Analytical Data
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Gene name
Ribonuclease
- Application
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Alternative Names
/
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Species
Bacillus amyloliquefaciens
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Source
E. coli
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00648
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Expression Region
48-157aa
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Molecular Weight
13.3 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
Ribonuclease (RNase) is an enzyme that plays a crucial role in RNA metabolism by catalyzing the degradation of RNA molecules. The study of recombinant RNase proteins has gained significant attention due to their potential applications in various fields, including molecular biology, biomedicine, and biotechnology. Recombinant DNA technology allows for the expression of RNase proteins in host systems, such as bacteria, yeast, or mammalian cells, enabling researchers to produce large quantities of the enzyme for detailed studies. Understanding the structure-function relationship of RNase is vital, as it can provide insights into its catalytic mechanisms and specificity towards different RNA substrates. Additionally, recombinant RNases have been explored for their therapeutic potential, particularly in the treatment of RNA virus infections and in cancer therapies, where they can selectively degrade the RNA of cancer cells. The ability to engineer RNases through mutations or modifications further enhances their efficacy and specificity, opening new avenues for drug development. Overall, the research on recombinant RNase proteins not only advances our understanding of fundamental biological processes but also paves the way for innovative applications in medicine and biotechnology.
