Analytical Data
-
Gene name
NDUFB5
- Application
-
Alternative Names
Complex I-SGDH ;CI-SGDHNADH-ubiquinone oxidoreductase SGDH subunit
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O43674
-
Expression Region
94-189aa
-
Molecular Weight
27.5 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
NDUFB5, a crucial subunit of the mitochondrial respiratory chain complex I, plays an essential role in cellular energy production through oxidative phosphorylation. This protein is involved in electron transfer processes, facilitating the reduction of ubiquinone to ubiquinol, which is vital for ATP synthesis. Mutations in the NDUFB5 gene have been linked to various mitochondrial diseases, resulting in impaired metabolic function and a range of clinical symptoms, including neurological deficits and myopathy. The study of NDUFB5 recombinant protein is vital for understanding the structure-function relationship within complex I and elucidating the mechanisms underlying mitochondrial dysfunction. Researchers are increasingly focused on characterizing this protein to explore its potential as a therapeutic target. By utilizing recombinant technology, scientists can produce and purify NDUFB5 for biochemical assays, structural analysis, and functional studies. This approach not only provides insights into the protein's role in the respiratory chain but also aids in the development of novel interventions for mitochondrial disorders. Understanding the dynamics of NDUFB5 and its interactions with other subunits of complex I could pave the way for innovative strategies to restore mitochondrial function in affected individuals and enhance our knowledge of bioenergetics in health and disease.
