Analytical Data
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Gene name
RpII215
- Application
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Alternative Names
DNA-directed RNA polymerase III largest subunit
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Species
Drosophila melanogaster
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04052
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Expression Region
1579-1881aa
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Molecular Weight
33.6 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
RpII215, a vital component of the RNA polymerase II complex, plays a crucial role in the transcription process, influencing gene expression and, consequently, cellular functions. The study of RpII215 is imperative because of its involvement in various biological processes including cell differentiation, proliferation, and response to environmental signals. Researchers are particularly interested in its structure-function relationships, as mutations or dysregulation in RpII215 have been linked to various diseases, including cancer. Understanding the molecular mechanisms by which RpII215 operates could unveil potential therapeutic targets for these conditions. Moreover, advancements in recombinant protein technology have facilitated the production and purification of RpII215, allowing for in-depth functional assays and structural analysis. This research not only enhances our comprehension of the fundamental principles of transcription regulation but also opens avenues for biotechnological applications, such as the development of novel inhibitors or drugs that could modulate the activity of RNA polymerase II in disease contexts. The ongoing investigation into RpII215 thus represents a significant intersection of molecular biology, biochemistry, and clinical research, aiming to decipher the complexities of eukaryotic gene expression and its implications for health and disease.
