Rat IL-11 Protein, Mouse IgG2a Fc Tag, low endotoxin (MALS verified)

IL-11 (Interleukin 11) is a pleiotropic cytokine in the IL-6 family, which also includes LIF, CNTF, Oncostatin M, Cardiotrophin-1, IL-27 and IL-31. In humans, IL-11 was also independently discovered as an adipogenesis inhibitory factor (AGIF). The human IL-11 cD encodes a 199 amino acid (aa) precursor, which generates a 178-aa, 19-kDa mature unglycosylated protein. Mature human IL-11 shares 88%, 88%, and 96% aa sequence identity with mouse, rat and canine IL-11, respectively. IL-11 is secreted by osteoblasts, synoviocytes, fibroblasts, chondrocytes, intestinal myofibroblasts, and trophoblasts, among other cell types. It is found in the plasma mainly during inflammation, such as that associated with viral infection, cancer, or inflammatory arthritis, and is traditionally considered primarily anti-inflammatory. It stimulates hematopoiesis and thrombopoiesis, regulates macrophage differentiation, and confers mucosal protection in the intestine. It has also been found to enhance T cell polarization toward Th2, promote B cell IgG production, increase osteoclast bone resorption, protect endothelial cells from oxidative stress, and regulate epithelial proliferation and apoptosis. IL-11 synergizes with several other cytokines to produce these effects, and its effects overlap with those of IL-6. IL-11 receptor activation requires formation of a complex of two IL-11 molecules with two molecules of the ligand-binding IL-11Rα and two molecules of the ubiquitously expressed signaling subunit gp130. A soluble form of IL-11Rα can bind IL-11 and either form a signaling complex with gp130 on the cell surface, or inhibit signaling mediated by the cell‑surface IL‑11Rα/gp130 complex.