Analytical Data
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Gene name
RNASE13
- Application
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Alternative Names
RNASE13；Probable inactive ribonuclease-like Protein 13
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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
Q5GAN3
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Expression Region
21-156aa
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AA Sequence
MDIKMQIGSR NFYTLSIDYP RVNYPKGFRG YCNGLMSYMR GKMQNSDCPK IHYVIHAPWK AIQKFCKYSD SFCENYNEYC TLTQDSLPIT VCSLSHQQPP TSCYYNSTLT NQKLYLLCSR KYEADPIGIA GLYSGI
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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 13, a member of the ribonuclease (RNase) family, has garnered significant attention due to its potential roles in various biological processes and its implications in disease mechanisms. Unlike other RNases that are well-characterized for their catalytic functions in RNA degradation, RNase 13 is less studied, prompting researchers to explore its structural and functional properties. Initial studies suggest that RNase 13 may be involved in immune responses and cellular stress regulation, which could be critical in understanding its role in health and disease. The recombinant form of RNase 13 allows for detailed biochemical analysis and functional assays, enabling researchers to elucidate its enzymatic activity, substrate specificity, and potential therapeutic applications. Understanding the molecular characteristics of RNase 13 can pave the way for novel insights into its biological significance, particularly in relation to viral infections and inflammatory diseases. Additionally, research into RNase 13 may contribute to the development of new biomolecules for biomedical applications, including cancer therapy and antiviral strategies. Thus, the study of RNase 13 and its recombinant protein form represents a promising frontier in molecular biology and therapeutic research, warranting further investigation into its potential mechanisms and applications.
