Analytical Data
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Gene name
RNASE8
- Application
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Alternative Names
RNASE8；Ribonuclease 8
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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
Q8TDE3
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Expression Region
28-154aa
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AA Sequence
KPK DMTSSQWFKT QHVQPSPQAC NSAMSIINKY TERCKDLNTF LHEPFSSVAI TCQTPNIACK NSCKNCHQSH GPMSLTMGEL TSGKYPNCRY KEKHLNTPYI VACDPPQQGD PGYPLVPVHL DKVV
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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
RNase 8, a member of the ribonuclease A superfamily, has garnered interest due to its unique expression pattern and potential roles in immunity and inflammation. It is predominantly expressed in immune cells, notably in the myeloid lineage, suggesting its involvement in host defense mechanisms against viral and bacterial infections. RNase 8 exhibits antiviral properties by degrading viral RNA, thereby inhibiting viral replication. Additionally, studies indicate that RNase 8 may play a role in modulating immune responses, as its expression is upregulated in various inflammatory conditions. The recombinant form of RNase 8 allows for detailed functional analyses and therapeutic exploration, particularly in understanding its mechanisms of action and potential applications in treating viral infections or autoimmune diseases. Recent research has focused on characterizing the protein’s enzymatic activity, stability, and structural properties, providing insights into its biological significance. This growing body of evidence highlights RNase 8 as a promising candidate for further investigation in both basic and clinical research settings. Understanding the multifaceted roles of RNase 8 can pave the way for novel therapeutic strategies harnessing its antiviral and immunomodulatory potential.
