Analytical Data
-
Gene name
NOX5
- Application
-
Alternative Names
NOX5A; NOX5B; NOX5-A; NOX5-B; NADPH Oxidase,EF-Hand Calcium Binding Domain 5
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96PH1
-
Expression Region
Ser456~Phe765
-
Molecular Weight
40kDa
-
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
NOX5 (NADPH oxidase 5) is a member of the NADPH oxidase family, which is crucial for the generation of reactive oxygen species (ROS) in various biological processes. Unlike its other family members, NOX5 is unique due to its calcium-dependent activation mechanism, making it particularly important in cells responsive to calcium fluctuations, such as endothelial cells and certain immune cells. The study of NOX5 has gained significant interest due to its involvement in various pathophysiological conditions, including cardiovascular diseases, cancer, and inflammation. Elevated NOX5 activity has been linked to oxidative stress, contributing to cell signaling dysregulation and tissue damage. Recent advancements in recombinant protein technology have facilitated the production of functional NOX5 proteins, allowing for detailed studies of its enzymatic properties, regulatory mechanisms, and role in ROS-mediated signaling pathways. Understanding the structure and function of NOX5 through recombinant techniques not only sheds light on its biological significance but also provides potential therapeutic insights, as targeting NOX5 could lead to novel treatments for diseases associated with oxidative stress. The elucidation of NOX5's role in cellular processes thus represents a promising avenue for research, with implications for both basic science and clinical applications.
