Analytical Data
-
Gene name
NOX4
- Application
-
Species
Pongo abelii
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q5R5C5
-
Expression Region
1-578aa
-
Molecular Weight
69.7 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
NOX4 (NADPH oxidase 4) is an important member of the NADPH oxidase family, predominantly expressed in endothelial cells and various types of tissues. It plays a crucial role in reactive oxygen species (ROS) generation, which contributes to cellular signaling and adaptation to oxidative stress. Elevated NOX4 activity has been implicated in various cardiovascular diseases, including hypertension, atherosclerosis, and heart failure, as it can lead to oxidative damage and inflammation. Researchers have increasingly focused on NOX4 as a potential therapeutic target, given its involvement in pathological conditions. The recombinant expression of NOX4 allows for detailed studies of its enzymatic properties, regulatory mechanisms, and interactions with other cellular proteins. Additionally, recombinant NOX4 can be utilized in drug screening and the development of inhibitors aimed at modulating its activity. Understanding the structure-function relationship of NOX4 through recombinant protein techniques can lead to novel insights into its role in disease mechanisms and therapeutic strategies. As a result, the study of NOX4 recombinant protein holds great promise for advancing our knowledge of oxidative stress-related diseases and developing targeted interventions.
