Oncostatin M (OSM), LIF, G-CSF, IL-6, and CNTF are structurally related members of the same cytokine family sharing similarities in their primary amino acid sequences, predicted secondary structure, and receptor components. OSM is a growth-regulating cytokine, affecting a number of tumor and normal cells. This material was first identified by its ability to inhibit the growth of A375 melanoma cells and other human tumor cells, but not inhibit the growth of normal human fibroblasts. It acts synergistically with TGF β1 to inhibit the proliferation of tumor cells like A375 melanoma cells. It induces an increase in LDL receptor expression and LDL uptake by hepatoma cells. OSM activates synovial fibroblast-like cells to produce urokinase type plasminogen activator. OSM is secreted by macrophages and activated T lymphocytes.
Physical form
Lyophilized from a 0.2 μm filtered solution of 1x PBS.
Analysis Note
The activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (humanerythroleukemic indicator cell line)
Legal Information
HumanKine is a registered trademark of Proteintech Group, Inc. and Humanzyme, Inc
Cellular and molecular life sciences : CMLS, 71(10), 1907-1916 (2013-12-11)
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The American journal of pathology, 181(5), 1782-1795 (2012-09-18)
Primary bone tumors, osteosarcomas and chondrosarcomas, derive from mesenchymal stem cells committed into osteoblasts and chondrocytes; in Ewing sarcomas (ESs), the oncogenic fusion protein EWS-FLI1 prevents mesenchymal differentiation and induces neuroectodermic features. Oncostatin M (OSM) is a cytokine from the
Cardiomyocyte remodeling, which includes partial dedifferentiation of cardiomyocytes, is a process that occurs during both acute and chronic disease processes. Here, we demonstrate that oncostatin M (OSM) is a major mediator of cardiomyocyte dedifferentiation and remodeling during acute myocardial infarction
Proceedings of the National Academy of Sciences of the United States of America, 110(42), 16975-16980 (2013-10-02)
The activation of STAT3 by tyrosine phosphorylation, essential for normal development and for a normal inflammatory response to invading pathogens, is kept in check by negative regulators. Abnormal constitutive activation of STAT3, which contributes to the pathology of cancer and
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