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.

Recombinant Human Dihydroorotate Dehydrogenase Protein, CF Scientific Data Examples

	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 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

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

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.

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

Volume (to add to vial)

Mass (in vial)

Desired Reconstitution Concentration

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).

Item	Value
References	Liu, S. et al. (2000) Structure. 8:25. Reis, R. A. G. et al. (2017) Arch. Biochem. Biophys. 632:175. Copeland, R. A. et al. (2000) J. Biol. Chem. 275:33373. Singh, A. et al. (2017) Eur. J. Med. Chem. 125:640. Baumann, P. et al. (2009) Mol. Cancer Ther. 8:366. Zhu, S. et al. (2013) PLoS One. 8:e71555. Lewis, T. A. et al. (2016) ACS Med. Chem. Lett. 7:1112. Koundinya, M. et al. (2018) Cell Chem. Biol. 21:705. Herrmann, M. L. et al. (2000) Immunopharmacology. 47:273. Li, E. K. et al. (2004) Clin. Ther. 26:447. Warnke, C. et al. (2013) Clin. Neurol. Neurosurg. 115:S90. O'Connor, P. et al. (2016) Neurology 86:920. Wang, Q. Y. et al. (2011) J. Virol. 85:6548. Smee, D. F. et al. (2012) Antivir. Chem. Chemother. 22:263. Skerlj, R. T. et al. (2011) ACS Med. Chem. Lett. 2:708. Ohishi, T. et al. (2018) Helicobacter 23:e12470. Oliver, J. D. et al. (2016) Proc. Natl. Acad. Sci. USA 113:12809. Fang, J. et al. (2012) Biosci. Rep. 32:631.
Long Name	Dihydroorotate Dehydrogenase
Entrez Gene IDs	1723 (Human); 56749 (Mouse); 65156 (Rat)
Alternate Names	DHODH, DHOdehase, Dihydroorotate Oxidase, EC 1.3.3.1, EC 1.3.5.2, POADS, URA1, dihydroorotate dehydrogenase, dihydroorotate dehydrogenase, mitochondrial, human complement of yeast URA1

Citations for Recombinant Human Dihydroorotate Dehydrogenase Protein, CF

View all citations for the Proteins and Enzymes platform.
Please visit our Instrument Citation Database to search our collection of scientific articles that feature our instruments.

Recombinant Human Dihydroorotate Dehydrogenase Protein, CF

Order Information

Shipping Information

Key Product Details

Complete Your Research

Product Specifications