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DUT encodes an essential enzyme of nucleotide metabolism. Additionally we are shipping Deoxyuridine Triphosphatase Proteins (88) and Deoxyuridine Triphosphatase Kits (6) and many more products for this protein.
Showing 10 out of 124 products:
Human Monoclonal DUT Primary Antibody for IF, IHC (p) - ABIN560672
Kiyonari, Iimori, Matsuoka, Watanabe, Morikawa-Ichinose, Miura, Niimi, Saeki, Tokunaga, Oki, Morita, Kadomatsu, Maehara, Kitao: The 1,2-Diaminocyclohexane Carrier Ligand in Oxaliplatin Induces p53-Dependent Transcriptional Repression of Factors Involved in Thymidylate Biosynthesis. in Molecular cancer therapeutics 2015
Cow (Bovine) Polyclonal DUT Primary Antibody for IHC, WB - ABIN2782436
Studebaker, Lafuse, Kloesel, Williams: Modulation of human dUTPase using small interfering RNA. in Biochemical and biophysical research communications 2005
Human Polyclonal DUT Primary Antibody for IHC, WB - ABIN2782437
Tóth, Varga, Kovács, Málnási-Csizmadia, Vértessy: Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme. in The Journal of biological chemistry 2007
revealed the importance of the PAA(10-12) tripeptide and the ID(17-18) dipeptide, as well as the role of the PAAK(10-13) segment in nuclear localization of dUTPase.
there is a conformational shift essential for catalytic competence in the 60-kDa Drosophila melanogaster dUTPase trimer
kinetic characterization, folding, and crystallographic studies of dUTPase
dUTPase is developmentally regulated in Drosophila melanogaster
dUTPase, a recently described eukaryotic model, has a similar affinity of binding towards alpha,beta-imino-dUTP as compared to the prokaryotic E. coli enzyme
dUTPase localization character showed strict timing to the nuclear cleavage phases and explained how its isoforms can be present within the nuclear microenvironment, although at different stages of cell cycle.
A single homozygous missense mutation (chr15.hg19:g.48,626,619A>G) located in the dUTPase (DUT) gene was associated with a syndrome of bone marrow failure and diabetes.
Comparison of the cellular distribution of wild-type dUTPase with those of hyperphosphorylation- and hypophosphorylation-mimicking mutants suggests that phosphorylation at Ser11 leads to the exclusion of dUTPase from the nucleus.
EBV-encoded dUTPase may act as an intercellular signaling molecule capable of modulating the cellular microenvironment
Data sugget that inhibition of dUTPase is a mechanism-based therapeutic approach to significantly enhance the efficacy of thymidylate synthase (TS)-targeted chemotherapeutic agents.
Repression of dUTPase induced specific expression level increments for thymidylate kinase and thymidine kinase, and also an increased sensitization to 5-fluoro-2'-deoxyuridine and 5-fluoro-uracil.
High dUTP pyrophosphatase is associated with recurrence in colorectal cancer patients undergoing 5-fluorouracil adjuvant chemotherapy
nuclear dUTPase may be a good biomarker for predicting prognosis in HCC patients after surgical resection
significant differences between the human and Plasmodium dUTPases
Novel gain of function activity of p53 mutants: activation of the dUTPase gene expression leading to resistance to 5-fluorouracil.
Nuclear dUTPase may contain a complex nuclear localization signal that is located throughout the entire protein.
dUTPase staining provides a useful measure of cell proliferation distinct from that offered by Ki-67 labeling. It proved particularly useful for the evaluation of diffuse astrocytomas.
kinetic model of the human dUTPase catalytic cycle
determined the crystal structure of the enzyme:alpha,beta-imino-dUTP
Establishment of a direct role for both mutant and wild-type forms of p53 in modulating dUTPase promoter activity.
hinge proline destabilize human and Escherichia coli dUTPases without preventing trimeric organization
This gene encodes an essential enzyme of nucleotide metabolism. The encoded protein forms a ubiquitous, homotetrameric enzyme that hydrolyzes dUTP to dUMP and pyrophosphate. This reaction serves two cellular purposes: providing a precursor (dUMP) for the synthesis of thymine nucleotides needed for DNA replication, and limiting intracellular pools of dUTP. Elevated levels of dUTP lead to increased incorporation of uracil into DNA, which induces extensive excision repair mediated by uracil glycosylase. This repair process, resulting in the removal and reincorporation of dUTP, is self-defeating and leads to DNA fragmentation and cell death. Alternative splicing of this gene leads to different isoforms that localize to either the mitochondrion or nucleus. A related pseudogene is located on chromosome 19.
, deoxyuridine triphosphatase
, deoxyuridine 5'-triphosphate nucleotidohydrolase
, deoxyuridine triphosphatase, dUTPase, P18
, dUTP nucleotidohydrolase
, deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
, PPAR-interacting protein 4