Analytical Data
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Gene name
rnhB
- Application
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Alternative Names
RNase HII
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Species
TNT-Thermus thermophilus
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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
Q5SLU5
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Expression Region
1-203aa
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Molecular Weight
23.9 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
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Protein Description
The rnhB gene, which encodes the enzyme ribonuclease H (RNase H), plays a crucial role in the degradation of RNA-DNA hybrids generated during various cellular processes, including DNA replication and repair. RNase H enzymes are essential for maintaining genomic stability by eliminating these hybrids, which, if accumulated, can lead to genomic instability and contribute to various diseases, including cancer. Research on rnhB recombinant protein has gained traction due to its potential applications in biotechnology and medicine. By understanding the structure and function of the rnhB-encoded RNase H, scientists aim to utilize this enzyme in therapeutic settings, such as targeting RNA viruses or enhancing gene therapy strategies. Additionally, the production of rnhB as a recombinant protein allows for the detailed study of its enzymatic properties and mechanisms, providing insights that could lead to the development of novel inhibitors for therapeutic intervention. Current studies are focused on optimizing expression and purification techniques to obtain high-yield, functional RNase H proteins for experimental use, paving the way for future innovations in disease treatment and genetic engineering.
