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Mouse Anti-DHODH Recombinant Antibody (6E1) (CBMAB-D0838-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Dihydroorotate Dehydrogenase (Quinone) (DHODH). The antibody can be used for immunoassay techniques, such as ELISA, IHC-P, WB.
See all DHODH antibodies
Published Data
Fig. 1 The relative DHODH protein expression was analyzed by immunoblot.
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Summary

Host Animal
Mouse
Specificity
Human
Clone
6E1
Antibody Isotype
IgG2a, λ
Application
ELISA, IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2a, λ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Dihydroorotate Dehydrogenase (Quinone)
Introduction
DHODH 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.
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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For research use only. Not intended for any clinical use.

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