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O9635

Sigma-Aldrich

Oncostatin M human

BioReagent, ≥97% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture

Synonym(s):

OSM

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in E. coli

product line

BioReagent

Assay

≥97% (SDS-PAGE)

form

lyophilized powder

potency

≤1.000 ng/mL ED50

mol wt

~22 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

technique(s)

cell culture | mammalian: suitable

impurities

endotoxin, tested

color

white

solubility

soluble 0.100 mL, clear, colorless (Solvent-PBS + 0.1% BSA)

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... OSM(5008)

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General description

Oncostatin M (OSM) is produced by activated T cells, monocytes and Kaposi′s sarcoma cells. OSM shares several structural and functional characteristics with leukemia inhibitory factor (LIF), interleukin-6 (IL-6), and ciliary neurotrophic factor (CNTF).

Application

Human oncostatin-M has been used to stimulate bovine full-depth cartilage explants. It has also been used to culture embryonic stem cells in standard minimum essential medium-α.

Biochem/physiol Actions

Oncostatin M (OSM) is a growth and differentiation factor that participates in the regulation of neurogenesis, osteogenesis and hematopoiesis. It can exert both stimulatory and inhibitory effects on cell proliferation. OSM 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. interleukin-6 (IL-6), granulocyte-macrophage colony-stimulating factor (GM-CSF) and granulocyte-colony-stimulating factor (G-CSF)] from endothelial cells.
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 in 10 mM acetic acid, containing 50 μg of bovine serum albumin per 1 μg of cytokine.

Analysis Note

The proliferative activity of human oncostatin M is tested in culture by using a human erythroleukemic cell line, TF-1.

Storage Class Code

4.1B - Flammable solid hazardous materials

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Oncostatin M and leukemia inhibitory factor do not use the same functional receptor in mice.
Ichihara M
Blood (1997)
Differential Diagnosis by Laboratory Medicine: A Quick Reference for Physicians null
The Effect of Protease Inhibitors on the Induction of Osteoarthritis-Related Biomarkers in Bovine Full-Depth Cartilage Explants
Yi He
PLoS ONE (2015)
Pulmonary expression of oncostatin M (OSM) promotes inducible BALT formation independently of IL-6, despite a role for IL-6 in OSM-driven pulmonary inflammation.
Botelho FM
Journal of Immunology (2013)
Oncostatin M stimulates the growth of dermal fibroblasts via a mitogen-activated protein kinase-dependent pathway.
Ihn H and Tamaki K
Journal of Immunology (2000)

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