Analytical Data
-
Gene name
PHYH
- Application
-
Alternative Names
Phytanic acid oxidase Phytanoyl-CoA alpha-hydroxylase
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O14832
-
Expression Region
1-338aa
-
Molecular Weight
62.4 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
The study of PHYH recombinant protein is rooted in the increasing recognition of the vital role that phytanoyl-CoA hydroxylase (PHYH) plays in human health and metabolism. PHYH is an enzyme primarily involved in the catabolism of phytanic acid, a dietary branched-chain fatty acid. Deficiencies in PHYH have been linked to Refsum disease, a rare genetic disorder characterized by the accumulation of phytanic acid in the body, leading to severe neurological and visual impairments. Research has focused on understanding PHYH's structure, function, and enzymatic mechanisms to develop potential therapeutic approaches for related disorders. The production of recombinant PHYH protein allows for detailed biochemical studies, including enzyme kinetics and structural biology, which are essential for elucidating the pathway of phytanic acid metabolism. Additionally, recombinant PHYH can serve as a powerful tool for screening small molecule inhibitors or enhancers, which could lead to novel treatments for metabolic disorders associated with its dysfunction. The integration of advanced techniques, such as CRISPR gene editing and high-throughput screening, in the study of PHYH is expected to yield critical insights into its biological significance and pave the way for innovative therapeutic strategies. Overall, the research on PHYH recombinant protein not only contributes to our understanding of metabolic processes but also highlights the importance of addressing genetic lipid metabolism diseases in clinical settings.
