Oncostatin M (OSM) (AA 26-221) (Active) Protein

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Proteinname
  • OSM
  • OncoM
  • oncostatin M
  • oncostatin M-like
  • oncostatin-M-like
  • OSM
  • Osm
  • LOC100342491
  • LOC100152038
Proteineigenschaft
AA 26-221
6
3
3
3
2
2
2
2
2
1
1
1
1
1
1
1
1
1
Spezies
Human
59
9
5
1
Quelle
Escherichia coli (E. coli)
48
6
3
3
1
1
1
1
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Applikation
Flow Cytometry (FACS)
Optionen
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Reinheit > 95 % , as determined by Coomassie stained SDS-PAGE.
Sterilität 0.22 μm filtered
Endotoxin-Niveau

Less than 0.01 ng per μg cytokine as determined by the LAL method.

Hintergrund Human oncostatin M (OSM) was initially isolated from supernatant of U937 cells treated with PMA. It was identified by its property to inhibit the proliferation of A375 melanoma cells and other human tumor cells. Bioinformatic homology analysis reveals that OSM has a similar composition and structure to LIF, G-CSF, and IL-6. OSM and LIF are located on human chromosome 22, and additional evidence suggests that these genes were derived by duplication of a common ancestral gene. In fact, many of its biological functions are shared with LIF. OSM binds two types of OSM receptor (OSMR) complexes. The type I receptor complex is composed of gp130 (IL-6 signal transducer) and LIF receptor β (LIFRβ) subunits. The type II receptor is constituted by the gp130 receptor and the OSMR β-chain. OSM also shares the OSMRβ-chain with the IL-31 receptor complex. The OSMRβ subunit is expressed by fibroblast, endothelial, hepatic, lung, and hematopoietic cells. The proinflammatory properties of OSM have been reported in skin, adipose tissue, lung, heart, and liver tissues. OSM triggers acute phase protein synthesis in hepatocytes. OSM is a potent inhibitor of keratinocyte proliferation and decreases the expression of both early and late keratinocyte differentiation markers. OSM transcripts are elevated in skin from psoriasis and atopic dermatitis patients, as compared with healthy skin. OSM and its receptor complexes play a key role in cutaneous inflammatory responses. In addition, OSM expression is increased in colonic biopsies of patients with active inflammatory bowel disease.
Molekulargewicht The 196 amino acid recombinant protein has a predicted molecular mass of approximately 22.1 kDa. The DTT-reduced and non-reduced protein migrate at approximately 20 kDa and 22 kDa, respectively, by SDS-PAGE. The predicted N-terminal amino acid is Ala.
Forschungsgebiet Immunology, Innate Immunity, Cytokines, Signaling, Receptors
Pathways JAK-STAT Signalweg, Negative Regulation of Hormone Secretion
Applikationshinweise Optimal working dilution should be determined by the investigator.
Kommentare

Biological activity: ED50 = 0.5 - 2.5 ng/ml, corresponding to a specific activity of 0.4 - 2.0 x 106

Beschränkungen Nur für Forschungszwecke einsetzbar
Format Liquid
Rekonstitution For maximum results, quick spin vial prior to opening. Stock solutions can also be prepared at 50 - 100 μg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2 - 1 % BSA or HSA and stored in working aliquots at -20 °C to -70 °C.
Buffer 0.22 μm filtered protein solution is in <20 % ACN, 0.1 % TFA.
Handhabung Avoid repeated freeze/thaw cycles.
Lagerung -20 °C
Informationen zur Lagerung Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for six months, or at -70°C for one year.
Allgemeine Veröffentlichungen Beigel, Friedrich, Probst, Sotlar, Göke, Diegelmann, Brand: "Oncostatin M mediates STAT3-dependent intestinal epithelial restitution via increased cell proliferation, decreased apoptosis and upregulation of SERPIN family members." in: PLoS ONE, Vol. 9, Issue 4, pp. e93498, 2014 (PubMed).

Schnittker, Kwofie, Ashkar, Trigatti, Richards: "Oncostatin M and TLR-4 ligand synergize to induce MCP-1, IL-6, and VEGF in human aortic adventitial fibroblasts and smooth muscle cells." in: Mediators of inflammation, Vol. 2013, pp. 317503, 2013 (PubMed).

Boniface, Diveu, Morel, Pedretti, Froger, Ravon, Garcia, Venereau, Preisser, Guignouard, Guillet, Dagregorio, Pène, Moles, Yssel, Chevalier, Bernard, Gascan, Lecron: "Oncostatin M secreted by skin infiltrating T lymphocytes is a potent keratinocyte activator involved in skin inflammation." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 178, Issue 7, pp. 4615-22, 2007 (PubMed).

Dillon, Sprecher, Hammond, Bilsborough, Rosenfeld-Franklin, Presnell, Haugen, Maurer, Harder, Johnston, Bort, Mudri, Kuijper, Bukowski, Shea, Dong, Dasovich, Grant, Lockwood, Levin, LeCiel, Waggie et al.: "Interleukin 31, a cytokine produced by activated T cells, induces dermatitis in mice. ..." in: Nature immunology, Vol. 5, Issue 7, pp. 752-60, 2004 (PubMed).

Mosley, De Imus, Friend, Boiani, Thoma, Park, Cosman: "Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation." in: The Journal of biological chemistry, Vol. 271, Issue 51, pp. 32635-43, 1997 (PubMed).

Rose, Bruce: "Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, Issue 19, pp. 8641-5, 1991 (PubMed).

Zarling, Shoyab, Marquardt, Hanson, Lioubin, Todaro: "Oncostatin M: a growth regulator produced by differentiated histiocytic lymphoma cells." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, Issue 24, pp. 9739-43, 1987 (PubMed).