Human DPYS / Dihydropyrimidinase Protein
DHP,DHPase
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| Catalog Number | P14884-HNCB |
|---|---|
| Organism Species | Human |
| Host | Baculovirus-Insect Cells |
| Synonyms | DHP,DHPase |
| Molecular Weight | The recombinant human DPYS consists of 521 amino acids and has a calculated molecular mass of 56.8 kDa. The recombinant protein migrates as an approximately 54 kDa band in SDS-PAGE under reducing conditions. |
| predicted N | Gly |
| SDS-PAGE | ![]() |
| Purity | > 95 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the human DPYS (NP_001376.1) (Met1-Pro519) was fused with two additional amino acids (Gly&Pro) at the N-terminus. |
| Bio-activity | |
| Research Area | Epigenetics |DNA / RNA |DNA / Nucleotides |
| Formulation | Lyophilized from sterile 20mM Tris, 500mM NaCl, 3mM DTT, 10% glycerol, pH 8.0. 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | DPYS, also known as dihydropyrimidinase, belongs to the DHOase family, hydantoinase/dihydropyrimidinase subfamily. DPYS catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. It can catalyzes the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate. DPYS 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. |
| Reference |

