Analytical Data
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Gene name
RNASE12
- Application
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Alternative Names
Probable inactive ribonuclease-like protein 12
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Species
Human
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Source
E. coli
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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
Q5GAN4
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Expression Region
Glu21~Lys147
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Molecular Weight
18kDa
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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
RNASE12, a member of the ribonuclease A superfamily, has garnered attention due to its potential roles in various biological processes, including RNA metabolism, immune response, and the regulation of gene expression. Initially identified in humans, the RNASE12 gene encodes an enzyme that exhibits unique structural and functional properties, distinguishing it from other RNases. Studies have suggested that RNASE12 may participate in antiviral defense mechanisms, making it a candidate for investigation in the context of infectious diseases. Additionally, its evolutionary significance is underscored by its presence in multiple vertebrate lineages, hinting at a conserved function over time. Recent research endeavors have focused on the recombinant expression of RNASE12 to elucidate its enzymatic activity and substrate specificity. By producing RNASE12 in a controlled laboratory environment, scientists aim to gain insights into its biochemical properties and potential therapeutic applications. Understanding the structure-function relationship of RNASE12 could pave the way for novel strategies in treating viral infections or regulating cellular processes linked to RNase activity. Furthermore, the investigation of RNASE12's interactions with RNA molecules may reveal new dimensions of RNA biology, highlighting the enzyme's importance beyond traditional ribonuclease functions. Overall, the study of RNASE12 not only contributes to our understanding of ribonucleases but also opens avenues for research in molecular biology, biotechnology, and medicine.
