Analytical Data
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Gene name
Rnase 1
- Application
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Alternative Names
Rnase-H2A; RNASEHI; RNHIA; RNHL; AGS4; Ribonuclease H2,Large Subunit; Aicardi-Goutieres Syndrome 4; Ribonuclease HI large subunit
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9CWY8
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Expression Region
Met1~Leu301
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Molecular Weight
37kDa
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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
Ribonuclease A (RNase A) is a well-studied enzyme known for its ability to degrade RNA, making it a valuable tool in molecular biology and biochemistry. Recombinant RNase A, produced through recombinant DNA technology, has gained significant attention due to its potential applications in RNA research, therapeutics, and biotechnology. The production of RNase A in a recombinant system allows for high yields and the possibility of post-translational modifications, which can enhance its activity or specificity. Researchers have explored various aspects of RNase A, including its catalytic mechanisms, structural biology, and interaction with RNA substrates. Additionally, recombinant RNase A has been investigated for its use in developing RNA-based therapies and as an adjuvant in cancer treatment, where its ability to induce apoptosis in tumor cells can be harnessed. The study of RNase A is not only crucial for understanding RNA metabolism but also holds promise for innovative applications in gene therapy and RNA interference technologies. As a result, ongoing research aims to optimize the production and functional properties of recombinant RNase A, paving the way for its integration into advanced biotechnological applications.
