Anti-DPYD Antibody Picoband® fluoro488 Vervoeging

DPYD (Dihydropyrimidine Dehydrogenase), also called DPD, is an enzyme that in humans is encoded by the DPYD gene. The protein encoded by this gene is a pyrimidine catabolic enzyme and the initial and rate-limiting factor in the pathway of uracil and thymidine catabolism. The structure of the DPYD gene contains 23 exons spanning about 950 kb. Using somatic cell hybrid strategies, the DPYD gene is mapped to the centromeric region of chromosome 1 between 1p22 and 1q21. By fluorescence in situ hybridization, the DPYD gene is mapped to 1p22. The highest level of DPD was found in monocytes followed by that in lymphocytes, granulocytes, and platelets, whereas no significant activity of DPD could be detected in erythrocytes. The activity of DPD in peripheral blood mononuclear cells was intermediate between that observed in monocytes and lymphocytes. By cDNA microarray, Western blot analysis, and luciferase reporter assay, the transcription factor LSF was identified as a positive regulator of DPYD.

Dihydropyrimidine dehydrogenase [NADP (+) ]; DHPDHase; DPD;1.3.1.2; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase; DPYD

DPYD

1806

Q12882

Human, Mouse, Rat

No cross-reactivity with other proteins

A synthetic peptide corresponding to a sequence at the N-terminus of human DPYD, different from the related rat and mouse sequences by one amino acid.

Found in most tissues with greatest activity found in liver and peripheral blood mononuclear cells.

Flow Cytometry

Amino Acid Metabolism, Amino Acids, Cancer, Energy Metabolism, Energy Transfer Pathways, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Signal Transduction

Immunogen affinity purified.

Liquid

Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.

1. Albin, N., Johnson, M. R., Shahinian, H., Wang, K., Diasio, R. B. Initial characterization of the molecular defect in human dihydropyrimidine dehydrogenase deficiency. Proc. Am. Assoc. Cancer Res. (Abstract) 36: 211 only, 1995. 2. McLeod, H. L., Collie-Duguid, E. S. R., Vreken, P., Johnson, M. R., Wei, X., Sapone, A., Diasio, R. B., Fernandez-Salguero, P., van Kuilenberg, A. B. P., van Gennip, A. H., Gonzales, F. J. Nomenclature for human DPYD alleles. Pharmacogenetics 8: 455-459, 1998. 3. Ridge, S. A., Brown, O., McMurrough, J., Fernandez-Salguero, P., Evans, W. E., Gonzalez, F. J., McLeod, H. L. Mutations at codon 974 of theDPYD gene are a rare event. Brit. J. Cancer 75: 178-179, 1997.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

111401 MW

No cross reactivity with other proteins.

6

Dihydropyrimidine dehydrogenase [NADP (+) ]

Cytoplasm.

Belongs to the dihydropyrimidine dehydrogenase family.

Dihydropyrimidine dehydrogenase [NADP (+) ] (DHPDHase/DPD)

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.