Recombinant Human Dihydroorotate Dehydrogenase Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 10062-DD

R&D Systems, part of Bio-Techne
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10062-DD-020
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Key Product Details

Source

E. coli

Accession #

Q02127

Conjugate

Unconjugated

Applications

Enzyme Activity

View all DHODH Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human DHODH protein
Thr31 - Arg395
with N-terminal Met and 6-His tag

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

41 kDa

SDS-PAGE

41 kDa, reducing conditions

Activity

Measured by its reduction of 2,6-dichloroindophenol during the oxidation of dihydroorotate.
The specific activity is >15000 pmol/min/μg, as measured under the described conditions.

Scientific Data Images for Recombinant Human Dihydroorotate Dehydrogenase Protein, CF

Recombinant Human Dihydroorotate Dehydrogenase Protein Binding Activity

Recombinant Human Dihydroorotate Dehydrogenase Protein Binding Activity

Recombinant Human DHODH (Catalog # 10062-DD) is measured by its reduction of 2,6-dichloroindophenol during oxidation of dihydroorotate.
Recombinant Human Dihydroorotate Dehydrogenase Protein SDS-PAGE

Recombinant Human Dihydroorotate Dehydrogenase Protein SDS-PAGE

2 μg/lane of Recombinant Human DHODH was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing a band at 41 kDa.

Formulation, Preparation and Storage

10062-DD
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: DHODH

Dihydroorotate dehydrogenase (DHODH) is a rate-limiting enzyme in the pyrimidine de novo pathway that converts dihydroorotate to orotate. DHODHs have a monomeric structure composed of a large C-terminal a/b barrel and a small N-terminal helical domain (1). There are two main classes of DHODHs based on similarity, preference of substrate, and subcellular location (1,2). Within Class 2, structural differences can be exploited for selective targeting (3,4).  Human DHODH belongs to Class 2 and is a monomeric, mitochondrial, FMN-dependent enzyme (2). It is ubiquitously expressed in most tissue. As DHODH catalyzes de novo pyrimidine synthesis for synthesis of DNA/RNA essential to rapidly proliferating cells, DHODH is currently a target for treatment of cancer (5-8). It has also been successfully targeted in treatment for rheumatoid arthritis (9-10), multiple sclerosis (11-12), viral infection (13-14), microbial infectious diseases such as malaria (4, 15) and gastrointestinal disease (3, 16), and antifungal infection (17). Mutations in the DHODH resulting in functional defects cause Miller syndrome, also known as postaxial acrofacial dystosis syndrome (POADS) (18).

References

  1. Liu, S. et al. (2000) Structure. 8:25.
  2. Reis, R. A. G. et al. (2017) Arch. Biochem. Biophys. 632:175.
  3. Copeland, R. A. et al. (2000) J. Biol. Chem. 275:33373.
  4. Singh, A. et al. (2017) Eur. J. Med. Chem. 125:640.
  5. Baumann, P. et al. (2009) Mol. Cancer Ther. 8:366.
  6. Zhu, S. et al. (2013) PLoS One. 8:e71555.
  7. Lewis, T. A. et al. (2016) ACS Med. Chem. Lett. 7:1112.
  8. Koundinya, M. et al. (2018) Cell Chem. Biol. 21:705.
  9. Herrmann, M. L. et al. (2000) Immunopharmacology. 47:273.
  10. Li, E. K. et al. (2004) Clin. Ther. 26:447.
  11. Warnke, C. et al. (2013) Clin. Neurol. Neurosurg. 115:S90.
  12. O'Connor, P. et al. (2016) Neurology 86:920.
  13. Wang, Q. Y. et al. (2011) J. Virol. 85:6548.
  14. Smee, D. F. et al. (2012) Antivir. Chem. Chemother. 22:263.
  15. Skerlj, R. T. et al. (2011) ACS Med. Chem. Lett. 2:708.
  16. Ohishi, T. et al. (2018) Helicobacter 23:e12470.
  17. Oliver, J. D. et al. (2016) Proc. Natl. Acad. Sci. USA 113:12809.
  18. Fang, J. et al. (2012) Biosci. Rep. 32:631.

Long Name

Dihydroorotate Dehydrogenase

Alternate Names

DHOdehase, Dihydroorotate Oxidase, POADS, URA1

Entrez Gene IDs

1723 (Human); 56749 (Mouse); 65156 (Rat)

Gene Symbol

DHODH

UniProt

Q02127

Additional DHODH Products

Product Documents for Recombinant Human Dihydroorotate Dehydrogenase Protein, CF

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Product Specific Notices for Recombinant Human Dihydroorotate Dehydrogenase Protein, CF

For research use only

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