Product Description
Size: 10µg
Recombinant Human DPD protein is a Human Full Length protein, in the 1 to 173 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
Key facts
Expression system:Wheat germ,
Tags:GST tag N-Terminus,
Applications:SDS-PAGE, ELISA, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q12882,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 0.79% Tris HCl, 0.3% Glutathione
Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
DPD also known as dihydropyrimidine dehydrogenase is an enzyme important for the breakdown of pyrimidines particularly uracil and thymine. The DPD protein has an important role in the initial step of pyrimidine catabolism. It catalyzes the NADPH-dependent reduction of these pyrimidines to dihydrouracil and dihydrothymine. It consists of 1025 amino acids giving it a mass of approximately 111 kDa. DPD is expressed in various tissues with significant expression in the liver and to a lesser extent in peripheral blood lymphocytes.
Biological function summary
Dihydropyrimidine dehydrogenase impacts nucleotide metabolism which is significant for cellular replication and repair processes. DPD exists as part of a multi-enzyme complex that handles pyrimidine metabolism. It serves an important regulatory function by controlling the level of pyrimidines within cells. This regulation keeps the balance of free nucleotides which is critical for DNA synthesis and overall cellular homeostasis.
Pathways
DPD holds an important position in pyrimidine metabolism pathways and the drug metabolism pathway specifically influencing fluoropyrimidine-based chemotherapeutic agents. Within the pyrimidine metabolic pathway DPD links to other enzymes that further breakdown pyrimidines into more basic compounds. In drug metabolism DPD plays a vital role by metabolizing drugs like 5-fluorouracil. Its activity affects how individuals process these medications linking it to enzymes like thymidylate synthase that share pathways in cancer treatment drug action.
DPD deficiency relates to a genetic disorder that causes an excessive build-up of uracil and thymine leading to developmental disorders and neurological problems. Additionally abnormalities in DPD activity influence the efficacy and toxicity of fluorouracil chemotherapy in cancer treatments. DPD enzymatic activity when not properly regulated can lead to severe toxic reactions especially in relation to therapies reliant on enzymes such as thymidylate synthase emphasizing the critical interplay between these proteins in the management of fluoropyrimidine drug treatments.
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Collaboration
Tony Tang
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