Analytical Data
-
Gene name
NDUFV3
- Application
-
Alternative Names
NDUFV3;NADH dehydrogenase [ubiquinone] flavoProtein 3. mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P56181
-
Expression Region
35-108aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSSAESGKSEKGQPQNSKKQSPPKKPAPV PAEPFDNTTYKNLQHHDYSTYTFLDLNLELSKFRMPQPSSGRESPRH
-
Molecular Weight
11 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
NDUFV3 is a crucial subunit of the mitochondrial respiratory chain complex I, which plays a vital role in cellular energy production through oxidative phosphorylation. Research on NDUFV3 has gained increasing attention due to its implications in various mitochondrial disorders and neurodegenerative diseases. Mutations in the NDUFV3 gene can lead to complex I deficiency, resulting in diminished ATP production and increased oxidative stress, both of which contribute to the pathogenesis of conditions such as Leigh syndrome and Parkinson’s disease. Furthermore, NDUFV3 is involved in the regulation of reactive oxygen species (ROS) and apoptosis, further underscoring its significance in cellular health and disease mechanisms. Advances in recombinant DNA technology have enabled the production of NDUFV3 protein in various systems, facilitating in-depth studies on its structure, function, and potential as a therapeutic target. Understanding the biochemical properties and interactions of NDUFV3 may provide insights into mitochondrial function and lead to the development of novel strategies for treating related disorders. As research progresses, elucidating the regulatory mechanisms governing NDUFV3 activity and its interplay with other mitochondrial components could unveil new avenues in tackling mitochondrial dysfunction and improving patient outcomes.
