Dihydropyrimidinase Like Protein 3, Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures.

Host: E Coli
Source: Prokaryotic expression

>95%

Supplied as lyophilized form in PBS, pH7.4, containing 5% trehalose, 0.01% sarcosyl.

5.6 (lot specific)

Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.
Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. The loss of this protein is less than 5% within the expiration date under appropriate storage condition.

Manufactured in an ISO 9001:2008 and ISO 13485:2003 Certified Laboratory.

Manufactured in a lab with traceable raw materials. Bulk orders can typically be prepared to the customer’s specifications, please inquire.

Small volumes of DPYSL3 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)

56,630 Da

dihydropyrimidinase

dihydropyrimidinase

Dihydropyrimidinase

DHP; DHPase  [Similar Products]

DPYS_HUMAN

Dihydropyrimidinase catalyzes the conversion of 5,6-dihydrouracil to 3-ureidopropionate in pyrimidine metabolism. Dihydropyrimidinase is expressed at a high level in liver and kidney as a major 2.5-kb transcript and a minor 3.8-kb transcript. Defects in the DPYS gene are linked to dihydropyrimidinuria. [provided by RefSeq, Jul 2008]

DPYS: Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6- dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate. Defects in DPYS are the cause of dihydropyrimidinase deficiency (DHPD). DHPD is an autosomal recessive disorder characterized by dihydropyrimidinuria and associated with a variable clinical phenotype: epileptic or convulsive attacks, dysmorphic features and severe developmental delay, and congenital microvillous atrophy. Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

Protein type: Nucleotide Metabolism - pyrimidine; Hydrolase; Other Amino Acids Metabolism - beta-alanine; Cofactor and Vitamin Metabolism - pantothenate and CoA biosynthesis; Xenobiotic Metabolism - drug metabolism - other enzymes; EC 3.5.2.2

Chromosomal Location of Human Ortholog: 8q22

Cellular Component: cytosol

Molecular Function: amino acid binding; thymine binding; dihydropyrimidinase activity; zinc ion binding; uracil binding; phosphoprotein binding

Biological Process: beta-alanine metabolic process; pyrimidine nucleoside catabolic process; pyrimidine base metabolic process; nucleobase, nucleoside and nucleotide metabolic process; uracil catabolic process; thymine catabolic process; pyrimidine base catabolic process; protein homotetramerization

Disease: Dihydropyrimidinase Deficiency

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