Oncostatin M Recombinant Protein

Oncostatin M (OSM) is a growth and differentiation factor that participates in the regulation of neurogenesis, osteogenesis and hematopoiesis. Produced by activated T cells, monocytes and Kaposi’s sarcoma cells, OSM can exert both stimulatory and inhibitory effects on cell proliferation. It stimulates the proliferation of fibroblasts, smooth muscle cells and Kaposi’s sarcoma cells, but inhibits the growth of some normal and tumor cell lines. It also promotes cytokine release (e.g. IL-6, GM-CSF and G-CSF) from endothelial cells, and enhances the expression of low-density lipoprotein receptors in hepatoma cells. OSM shares several structural and functional characteristics with LIF, IL-6, and CNTF. Human OSM is active on murine cells. The human OSM gene encodes for a 252 amino acid polypeptide, containing 25 amino acid signal sequence for secretion and a 227 precursor protein. Proteolytic processing of this precursor removes an 18 amino acid C-terminal peptide, and generates the mature OSM form. Recombinant Human Oncostatin M (196 a.a.) is a HEK293 cell-derived, 196 amino-acid length glycoprotein that has a calculated theoretical molecular weight of 22.2 kDa, but migrates at an apparent molecular weight of 32-34 kDa by SDS-PAGE analysis under reducing conditions due to glycosylation.

The recombinant protein is stable for at least 2 years from date of receipt at -20˚ C. Reconstituted protein is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚ C. As with any protein, exposing the recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.