Analytical Data
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Gene name
DPYS
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简介
The DPYS protein plays a key role in the reductive pyrimidine degradation pathway by catalyzing the second step involving the reversible hydrolysis of dihydropyrimidines. Its enzymatic activity extends to the ring opening of 5,6-dihydrouracil, leading to the formation of N-carbamoyl-alanine, and the conversion of 5,6-dihydrothymine to N-carbamoyl-aminoisobutylene acid ester. DPYS Protein, Human (sf9) is the recombinant human-derived DPYS protein, expressed by Sf9 insect cells, with tag free.
- Application
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Alternative Names
Dihydropyrimidinase; DHP; DHPase; Hydantoinase; DPYS
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Species
Human
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Source
Baculovirus
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q14117
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Expression Region
Q14117 (N-G&P, M1-P519)
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Protein Length
Full Length
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Molecular Weight
54 kDa
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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
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Protein Description
DPYS (dihydropyrimidinase) is a crucial enzyme involved in the catabolism of pyrimidine bases, playing a significant role in the uracil and thymine degradation pathway. Its activity is vital for maintaining nucleotide homeostasis and is particularly important in rapidly dividing cells, such as those in cancerous tissues. Mutations or deficiencies in the DPYS gene can lead to dihydropyrimidine dehydrogenase deficiency, resulting in elevated levels of toxic metabolites that may cause various clinical manifestations, including neurological disorders. The study of recombinant DPYS protein is essential for understanding its enzymatic mechanisms and for developing potential therapeutic interventions. By producing this enzyme in a controlled laboratory environment, researchers can investigate its structure-function relationships, explore its role in metabolic pathways, and assess how specific mutations affect its functionality. Furthermore, recombinant DPYS can be utilized in drug development, providing insights into designing inhibitors or enhancers that could modulate its activity in pathological conditions, particularly in cancer therapy where targeting metabolic pathways holds promise. The advancement of recombinant DNA technology has made it feasible to study DPYS more intricately, opening avenues for novel therapeutic strategies aimed at conditions associated with pyrimidine metabolism dysregulation. Overall, the exploration of DPYS and its recombinant forms stands at the intersection of enzymology, genetics, and therapeutic development, with implications that could significantly enhance our understanding of nucleotide metabolism and its related disorders.
