Oncostatin M (OSM) (AA 26-252) (Active) Protein

Details zu Produkt Nr. ABIN2181568, Anbieter: Anmelden zum Anzeigen
Proteinname
  • OSM
  • OncoM
  • oncostatin M
  • oncostatin M-like
  • oncostatin-M-like
  • OSM
  • Osm
  • LOC100342491
  • LOC100152038
Proteineigenschaft
AA 26-252
7
3
3
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
Spezies
Human
59
9
5
1
Quelle
HEK-293 Cells
49
5
3
3
1
1
1
1
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Optionen
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Marke ActiveMax®
Produktmerkmale This protein carries no "tag". The protein has a calculated MW of 25.8 kDa. The protein migrates as 36 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Reinheit >95 % as determined by SDS-PAGE.
Sterilität 0.22 μm filtered
Endotoxin-Niveau Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line). The ED50 for this effect is typically 2-10 ng/mL.

SDS-PAGE: of reduced rhOSM.
Hintergrund Oncostatin M is also known as OSM, is a glycoprotein belonging to the interleukin-6 family of cytokines that has functions mainly in cell growth. Of these cytokines it most closely resembles leukemia inhibitory factor (LIF) in both structure and function. However, it is as yet poorly defined and is proving important in liver development, haematopoeisis, inflammation and possibly CNS development. It is also associated with bone formation and destruction. OSM signals through cell surface receptors that contain the protein gp130. The type I receptor is composed of gp130 and LIFR, the type II receptor is composed of gp130 and OSMR. Oncostatin M (OSM) was previoustly identified by its ability to inhibit the growth of cells from melanoma and other solid tumors. It also has been reported that OSM, like LIF, IL-6 and G-CSF, has the ability to inhibit the proliferation of murine M1 myeloid leukemic cells and can induce their differentiation into macrophage-like cells. The human form of OSM is insensitive between pH 2 and 11 and resistant to heating for one hour at 56 degree but is not stable at 90 degrees. The three dimensional structure of human OSM has been solved to atomic resolution, confirming the predicted long chain four helix bundle topology. Comparing this structure with the known structures of other known LC cytokines shows it to be most closely related to LIF.
Molekulargewicht 25.8 kDa
NCBI Accession NP_065391
UniProt P13725
Forschungsgebiet Immunology, Innate Immunity, Cytokines, Signaling, Receptors
Pathways JAK-STAT Signalweg, Negative Regulation of Hormone Secretion
Beschränkungen Nur für Forschungszwecke einsetzbar
Format Lyophilized
Rekonstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handhabung Avoid repeated freeze-thaw cycles.
Lagerung -20 °C
Informationen zur Lagerung No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Bilder des Herstellers
SDS-PAGE (SDS) image for Oncostatin M (OSM) (AA 26-252) (Active) Protein (ABIN2181568) Human Oncostatin M on SDS-PAGE under reducing (R) condition. The gel was stained over...
Allgemeine Veröffentlichungen Walker, McGregor, Poulton, Solano, Pompolo, Fernandes, Constable, Nicholson, Zhang, Nicola, Gillespie, Martin, Sims: "Oncostatin M promotes bone formation independently of resorption when signaling through leukemia inhibitory factor receptor in mice." in: The Journal of clinical investigation, Vol. 120, Issue 2, pp. 582-92, 2010 (PubMed).

Tanaka, Miyajima: "Oncostatin M, a multifunctional cytokine." in: Reviews of physiology, biochemistry and pharmacology, Vol. 149, pp. 39-52, 2003 (PubMed).

Auguste, Guillet, Fourcin, Olivier, Veziers, Pouplard-Barthelaix, Gascan: "Signaling of type II oncostatin M receptor." in: The Journal of biological chemistry, Vol. 272, Issue 25, pp. 15760-4, 1997 (PubMed).