Analytical Data
-
Gene name
dusB
- Application
-
Species
Escherichia coli O6:H1
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0ABT6
-
Expression Region
1-321aa
-
Molecular Weight
43.3 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
DusB, or tRNA-uridine phosphorylase, is an essential enzyme involved in the post-transcriptional modification of tRNA by catalyzing the addition of uridine residues to specific positions in tRNA molecules, thereby influencing their stability and function. Research on DusB has gained significant attention due to its critical role in bacterial physiology and its potential as a target for antimicrobial therapy. As antibiotic resistance rises, understanding the mechanisms that govern tRNA modification presents a promising avenue for developing novel antibiotics. The study of DusB not only enhances our comprehension of cellular processes in prokaryotes but also opens new frontiers in synthetic biology and genetic engineering, where modified tRNAs can be utilized for enhanced protein expression in various organisms. Current investigations focus on the structural and functional characterization of DusB, including its substrate specificity, catalytic mechanisms, and regulatory interactions within the cell. By elucidating these aspects, researchers aim to provide insights into how tRNA modifications contribute to bacterial adaptation and survival, ultimately fostering the development of innovative strategies to combat resistant bacterial strains.
