Analytical Data
-
Gene name
ubiF
- Application
-
Alternative Names
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P75728
-
Expression Region
1-391aa
-
Molecular Weight
46.5 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
Research on ubiF recombinant proteins has garnered significant attention due to their potential role in the biosynthesis of natural compounds. UbiF, a member of the ubiquinone biosynthetic pathway, is involved in the conversion of 3-polyprenyl-4-hydroxybenzoate to ubihydroquinone, a crucial step in the production of ubiquinone, also known as coenzyme Q. Ubiquinone plays a vital role in cellular energy metabolism and is essential for ATP production in mitochondria. In various organisms, including bacteria and eukaryotes, the pathways leading to ubiquinone synthesis are critical for maintaining cellular functions and overall metabolic health. The study of ubiF recombinant proteins not only aids in understanding the enzymatic mechanisms underpinning ubiquinone biosynthesis but also holds promise for biotechnological applications, such as the production of bioactive compounds and therapeutic agents. By exploring the structural and functional characteristics of ubiF, researchers aim to elucidate its catalytic properties and regulatory mechanisms, offering insights into metabolic engineering and the development of novel strategies for enhancing ubiquinone production. The insights gained from these studies could pave the way for advancements in health, nutrition, and sustainable bioprocessing.
