Human Oncostatin M/OSM Alexa Fluor® 488-conjugated Antibody Summary
Accession # P13725
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
Background: Oncostatin M/OSM
Oncostatin M (OSM) is a cytokine originally isolated from medium conditioned by PMA-treated U-937 human histiocytic leukemia cells based on its ability to inhibit growth of A375 melanoma cells. The human OSM cDNA encodes a 252 amino acid pre-pro-OSM polypeptide with a 25 residue hydrophobic signal peptide and a hydrophilic C-terminal domain that are proteolytically processed to generate the 196 residue mature form of OSM. Although both mature and pro-OSM are equally active in radio-receptor assays, the mature OSM is 5- to 60-fold more active in growth inhibition assays. Thus, proteolytic processing of the pro-OSM peptide may be important in regulating the in vivo activities of OSM.
OSM is a pleiotropic cytokine that initiates its biological activities by binding to specific cell surface receptors. The biological activity of human OSM is mediated either by the LIF/OSM receptor complex composed of gp130 and LIF R alpha or by a human OSM specific receptor composed of gp130 and OSM R alpha. The gp130, a signal transducing component ( beta subunit) of the IL-6, LIF and CNTF receptor complexes, was identified as a low-affinity OSM receptor that does not transduce OSM signals. The low affinity LIF receptor (LIF R, a gp130-related protein) has been identified to be a component of a high-affinity OSM receptor that will transduce OSM signals. Besides its growth inhibitory activities on human A375 melanoma and mouse M1 myeloid leukemic cells, as well as on other solid tumor cells, OSM also has growth stimulatory activities on normal fibroblasts, AIDS-Kaposi’s sarcoma cells, and a human erythroleukemia cell line, TF-1. Other OSM-mediated activities reported to date include: stimulation of plasminogen activator activity in cultured bovine aortic endothelial cells; regulation of IL-6 expression in human endothelial cells; and stimulation of LDL uptake and up-regulation of cell surface LDL receptors in HepG2 cells.
Product Specific Notices
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
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