Recombinant Human IL-10 (Animal-Free)

IL-10 was first described as a cytokine that is produced by T helper 2 (Th2) cell clones. It inhibits IFN-γ synthesis in Th1 cells, and therefore it was initially called cytokine synthesis inhibiting factor (CSIF).  Macrophages are the main source of IL-10 and its secretion can be stimulated by endotoxin (via Toll-like receptor 4, NF-kB dependent), tumor necrosis factor TNF-α (via TNF receptor p55, NF-κB-dependent), catecholamines, and IL-1. IL-10 controls inflammatory processes by suppressing the expression of proinflammatory cytokines, chemokines, adhesion molecules as well as antigen-presenting and costimulatory molecules in monocytes/macrophages, neutrophils, and T cells. IL-10 inhibits the production of proinflammatory mediators by monocytes and macrophages such as endotoxin- and IFNγ-induced release of IL-1α, IL-6, IL-8, G-CSF, GM-CSF, and TNF-α. In addition, it enhances the production of anti-inflammatory mediators such as IL-1RA and soluble TNF-α receptors. IL-10 inhibits the capacity of monocytes and macrophages to present antigen to T cells. This is realized by downregulation of constitutive and IFNγ-induced cell surface levels of MHC class II, of costimulatory molecules such as CD86 and of some adhesion molecules such as CD58. IL-10 belongs to a family of nine members: IL-10, IL-19, IL-20, IL-22, IL-24, IL-26, and the more distantly related IL-28A, IL-28B, and IL-29. This family of cytokines emerged before the adaptive immune response.