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Recombinant Human OSM


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Product Source Size Cat. No. Price
Recombinant Human OSM CHO cells25 µg Z101365 $760.00
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Data Sheet
Print Version
Alternative Names OSM
Description Oncostatin M is produced by monocytes and T cells after cell activation, adherent macrophages, and various T cell lines. Oncostatin M is a member of the IL-6-related cytokine subfamily that includes IL-6, IL-11, LIF, CNTF and CT-1. Oncostatin M mediates its bioactivities through two different heterodimer receptors. They both involve gp130 as a signal transducing moiety, which is found also in receptors for a number of other cytokines. When gp130 dimerizes with LIF receptor beta subunit this generates the high affinity type 1 OSM receptor. When gp130 dimerizes with a protein known as OSM receptor beta this generates the type 2 OSM receptor. Both OSM receptors activate the receptor-associated Janus kinases JAK1, JAK2, and TYK2. Signaling also involves the transcriptional activators STAT3 and STAT5b (see also: STAT proteins) were specifically activated through the gp130-OSM-R-beta type II heterocomplex. The signaling pathway differences observed between the common type I LIF/OSM receptor and the specific type II OSM receptor might explain some of the bioactivities specifically displayed by OSM. Oncostatin M inhibits the growth of several tumor cell lines (A375 melanoma, lung carcinomas). The antiproliferative activity of oncostatin M for some cell lines is synergised by TGF-beta and IFN-gamma. It promotes the growth of human fibroblasts, vascular smooth muscle cells, and some normal cell lines. Oncostatin can inhibit the proliferation of murine M1 myeloid leukemic cells and induces their differentiation into macrophage-like cells, a function shared by LIF, G- CSF, and IL-6.
Gene Symbol OSM
Gene ID 5008
Accession No. P13725
Source CHO cells
Appearance Lyophilized Powder
Molecular Weight 26.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method.
Purity >95% as determined by SDS-PAGE
Bioactivity The ED(50) was determined by the dose-dependent stimulation of the proliferation of f human TF-1 cells is ≤ 3.0 ng/mL, corresponding to a specific activity of ≥ 2.0 x 10^5 units/mg.
Formulation Recombinant Oncostatin M was lyophilized from a 0.2μm filtered concentrated (1.0 mg/mL) PBS solution, pH 7.0.
Reconstitution A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Storage The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage For research use only. Not for diagnostic or therapeutic use.
Product Documents
Product References
Submit a new question:
How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970.

· Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL).

· For recombinant proteins: EU is reported per microgram of protein.

· One EU = 0.1-0.2 ng endotoxin/µg of protein.

· At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.