Analytical Data
-
Gene name
DsbA
- Application
-
Alternative Names
DsbA;Glutathione S-transferase kappa 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O52376
-
Expression Region
23-214aa
-
AA Sequence
AEPIESGKQYVELTSAVPVAVPGKIEVIELFWYGCPHCYAFEPTINPWVEKLPSDVNFVRIPAMFGGPWDAHGQLFITLDTMGVEHKVHAAVFEAIQKGGKRLTDKNDMADFVATQGVNKDDFLKTFDSFAVKGKIAQYKELAKKYEVTGVPTMIVNGKYRFDLGSAGGPEKTLQVADQLIDKERAAAKAAK
-
Molecular Weight
25.1kDa
-
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
DsbA is a disulfide bond oxidoreductase that plays a crucial role in the formation and isomerization of disulfide bonds in periplasmic proteins of Gram-negative bacteria. It is particularly important for protein folding and stability, facilitating the maturation of secreted proteins that require disulfide bonds to achieve their functional conformations. Research on DsbA has gained significant attention due to its implications in bacterial pathogenicity, as many virulence factors depend on proper disulfide bond formation. Furthermore, DsbA serves as a model for understanding protein folding mechanisms, making it valuable for biotechnological applications, such as the design of recombinant proteins with enhanced stability and activity. Recent studies have explored the structural and functional aspects of DsbA, revealing insights into its catalytic mechanisms and interactions with substrate proteins. This knowledge not only enhances our understanding of bacterial physiology but also presents potential targets for developing novel antimicrobial agents, given that inhibiting DsbA's activity could impair bacterial growth and virulence. The continued investigation into DsbA and its enzymatic properties holds promise for both fundamental research in molecular biology and practical applications in medicine and biotechnology.
