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A DNA sequence encoding the human Oncostatin M protein sequence (containing the signal peptide sequence, the C-terminal propeptide sequence, and the mature Oncostatin M sequence) was expressed in modified human 293 cells.

Oncostatin M (OSM) is a member of the IL-6 family of cytokines, which includes IL-6, IL-11, LIF, ciliary neurotrophic factor (CNTF), cardiotrophin-1 (CT-1) and cardiotropin-like cytokine. Structurally, OSM is a 196 amino acid monomeric glycoprotein with two potential N-linked glycosylation sites and five cysteine residues, four of which form disulfide bonds. OSM is a growth regulator, in particular with respect to human fibroblasts and vascular smooth muscle cells. Additionally, OSM stimulates the production of IL-6, G-CSF and GM-CSF from endothelial cells and hence plays a role in hematopoiesis and myelopoiesis. OSM mediates the differentiation of megakaryocytes, as well as the regulation of cholesterol metabolism, bone formation and wound healing. OSM has also been shown to play a role in both pro and anti-inflammatory actions. The expression of OSM from activated T-cells and macrophages is implicated in the initiation phase of an inflammatory response. OSM induces inflammation and destruction of mouse joints in vivo and an elevated level of OSM is present in joints of patients with rheumatoid arthritis. OSM may also be involved in multiple sclerosis (MS), as it is present in MS lesions in microglial cells and infiltrating leukocytes. Conversely, mice with myelin antigen induced encephalomyelitis exhibit symptom reduction when treated with human OSM. The actions of OSM are exerted through binding to a heterodimeric membrane receptor composed of either the OSM receptor or LIF receptor subunit associated with the gp 130-receptor chain.