Analytical Data
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Gene name
RNASE8
- Application
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Alternative Names
Rnase-A8; Ribonuclease,RNase A Family,8
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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
Q8TDE3
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Expression Region
Trp19~Val154
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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
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Protein Description
Ribonuclease A-like protein 8 (RNASE8) is a member of the ribonuclease A superfamily, primarily expressed in human tissues, particularly in epithelial cells of the lungs and reproductive system, as well as in immune cells. This protein is believed to play crucial roles in various biological processes, including antiviral responses, inflammation, and potentially in the regulation of cellular apoptosis. Recent studies have indicated that RNASE8 exhibits antimicrobial activity against a range of pathogens, highlighting its potential as a natural defender in the immune system. Furthermore, it has been suggested that RNASE8 could be implicated in several diseases, such as asthma and certain cancers, due to its expression patterns and biochemical functions. Therefore, understanding the structure and function of RNASE8 is essential for elucidating its biological roles and therapeutic potential. Researchers have been focusing on recombinant protein technology to produce RNASE8 for biochemical characterization and functional studies. By generating recombinant RNASE8, scientists aim to investigate its enzymatic activity, interaction with nucleic acids, and the mechanisms underlying its role in immune responses. This research could pave the way for developing novel therapeutic strategies that leverage the unique properties of RNASE8, either as a therapeutic agent itself or as a target for drug development in treating diseases associated with dysregulated immune responses. Overall, the study of RNASE8 is vital not only for understanding its functions in health and disease but also for exploring its potential applications in medicine.











