Mouse Anti-DHODH Recombinant Antibody (EG958) (CBMAB-EN1137-LY)

Name: Mouse Anti-DHODH Recombinant Antibody (EG958)
SKU: CBMAB-EN1137-LY
Rating: 5 (1 reviews)

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Published Data

Mouse Anti-DHODH Recombinant Antibody (EG958) (CBMAB-EN1137-LY-1) in WB

Western blot analysis of DHODH protein expression with teriflunomide treatment. All statistical analyses were performed using Student's t-test, and statistical significances are represented as * p < 0.05, ** p < 0.01, **** p < 0.0001. ...View More

Zhao, S., Francois, A., & Kidane, D. (2023). Inhibition of DHODH enhances replication-associated genomic instability and promotes sensitivity in endometrial cancer. Cancers, 15(24), 5727.

Mouse Anti-DHODH Recombinant Antibody (EG958) (CBMAB-EN1137-LY-2) in WB

Genetic and pharmacological inhibition of DHODH induces apoptosis in SK-NBE(2)C but not SK-N-AS cells in vitro. Western blots demonstrate protein expression of DHODH as well as cleaved PARP and activated caspase-3 (apoptosis markers) after shRNA DHODH knockdown and brequinar treatment. ...View More

Olsen, T. K., Dyberg, C., Embaie, B. T., Alchahin, A., Milosevic, J., Ding, J., ... & Baryawno, N. (2022). DHODH is an independent prognostic marker and potent therapeutic target in neuroblastoma. Jci Insight, 7(17), e153836.

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

EG958

Application

WB, IP, IF, ELISA

Immunogen

Amino acids 1-300 mapping at the N-terminus of human DHODH.

Host Species

Mouse

Specificity

Human, Mouse, Rat

Antibody Isotype

IgG2b, κ

Clonality

Monoclonal Antibody

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
ELISA	1:100-1:1,000
WB	1:100-1:1,000
IP	1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)	1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

Gelatin & PBS

Preservative

Sodium Azide

Concentration

0.2 mg/ml

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

Dihydroorotate Dehydrogenase (Quinone)

Introduction

The protein encoded by this gene catalyzes the fourth enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate, in de novo pyrimidine biosynthesis. This protein is a mitochondrial protein located on the outer surface of the inner mitochondrial membrane. [provided by RefSeq, Jul 2008]

Entrez Gene ID

1723

UniProt ID

Q02127

Alternative Names

Dihydroorotate Dehydrogenase (Quinone); Dihydroorotate Oxidase; DHOdehase; Dihydroorotate Dehydrogenase (Quinone), Mitochondrial; Human Complement Of Yeast URA1; Dihydroorotate Dehydrogenase;

Function

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

Biological Process

de novo' pyrimidine nucleobase biosynthetic process Source: GO_Central
'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
Female pregnancy Source: Ensembl
Lactation Source: Ensembl
Positive regulation of apoptotic process Source: Ensembl
Pyrimidine nucleoside biosynthetic process Source: Reactome
Pyrimidine ribonucleotide biosynthetic process Source: GO_Central
Regulation of mitochondrial fission Source: Ensembl
Response to caffeine Source: Ensembl
Response to drug Source: Ensembl
Response to L-arginine Source: Ensembl
Response to starvation Source: Ensembl

Cellular Location

Mitochondrion inner membrane

Involvement in disease

Postaxial acrofacial dysostosis (POADS):
POADS is characterized by severe micrognathia, cleft lip and/or palate, hypoplasia or aplasia of the posterior elements of the limbs, coloboma of the eyelids and supernumerary nipples. POADS is a very rare disorder: only 2 multiplex families, each consisting of 2 affected siblings born to unaffected, nonconsanguineous parents, have been described among a total of around 30 reported cases.

Topology

Mitochondrial matrix: 1-10
Helical: 11-30
Mitochondrial intermembrane: 31-395

PTM

The uncleaved transit peptide is required for mitochondrial targeting and proper membrane integration.

Horwitz, S. M., Blue, T. C., Ambarian, J. A., Hoshino, S., Seyedsayamdost, M. R., & Davis, K. M. (2022). Structural insights into inhibition of the drug target dihydroorotate dehydrogenase by bacterial hydroxyalkylquinolines. RSC chemical biology, 3(4), 420-425.

Sousa, F. M., Refojo, P. N., & Pereira, M. M. (2021). Investigating the amino acid sequences of membrane bound dihydroorotate: quinone oxidoreductases (DHOQOs): Structural and functional implications. Biochimica et Biophysica Acta (BBA)-Bioenergetics, 1862(1), 148321.

de Mori, R. M., Aleixo, M. A., Zapata, L. C., Calil, F. A., Emery, F. S., & Nonato, M. C. (2021). Structural basis for the function and inhibition of dihydroorotate dehydrogenase from Schistosoma mansoni. The FEBS Journal, 288(3), 930-944.

Orozco Rodriguez, J. M., Krupinska, E., Wacklin-Knecht, H., & Knecht, W. (2021). Protein production, kinetic and biophysical characterization of three human dihydroorotate dehydrogenase mutants associated with Miller syndrome. Nucleosides, Nucleotides & Nucleic Acids, 1-19.

Sato, D., Hartuti, E. D., Inaoka, D. K., Sakura, T., Amalia, E., Nagahama, M., ... & Shiba, T. (2020). Structural and biochemical features of Eimeria tenella dihydroorotate dehydrogenase, a potential drug target. Genes, 11(12), 1468.

Nonato, M. C., de Pádua, R. A., David, J. S., Reis, R. A., Tomaleri, G. P., Pereira, H. D. M., & Calil, F. A. (2019). Structural basis for the design of selective inhibitors for Schistosoma mansoni dihydroorotate dehydrogenase. Biochimie, 158, 180-190.

Calil, F. A., David, J. S., Chiappetta, E. R., Fumagalli, F., Mello, R. B., Leite, F. H., ... & Nonato, M. C. (2019). Ligand-based design, synthesis and biochemical evaluation of potent and selective inhibitors of Schistosoma mansoni dihydroorotate dehydrogenase. European journal of medicinal chemistry, 167, 357-366.

Reis, R. A., Calil, F. A., Feliciano, P. R., Pinheiro, M. P., & Nonato, M. C. (2017). The dihydroorotate dehydrogenases: past and present. Archives of biochemistry and biophysics, 632, 175-191.

Singh, A., Maqbool, M., Mobashir, M., & Hoda, N. (2017). Dihydroorotate dehydrogenase: a drug target for the development of antimalarials. European Journal of Medicinal Chemistry, 125, 640-651.

Kamyingkird, K., Cao, S., Tuvshintulga, B., Salama, A., Mousa, A. A., Efstratiou, A., ... & Xuan, X. (2017). Effects of dihydroorotate dehydrogenase (DHODH) inhibitors on the growth of Theileria equi and Babesia caballi in vitro. Experimental Parasitology, 176, 59-65.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

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For research use only. Not intended for any clinical use.

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