Recombinant Human Oncostatin M (OSM), Animal-Free Protein

OSM activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected HEK293T cells. Cells are treated in triplicate with a serial dilution of OSM for 6 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 0.75 ng/ml (34.2 pM).*Promega pGL4.33[luc2P/SRE/Hygro] #E1340

OSM migrates as a single band at 20 kDa in non-reducing (NR) conditions and 22 kDa upon reduction (R). The slight band under the main band in the reduced sample is likely an artefact of the reduction protocol. No contaminating protein bands are visible.Purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+ beta -mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Oncostatin M (OSM), Animal-Free Protein Summary

• Details of Functionality: No significant difference between EC₅₀ of reference and test lots
• Source: E. coli-derived human Oncostatin M/OSM protein
• Accession #: P13725.2
• Protein/Peptide Type: Animal-Free Recombinant Proteins
• Endotoxin Note: <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: Monomeric Oncostatin M (OSM) protein only

Packaging, Storage & Formulations

• Storage: Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.
• Buffer: Lyophilized from acetonitrile/TFA
• Reconstitution Instructions: Resuspend in water at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.

Notes

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Oncostatin M (OSM), Animal-Free Protein

• 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.

1. Richards, C.D. (2013) ISRN Inflamm. 2013:512103.
2. Malik, N. et al. (1989) Mol. Cel. Biol. 9:2847.
3. Linsley, P.S. et al. (1990) Mol. Cel. Biol. 10:1882.
4. Liu, J. et al. (1994) Cytokine 6:272.
5. Mosley, B. et al. (1996) J. Biol. Chem. 271:32635.
6. Grant, S.L. et al. (2001) Growth Factors 19:153.
7. Chollangi, S. et al. (2012) J. Biol. Chem. 287:32848.
8. Larrea, E. et al. (2014) J. Hepatol. 60:482.

Bioinformatics

• Uniprot:
  • P13725.2()