Analytical Data
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Gene name
QDPR
- Application
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Alternative Names
QDPR;DHPR;SDR33C1;Dihydropteridine reductase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09417
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Expression Region
2-244aa
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AA Sequence
AAAAAAGEA RRVLVYGGRG ALGSRCVQAF RARNWWVASV DVVENEEASA SIIVKMTDSF TEQADQVTAE VGKLLGEEKV DAILCVAGGW AGGNAKSKSL FKNCDLMWKQ SIWTSTISSH LATKHLKEGG LLTLAGAKAA LDGTPGMIGY GMAKGAVHQL CQSLAGKNSG MPPGAAAIAV LPVTLDTPMN RKSMPEADFS SWTPLEFLVE TFHDWITGKN RPSSGSLIQV VTTEGRTELT PAYF
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
QDPR (Quinoid Dihydropteridine Reductase) is an essential enzyme in the metabolic pathway of phenylalanine and tyrosine, playing a crucial role in the biosynthesis of tetrahydrobiopterin (BH4), a vital cofactor for various hydroxylation reactions in the body. Mutations in the QDPR gene can lead to a rare disorder known as phenylketonuria (PKU), characterized by the accumulation of phenylalanine, which can cause severe neurological consequences if left untreated. Understanding the structure and function of QDPR is therefore paramount, not only for elucidating the biochemical basis of PKU but also for developing effective treatments. Recent advances in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have provided valuable insights into the three-dimensional architecture of QDPR and its interactions with substrates and cofactors. These studies reveal how specific amino acid residues contribute to the enzyme's catalytic mechanism and stability, paving the way for targeted therapeutic strategies. Furthermore, the research into QDPR restructuring through potential gene therapies and small molecule drug design aims to provide new avenues for managing PKU and enhancing patient outcomes. Overall, the investigation into QDPR is a critical aspect of metabolic disorder research, emphasizing the intersection of enzymology, genetics, and biotechnology in the quest for novel therapeutic solutions.
