IgE production and allergic response.

Mouse Interleukin-4(IL-4) is a monomeric, Th2 cytokine that shows pleiotropic effects during immune responses. It is a glycosylated polypeptide that contains three intrachain disulfide bridges and adopts a bundled four α-helix structure. IL-4 exerts its effects through two receptor complexes, Participates in at least several B-cell activation processes as well as of other cell types. IL-4 is primarily expressed by Th2-biased CD4+T cells, mast cells, basophils, and eosinophils. It promotes cell proliferation, survival, and immunoglobulin class switch to IgG1 and IgE in mouse B cells, acquisition of the Th2 phenotype by na?ve CD4+T cells, priming and chemotaxis of mast cells, eosinophils, and basophils, and the proliferation and activation of epithelial cells. IL-4 plays a dominant role in the development of allergic inflammation and asthma. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes.

Mouse interleukin 13 (mIL-13) is a pleiotropic cytokine produced by activated Th2 cells. IL-13 induces B cell proliferation and immunoglobin production. It contains a four helical bundle with two internal disulfide bonds. Mouse IL13 shares 58% sequence identity with human protein and exhibits cross-species activity. IL13 signals via receptor IL13R (type2, IL4R) and activates STAT-6. IL13 initially binds IL-13Rα1 with low affinity and triggers association of IL4Rα, generating a high affinity heterodimeric receptor IL13R and eliciting downstream signals. IL13 also binds IL-13Rα2 with high affinity, which plays a role in a negative feedback system of IL13 signaling. IL13 is an important mediator of allergic inflammation and disease.

Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.

Interleukin-6 (IL-6) is a multifunctional α-helical cytokine that regulates cell growth and differentiation of various tissues, which is known particularly for its role in the immune response and acute phase reactions. IL-6 protein is secreted by a variety of cell types including T cells and macrophages as phosphorylated and variably glycosylated molecule. It exerts actions through the its heterodimeric receptor composed of IL-6R that lacks the tyrosine/kinase domain and binds IL-6 with low affinity, and ubiquitously expressed glycoprotein 130 (gp130) that binds the IL-6. IL-6R complex with high affinity and thus transduces signals. IL-6 is also involved in hematopoiesis, bone metabolism, and cancer progression, and has been defined an essential role in directing transition from innate to acquired immunity.