Recombinant Human Oncostatin M (HEK-293-expressed), CF Summary
Details of Functionality
Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 0.05-0.3 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human Oncostatin M/OSM protein Ala26-Arg221
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
22 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
27-35 kDa, reducing conditions
Publications
Read Publication using 8475-OM/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE with silver staining
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Oncostatin M (HEK-293-expressed), CF
MGC20461
oncostatin M
oncostatin-M
OSM
Background
Oncostatin M (OSM) is an approximately 30 KDa secreted cytokine belonging to the Interleukin-6 family. Like other members of the IL-6 family such as IL-11, CNTF, and Cardiotrophin-1, OSM plays crucial roles in inflammation, neuroprotection, hematopoiesis, metabolism and development (1). The human OSM cDNA encodes a 252 amino acid (aa) prepro protein with a signal peptide and a hydrophilic Cterminal domain that are proteolytically processed to generate the 195 aa mature form (2). Although both mature and pro-OSM are equally active in radioreceptor assays, the mature OSM is 5 to 60 fold more active in growth inhibition assays (3). Thus, proteolytic processing of the pro-OSM peptide may be important in regulating the in vivo activities of OSM (3). Cytokines of the IL-6 family share a common receptor subunit, gp130, which allows intracellular signal transduction. In contrast to other cytokines, OSM binds gp130 with very low affinity and has little to no biological activity unless a second receptor chain is recruited (4). The OSM-gp130 complex recruits either LIF R alpha, or OSM R beta to form the OSM receptor type I or OSM receptor type II respectively (5). Among multiples roles, OSM has been reported to modulate tumor cell and epithelial cell growth (6, 7). An axis involving OSM, CD40 Ligand and OSM receptor described as an antiviral and immunostimulatory system is disrupted in patients liver showing hepatitis C infection (8). Human OSM shares 45% aa sequence homology with mouse and rat OSM.
Richards, C.D. (2013) ISRN Inflamm. 2013:512103.
Malik, N. et al. (1989) Mol. Cel. Biol. 9:2847.
Linsley, P.S. et al. (1990) Mol. Cel. Biol. 10:1882.
Liu, J. et al. (1994) Cytokine 6:272.
Mosley, B. et al. (1996) J. Biol. Chem. 271:32635.
Grant, S.L. et al. (2001) Growth Factors 19:153.
Chollangi, S. et al. (2012) J. Biol. Chem. 287:32848.
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