Recombinant Mouse Osm protein (rFc Tag)

Species

Mouse

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg2921

---

Validation Data Gallery

---

Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <1.0 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Mouse Osm protein Asn25-Arg206 (Accession# P53347) with a rabbit IgG Fc tag at the C-terminus.
• GeneID: 18413
• Accession: P53347
• PredictedSize: 46.1 kDa
• Formulation: Lyophilized from sterile PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Oncostatin M (OSM) is a multifunctional cytokine that belongs to the interleukin-6 (IL-6) family. It is primarily secreted by activated T lymphocytes and macrophages as a 28 kDa glycoprotein. OSM shares properties with all members of this cytokine family, but is most closely related in structure and function to leukemia inhibitory factor (LIF). OSM acts on a variety of cells and is involved in regulating gene activation, cell growth, and inflammatory processes. It is a potent inducer of anti-proteases, has anti-inflammatory properties, acts as an immune modifier, and promotes the deposition of extracellular matrix proteins. In the context of respiratory diseases, OSM may play a significant role in normal wound healing, as well as in remodeling and pathological fibrosis.

References:

1.Tanaka, M, and A Miyajima. Reviews of physiology, biochemistry and pharmacology vol. 149 (2003): 39-52.
2.Tran, T A et al. Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc vol. 13,4 (2000): 427-32.
3.Tiffen, Paul G et al. Molecular endocrinology (Baltimore, Md.) vol. 22,12 (2008): 2677-88.
4.Baker, Brandi J et al. Glia vol. 56,11 (2008): 1250-62. 
5.West, Nathaniel R et al. Scandinavian journal of immunology vol. 88,3 (2018): e12694.
6.Huguier, Vincent et al. Scientific reports vol. 9,1 (2019): 2113.