Analytical Data
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Gene name
ROS1
- Application
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Alternative Names
DEMETER-like protein 1 Repressor of silencing 1
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Species
Arabidopsis thaliana
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9SJQ6
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Expression Region
1-320aa
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Molecular Weight
52.3 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
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Protein Description
Recombinant proteins, particularly those derived from the Rous sarcoma virus (RSV), have garnered significant attention in the fields of virology and biotechnology due to their implications in cancer research and therapeutic development. The Rous sarcoma virus is known for its ability to induce tumors in chickens, and the study of its components has provided crucial insights into the mechanisms of cancer progression. Researchers focus on isolating and expressing specific viral proteins, such as the oncogenic Src kinase, which plays a vital role in cell signaling pathways that govern cell growth and division. By employing techniques like genetic engineering and expression in suitable host systems (e.g., bacterial, yeast, or mammalian cells), scientists can produce these recombinant proteins in high yields. This not only facilitates the study of their biochemical properties and interactions but also aids in the development of diagnostic tools, vaccines, and targeted therapies. Understanding the structure-function relationship of these proteins can lead to breakthroughs in cancer treatment strategies and enhance our overall knowledge of viral pathogenesis. As a result, the research surrounding RSV recombinant proteins continues to be a pivotal area of study, bridging the gap between basic science and clinical applications in oncology.
