Analytical Data
-
Gene name
NDUFA2
- Application
-
Alternative Names
Complex I-B8 ;CI-B8NADH-ubiquinone oxidoreductase B8 subunit
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O43678
-
Expression Region
4-99aa
-
Molecular Weight
37.6 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
NDUFA2, or NADH:ubiquinone oxidoreductase subunit A2, is an essential component of the mitochondrial respiratory chain complex I, which plays a critical role in cellular energy production by facilitating electron transfer from NADH to ubiquinone. Research has shown that NDUFA2 is not only crucial for ATP synthesis but also for the proper function of the electron transport chain, impacting overall mitochondrial health. Mutations or dysregulation of NDUFA2 have been associated with various mitochondrial diseases, highlighting its significance in both energy metabolism and potential pathophysiological conditions. Furthermore, the study of NDUFA2 has gained traction in understanding the molecular mechanisms underlying mitochondrial dysfunction, which is linked to neurodegenerative disorders and metabolic syndromes. Recombining and characterizing the NDUFA2 protein allows for a deeper exploration of its structural and functional properties, facilitating the development of therapeutics aimed at ameliorating the effects of mitochondrial diseases. Recent advances in recombinant DNA technology have enabled researchers to produce NDUFA2 in vitro, paving the way for detailed biochemical assays and structural studies, which can provide insights into its interactions with other complex I components and its role in the regulation of mitochondrial function. As the understanding of NDUFA2 expands, it holds promise for unveiling new therapeutic strategies and biomarkers for mitochondrial-related disorders.
