Recombinant Human beta-Ureidopropionase/UPB1 is produced by our E. coli expression system. The target protein is expressed with sequence (Met1-Glu384) of Human UPB1 fused with a His tag at the C-terminus.
Pureté
> 95 % as determined by reducing SDS-PAGE.
Stérilité
0.2 μm filtered
niveau d'endotoxine
Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
UPB1
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
> 80 % as determined by SDS-PAGE and Coomassie blue staining
AbP, STD
Restrictions
For Research Use only
Format
Liquid
Reconstitution
It is not recommended to reconstitute to a concentration less than 100 μg/mL. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Buffer
Supplied as a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.
Conseil sur la manipulation
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
Stock
-80 °C
Stockage commentaire
Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
Beta-Ureidopropionase is a cytoplasmic protein which belongs to the CN hydrolase family of BUP subfamily. beta-Ureidopropionase binds one zinc ion per subunit, catalyzes the last step in the pyrimidine degradation pathway. beta-Ureidopropionase can convert N-carbamyl-beta-aminoisobutyric acid and N-carbamyl-beta-alanine to beta-aminoisobutyric acid and beta-alanine, ammonia and carbon dioxide, respectively. 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. Defects in beta-Ureidopropionase are the cause of beta-Ureidopropionase deficiency that is characterized by muscular hypotonia, dystonic movements, scoliosis, microcephaly and severe developmental delay. Alternative Names: Beta-Ureidopropionase, BUP-1, Beta-Alanine Synthase, N-Carbamoyl-Beta-Alanine Amidohydrolase, UPB1, BUP1