Alternative Name(s):

Dihydroorotate oxidase

Species: (Organism)

Homo sapiens (Human)

Gene Names:

DHODH

Tag info:

N-terminal 10xHis-tagged

Target Protein AA Sequence:

TGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR

Expression Region:

31-395aa

Subcellular Location:

Mitochondrion inner membrane, Single-pass membrane protein

Tissue Specificity:

Protein Length:

Partial

Pathway:

Mol. Weight:

45.1 kDa

Purity:

Greater than 85% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Signal Transduction

Function:

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

Involvement in disease:

Postaxial acrofacial dysostosis (POADS)

Relevance:

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Dihydroorotate dehydrogenase family, Type 2 subfamily

Reference:

"Recombinant human dihydroorotate dehydrogenase: expression, purification, and characterization of a catalytically functional truncated enzyme." Copeland R.A., Davis J.P., Dowling R.L., Lombardo D., Murphy K.B., Patterson T.A. Arch. Biochem. Biophys. 323:79-86(1995)