Analytical Data
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Gene name
OSF
- Application
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Alternative Names
OSF；Cadherin-11
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21246
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Expression Region
33-168aa
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AA Sequence
GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD
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Molecular Weight
15.3 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
OSF (Osteosarcoma-derived secreted factor) recombinant proteins have garnered significant attention in recent years due to their potential implications in cancer biology and therapeutics. Originating from osteosarcoma, a type of bone cancer predominantly affecting adolescents and young adults, OSF plays a crucial role in tumor growth, metastasis, and the interaction between tumor cells and the microenvironment. Research has shown that OSF can influence various cellular pathways, affecting not only the proliferation and survival of cancer cells but also the behavior of surrounding stromal cells. As understanding of OSF’s molecular mechanisms deepens, the development of recombinant OSF proteins offers promising avenues for studying their functional roles in osteosarcoma and potentially other malignancies. These proteins can be utilized in various experimental settings, including in vitro assays and in vivo models, to elucidate the pathways that OSF modulates, enabling researchers to identify novel therapeutic targets. Furthermore, the exploration of OSF as a biomarker for the diagnosis and prognosis of osteosarcoma enhances the clinical relevance of this research. Overall, the study of OSF recombinant proteins represents a convergence of cancer biology, molecular research, and therapeutic development, aiming to improve outcomes for patients affected by osteosarcoma and potentially contribute to broader cancer treatment strategies.
