Analytical Data
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Gene name
RNASEH
- Application
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Alternative Names
RNASEH；RNH1；Ribonuclease H1
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Species
E.coli
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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
P0A7Y4
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Expression Region
1-155aa
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AA Sequence
MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALKEHCEVILSTDSQYVRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEWVKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV
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Molecular Weight
17.5 kDa
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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 H (ribonuclease H) is an enzyme that plays a critical role in the degradation of RNA strands in RNA-DNA hybrids, which are vital intermediates in various cellular processes, including DNA replication and transcription. The RNase H family comprises several members, with RNase H1 and RNase H2 being the most studied due to their involvement in maintaining genomic stability and their implications in various diseases, such as neurodegenerative disorders and cancer. Recent advances in structural biology have provided insights into the enzyme’s mechanism and substrate specificity, which are essential for understanding its biological function and potential therapeutic applications. Recombinant RNase H proteins have been engineered for functional studies, allowing researchers to dissect their mechanisms of action and interactions with other molecular players. Furthermore, RNase H inhibitors have gained attention as potential antiviral agents, particularly against HIV and other retroviruses, highlighting the enzyme's significance in pharmacological research. Understanding RNase H's structure-function relationship is vital for the development of targeted therapies and the exploration of its role in RNA metabolism and disease progression. This research not only enhances our knowledge of fundamental biological processes but also paves the way for innovative strategies in drug design and disease treatment.
