Analytical Data
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Gene name
RNASE12
- Application
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Alternative Names
RNASE12；Probable inactive ribonuclease-like Protein 12
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
21-147aa
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AA Sequence
EAVMSTLEHL HVDYPQNDVP VPARYCNHMI IQRVIREPDH TCKKEHVFIH ERPRKINGIC ISPKKVACQN LSAIFCFQSE TKFKMTVCQL IEGTRYPACR YHYSPTEGFV LVTCDDLRPD SFLGYVK
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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 is a member of the ribonuclease A superfamily, which plays a critical role in RNA metabolism and antiviral defense. Recent studies have highlighted its significance in various biological processes, including its potential involvement in gene regulation and immune responses. Unlike other ribonucleases, RNASE12 exhibits unique enzymatic properties and has been found to have antiviral activity against specific RNA viruses. Researchers are increasingly interested in characterizing the recombinant form of RNASE12 to better understand its functional mechanisms and therapeutic potential. The recombinant protein can be produced using advanced expression systems, enabling the detailed study of its structure-function relationships. This research could pave the way for novel antiviral strategies and enhance our understanding of the innate immune system. Additionally, insights gained from RNASE12 could contribute to the development of RNA-targeting therapeutics, which are becoming increasingly important in combating viral infections and managing RNA-related diseases. As the exploration of RNASE12 progresses, it holds promise for significant advancements in both basic and applied biomedical research fields.
