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Anti-DPYD Antibody Picoband® Fluoro488 Conjugated

Product Specifications

Background

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.

Synonyms

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

Gene Name

DPYD

Gene ID

1806

UniProt

Q12882

Host

Rabbit

Reactivity

Human, Mouse, Rat

Cross Reactivity

No cross-reactivity with other proteins

Immunogen

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.

Clonality

Polyclonal

Tissue Specificity

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

Applications

Flow Cytometry

Field of Research

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

Purification

Immunogen affinity purified.

Form

Liquid

Function

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

References & Citations

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.

Storage Conditions

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

Calculated Molecular Weight

111401 MW

Specificity

No cross reactivity with other proteins.

Applications Notes

6

Gene Name Synonym

Dihydropyrimidine dehydrogenase [NADP (+) ]

Subcellular Location

Cytoplasm.

Sequence Similarities

Belongs to the dihydropyrimidine dehydrogenase family.

Protein Name

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

Isotype

Rabbit IgG

Contents

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

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