Analytical Data
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Gene name
Oncostatin M/OSM Protein
- Application
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Species
Canine
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Source
HEK293
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Tag
C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A8I3Q5M1
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Expression Region
S27-R207
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Protein Length
Partial
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Molecular Weight
27-35 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Oncostatin M (OSM) is a member of the interleukin-6 (IL-6) cytokine family and plays a crucial role in various physiological and pathological processes, including inflammation, tissue remodeling, and cancer progression. OSM is expressed in several cell types, including macrophages and T cells, and is known to exert its effects through activation of the gp130 receptor, subsequently triggering signaling pathways such as JAK/STAT and MAPK. Its involvement in biological processes such as the inhibition of cancer cell proliferation and the promotion of differentiation in certain cell types has made OSM a subject of interest for therapeutic applications. Furthermore, dysregulation of OSM expression is associated with various diseases, including cancer, rheumatoid arthritis, and cardiovascular diseases. Therefore, the optimization of recombinant OSM protein production has been pivotal for understanding its functional mechanisms and potential therapeutic uses. Research efforts have focused on enhancing its solubility, bioactivity, and stability, utilizing techniques such as gene engineering and various expression systems. The successful production of recombinant OSM protein is thus essential for in vitro and in vivo studies that seek to clarify its biological roles and therapeutic potential, making it a valuable candidate for further development in targeted therapies for inflammatory and neoplastic diseases.
