Analytical Data
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Gene name
dusB
- Application
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Alternative Names
dusB；PIR1；RNA/RNP complex-1-interacting phosphatase
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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
P0ABT6
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Expression Region
1-321aa
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AA Sequence
MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMADAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDVVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCEEIAQLAEDCGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENFA
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Molecular Weight
43.3 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
DusB, short for D-tyrosyl-tRNA synthetase-binding protein B, is an essential player in the selenoprotein synthesis pathway in various organisms, including bacteria and eukaryotes. Its role has garnered significant interest due to its vital function in the incorporation of selenocysteine, an amino acid that contains selenium and is critical for the activity of several key enzymes. The research into DusB recombinant protein has been fueled by the need to understand the molecular mechanisms underlying selenoprotein synthesis, which is crucial for maintaining cellular redox balance and protecting against oxidative stress. Additionally, selenoproteins are implicated in various physiological processes, ranging from immune response to thyroid hormone metabolism, making DusB a potential target for therapeutic interventions in diseases linked to selenium deficiency. Recent advancements in molecular biology techniques have facilitated the production and characterization of the DusB recombinant protein, enabling researchers to study its structure, function, and interaction with other molecular components involved in tRNA processing and selenocysteine insertion. This research not only provides insights into fundamental biological processes but also holds promise for biotechnological applications, including the development of novel drugs and supplements that leverage the role of selenium in human health. As a result, the investigation of DusB recombinant protein is positioned at the intersection of basic science and applied research, highlighting its importance in both understanding cellular mechanisms and addressing health-related challenges.
