Analytical Data
-
Gene name
viaA
- Application
-
Alternative Names
VWA domain protein interacting with AAA ATPase
-
Species
Salmonella typhi
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8Z2R0
-
Expression Region
3-476aa
-
Molecular Weight
58.2 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
The study of ViaA recombinant proteins has gained increasing attention in recent years due to their crucial role in various biological processes and their potential applications in biotechnology and medicine. ViaA, a member of the ABC (ATP-binding cassette) transporters, is involved in the uptake of nutrients and molecules across cellular membranes. Understanding its structure and function can provide insights into fundamental cellular mechanisms, including nutrient transport and drug resistance in pathogenic organisms. Researchers have focused on characterizing ViaA's molecular structure, as well as its interactions with other cellular components, to elucidate its role in health and disease. The recombinant expression of ViaA proteins in host systems, such as bacteria or yeast, allows for detailed biochemical analysis and offers a platform for the development of novel therapeutic strategies. Moreover, the manipulation of ViaA functions may lead to innovative approaches in the treatment of infections or metabolic disorders, highlighting the importance of this protein in both basic and applied biological research. As such, the exploration of ViaA recombinant proteins is not only pivotal for advancing our understanding of cellular biology but also opens new avenues for the development of biotechnological applications.
