Analytical Data
-
Gene name
NDUFB7
- Application
-
Alternative Names
NDUFB7；NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P17568
-
Expression Region
2-137aa
-
AA Sequence
GAHLVRRYLGDASVEPDPLQMPTFPPDYGFPERKEREMVATQQEMMDAQLRLQLRDYCAHHLIRLLKCKRDSFPNFLACKQERHDWDYCEHRDYVMRMKEFERERRLLQRKKRREKKAAELAKGQGPGEVDPKVAL
-
Molecular Weight
43.3 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
NDUFB7, part of the NADH:ubiquinone oxidoreductase complex (Complex I) in the mitochondrial electron transport chain, plays a crucial role in cellular respiration and energy production. The significance of NDUFB7 arises from its involvement in the conversion of NADH to ubiquinone, facilitating the transfer of electrons and contributing to ATP synthesis. Mutations or deficiencies in NDUFB7 have been linked to various mitochondrial disorders, which can result in severe metabolic dysfunction and neurological disorders. This has prompted extensive research into the structure, function, and dynamics of NDUFB7, as well as its interactions with other subunits of Complex I and potential implications for therapeutic interventions. The characterization of recombinant NDUFB7 proteins has become a focal point, enabling scientists to explore its biochemical properties, stability, and role in mitochondrial pathophysiology. Understanding these aspects could provide insights into the mechanisms underlying mitochondrial diseases and highlight the potential for developing targeted treatments aimed at restoring functional integrity to the electron transport chain in affected individuals.
