Cytokines & Chemokines

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, which also includes IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and shares a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, which also includes IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and shares a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, which also includes IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and shares a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

Interleukin-18 binding protein, also known as IL-18BP and tadekinig-alfa, is a secreted glycoprotein that contains an Ig-like C2-type domain. It is expressed in heart, lung, placenta and spleen. IL-18BP functions as an inhibitor of the proinflammatory cytokine IL-18. It binds to IL-18, prevents the binding of IL-18 to its receptor, and thus blocks IL-18-induced IFN-gamma production. The complete Ig domain has been shown to mediate the binding and neutralizing properties. IFN-gamma is able to upregulate the expression of IL-18BP, indicating that IL-18 activity is regulated by a feedback mechanism through IL-18BP.

Interleukin-18 binding protein, also known as IL-18BP and tadekinig-alfa, is a secreted glycoprotein that contains an Ig-like C2-type domain. It is expressed in heart, lung, placenta and spleen. IL-18BP functions as an inhibitor of the proinflammatory cytokine IL-18. It binds to IL-18, prevents the binding of IL-18 to its receptor, and thus blocks IL-18-induced IFN-gamma production. The complete Ig domain has been shown to mediate the binding and neutralizing properties. IFN-gamma is able to upregulate the expression of IL-18BP, indicating that IL-18 activity is regulated by a feedback mechanism through IL-18BP.

Interleukin-18 binding protein, also known as IL-18BP and tadekinig-alfa, is a secreted glycoprotein that contains an Ig-like C2-type domain. It is expressed in heart, lung, placenta and spleen. IL-18BP functions as an inhibitor of the proinflammatory cytokine IL-18. It binds to IL-18, prevents the binding of IL-18 to its receptor, and thus blocks IL-18-induced IFN-gamma production. The complete Ig domain has been shown to mediate the binding and neutralizing properties. IFN-gamma is able to upregulate the expression of IL-18BP, indicating that IL-18 activity is regulated by a feedback mechanism through IL-18BP.