You Searched For: 6-(Trifluoromethyl)uracil

Catalog Number: (10348-946)

Supplier: Bioss

Description: Converts cytosine to uracil or 5-methylcytosine to thymine by deaminating carbon number 4.

Catalog Number: (76083-096)

Supplier: Bioss

Description: Converts cytosine to uracil or 5-methylcytosine to thymine by deaminating carbon number 4.

Catalog Number: (76083-098)

Supplier: Bioss

Description: Converts cytosine to uracil or 5-methylcytosine to thymine by deaminating carbon number 4.

Catalog Number: (10348-944)

Supplier: Bioss

Description: Converts cytosine to uracil or 5-methylcytosine to thymine by deaminating carbon number 4.

Catalog Number: (76100-844)

Supplier: Bioss

Description: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.

Catalog Number: (10450-102)

Supplier: Bioss

Description: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.

Catalog Number: (10166-608)

Supplier: Genetex

Description: Rabbit Polyclonal antibody to UNG (uracil-DNA glycosylase)

Catalog Number: (10108-964)

Supplier: Prosci

Description: UPB1 is a protein that belongs to the CN hydrolase family. Beta-ureidopropionase catalyzes the last step in the pyrimidine degradation pathway. The pyrimidine bases uracil and thymine are degraded via the consecutive action of dihydropyrimidine dehydrogenase (DHPDH), dihydropyrimidinase (DHP) and beta-ureidopropionase (UP) to beta-alanine and beta-aminoisobutyric acid, respectively. UP deficiencies are associated with N-carbamyl-beta-amino aciduria and may lead to abnormalities in neurological activityThis gene encodes a protein that belongs to the CN hydrolase family. Beta-ureidopropionase catalyzes the last step in the pyrimidine degradation pathway. The pyrimidine bases uracil and thymine are degraded via the consecutive action of dihydropyrimidine dehydrogenase (DHPDH), dihydropyrimidinase (DHP) and beta-ureidopropionase (UP) to beta-alanine and beta-aminoisobutyric acid, respectively. UP deficiencies are associated with N-carbamyl-beta-amino aciduria and may lead to abnormalities in neurological activity.

Catalog Number: (10450-368)

Supplier: Bioss

Description: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.

Catalog Number: (10481-160)

Supplier: Bioss

Description: Dihydropyrimidine dehydrogenase (DPYD) catalyzes the first rate-limiting step of the NADPH-dependent catabolism of uracil and thymine to dihydrouracil and dihydrothymine; thus, a deficiency of DPYD leads to an accumulation of uracil and thymine. Abnormal concentrations of these metabolites in bodily fluids may be the cause of neurological disease and a contraindication for treatment of cancer patients with certain pyrimidine analogs. DPYD also catalyzes the anticancer agent 5-fluorouracil (5-FU) pathway and is involved in the efficacy and toxicity of 5-FU. Variations in DPYD concentration may arise from alterations at the transcriptional level of the dihydropyrimidine dehydrogenase gene. Specifically, hypermethylation of the DPYD promoter downregulates dihydropyrimidine dehydrogenase expression. Deficient DPYD alleles may constitute a risk factor for severe toxicity following treatment with 5-FU.Involvement in disease:Defects in DPYD are the cause of dihydropyrimidine dehydrogenase deficiency (DPYD deficiency) ; also known as hereditary thymine-uraciluria or familial pyrimidinemia. DPYD deficiency is a disease characterized by persistent urinary excretion of excessive amounts of uracil, thymine and 5-hydroxymethyluracil. Patients suffering from this disease show a severe reaction to the anticancer drug 5-fluorouracil. This reaction includes stomatitis, Leukopenia, thrombocytopenia, hair loss, diarrhea, fever, marked weight loss, cerebellar ataxia, and neurologic symptoms, progressing to semicoma.

Catalog Number: (10481-174)

Supplier: Bioss

Description: Dihydropyrimidine dehydrogenase (DPYD) catalyzes the first rate-limiting step of the NADPH-dependent catabolism of uracil and thymine to dihydrouracil and dihydrothymine; thus, a deficiency of DPYD leads to an accumulation of uracil and thymine. Abnormal concentrations of these metabolites in bodily fluids may be the cause of neurological disease and a contraindication for treatment of cancer patients with certain pyrimidine analogs. DPYD also catalyzes the anticancer agent 5-fluorouracil (5-FU) pathway and is involved in the efficacy and toxicity of 5-FU. Variations in DPYD concentration may arise from alterations at the transcriptional level of the dihydropyrimidine dehydrogenase gene. Specifically, hypermethylation of the DPYD promoter downregulates dihydropyrimidine dehydrogenase expression. Deficient DPYD alleles may constitute a risk factor for severe toxicity following treatment with 5-FU.Involvement in disease:Defects in DPYD are the cause of dihydropyrimidine dehydrogenase deficiency (DPYD deficiency) ; also known as hereditary thymine-uraciluria or familial pyrimidinemia. DPYD deficiency is a disease characterized by persistent urinary excretion of excessive amounts of uracil, thymine and 5-hydroxymethyluracil. Patients suffering from this disease show a severe reaction to the anticancer drug 5-fluorouracil. This reaction includes stomatitis, Leukopenia, thrombocytopenia, hair loss, diarrhea, fever, marked weight loss, cerebellar ataxia, and neurologic symptoms, progressing to semicoma.

Catalog Number: (10481-182)

Supplier: Bioss

Description: Dihydropyrimidine dehydrogenase (DPYD) catalyzes the first rate-limiting step of the NADPH-dependent catabolism of uracil and thymine to dihydrouracil and dihydrothymine; thus, a deficiency of DPYD leads to an accumulation of uracil and thymine. Abnormal concentrations of these metabolites in bodily fluids may be the cause of neurological disease and a contraindication for treatment of cancer patients with certain pyrimidine analogs. DPYD also catalyzes the anticancer agent 5-fluorouracil (5-FU) pathway and is involved in the efficacy and toxicity of 5-FU. Variations in DPYD concentration may arise from alterations at the transcriptional level of the dihydropyrimidine dehydrogenase gene. Specifically, hypermethylation of the DPYD promoter downregulates dihydropyrimidine dehydrogenase expression. Deficient DPYD alleles may constitute a risk factor for severe toxicity following treatment with 5-FU.Involvement in disease:Defects in DPYD are the cause of dihydropyrimidine dehydrogenase deficiency (DPYD deficiency) ; also known as hereditary thymine-uraciluria or familial pyrimidinemia. DPYD deficiency is a disease characterized by persistent urinary excretion of excessive amounts of uracil, thymine and 5-hydroxymethyluracil. Patients suffering from this disease show a severe reaction to the anticancer drug 5-fluorouracil. This reaction includes stomatitis, Leukopenia, thrombocytopenia, hair loss, diarrhea, fever, marked weight loss, cerebellar ataxia, and neurologic symptoms, progressing to semicoma.

Catalog Number: (76108-484)

Supplier: Bioss

Description: Dihydropyrimidine dehydrogenase (DPYD) catalyzes the first rate-limiting step of the NADPH-dependent catabolism of uracil and thymine to dihydrouracil and dihydrothymine; thus, a deficiency of DPYD leads to an accumulation of uracil and thymine. Abnormal concentrations of these metabolites in bodily fluids may be the cause of neurological disease and a contraindication for treatment of cancer patients with certain pyrimidine analogs. DPYD also catalyzes the anticancer agent 5-fluorouracil (5-FU) pathway and is involved in the efficacy and toxicity of 5-FU. Variations in DPYD concentration may arise from alterations at the transcriptional level of the dihydropyrimidine dehydrogenase gene. Specifically, hypermethylation of the DPYD promoter downregulates dihydropyrimidine dehydrogenase expression. Deficient DPYD alleles may constitute a risk factor for severe toxicity following treatment with 5-FU.Involvement in disease:Defects in DPYD are the cause of dihydropyrimidine dehydrogenase deficiency (DPYD deficiency) ; also known as hereditary thymine-uraciluria or familial pyrimidinemia. DPYD deficiency is a disease characterized by persistent urinary excretion of excessive amounts of uracil, thymine and 5-hydroxymethyluracil. Patients suffering from this disease show a severe reaction to the anticancer drug 5-fluorouracil. This reaction includes stomatitis, Leukopenia, thrombocytopenia, hair loss, diarrhea, fever, marked weight loss, cerebellar ataxia, and neurologic symptoms, progressing to semicoma.

Catalog Number: (10348-924)

Supplier: Bioss

Description: Converts cytosine to uracil or 5-methylcytosine to thymine by deaminating carbon number 4.

Catalog Number: (10095-718)

Supplier: Proteintech

Description: TRUB1 gene encodes a 349-amino acid product, with a VFAVHKPKGPTSA box in positions 71-83 corresponding to motif I of the TruB family (probably involved in conserving protein structure). This protein may be responsible for synthesis of pseudouridine from uracil in transfer RNAs.

Catalog Number: (89416-074)

Supplier: Prosci

Description: UNG1 Antibody: The human uracil-DNA glycosylase (UNG) gene encodes both mitochondrial (UNG1) and nuclear (UNG2) forms through differentially regulated promotes and alternative splicing. While UNG2 is the major enzyme in the base excision repair pathway that removes uracil residues from nuclear DNA that arise through either misincorporation during replication or cytosine deamination, inhibition of UNG1 by uracil glycosylase inhibitor did not lead to increased levels of spontaneous or induced mitochondrial DNA mutations. However, decreased levels of UNG activity and increased oxidative damage to mitochondrial DNA were seen in older mice, suggesting that mitochondrial DNA repair mechanisms may be involved in various neurodegenerative disorders in an age-dependent manner. This UNG1 antibody will not cross-react with UNG2.