Human IL-11 Biotinylated Antibody

Interleukin 11 is a pleiotropic cytokine that was originally detected in the conditioned medium of an IL-1 alpha-stimulated primate bone marrow stromal cell line (PU-34) as a mitogen for the IL-6-responsive murine plasmacytoma cell line T1165. IL-11 was also independently discovered as an adipogenesis inhibitory factor (AGIF). The human IL-11 cDNA encodes a 199 amino acid residue precursor polypeptide with a 21 amino acid residue hydrophobic signal that is processed proteolytically to generate the 178 amino acid residue mature protein. IL-11 contains no cysteine residues or potential glycosylation sites.

IL-11 has multiple effects on both hematopoietic and nonhematopoietic cells. Many of the biological effects described for IL-11 overlap those for IL-6. In vitro, IL-11 can synergize with IL-3, IL-4 and SCF to shorten the G₀ period of early hematopoietic progenitors. IL-11 also enhances the IL-3-dependent megakaryocyte colony formation. IL-11 has been found to stimulate the T cell dependent development of specific immunoglobulin-secreting B cell. IL-11, in the presence of IL-3 or SCF, has also been shown to stimulate erythropoiesis. Among nonhematopoietic cell populations, IL-11, like IL-6 and LIF, can stimulate the synthesis of hepatic acute-phase proteins. Consistent with the in vitro functions of IL‑11, in vivo administration of rhIL-11 in normal mice was found to enhance the generation of Ig producing cells and platelets, and to increase the cycling rates of bone marrow-derived CFU-GM, BFU-E, and CFU-GEMM progenitors.

IL-11 exerts its biological activities through binding to a specific high-affinity receptor having an apparent molecular mass of 150 kDa. Although the IL-11 binding subunit of the receptor complex has not yet been cloned, evidence suggests that, similar to IL-6, leukemia inhibitory factor, oncostatin M, and ciliary neurotrophic factor, IL-11 utilizes the IL-6 signal transducer, gp130, for signal transduction.