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Mouse Anti-OGDH Recombinant Antibody (9F4BD5) (CBMAB-O0324-CQ)

This product is a mouse antibody that recognizes OGDH. The antibody 9F4BD5 can be used for immunoassay techniques such as: ELISA, ICC, WB.
See all OGDH antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
9F4BD5
Antibody Isotype
IgG1
Application
ELISA, ICC, WB

Basic Information

Immunogen
Purified OGDH from porcine heart, purified GLUD from bovine liver
Specificity
Human
Antibody Isotype
IgG1
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!]

Format
Liquid
Buffer
HEPES buffered saline
Preservative
0.02% Sodium Azide
Concentration
1 mg/mL
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
Oxoglutarate Dehydrogenase
Introduction
This gene encodes one subunit of the 2-oxoglutarate dehydrogenase complex. This complex catalyzes the overall conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA and CO(2) during the Krebs cycle. The protein is located in the mitochondrial matrix and uses thiamine pyrophosphate as a cofactor. A congenital deficiency in 2-oxoglutarate dehydrogenase activity is believed to lead to hypotonia, metabolic acidosis, and hyperlactatemia. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
Entrez Gene ID
4967
UniProt ID
Q02218
Alternative Names
Oxoglutarate Dehydrogenase; Oxoglutarate (Alpha-Ketoglutarate) Dehydrogenase (Lipoamide); 2-Oxoglutarate Dehydrogenase Complex Component E1; EC 1.2.4.2; OGDC-E1; Oxoglutarate Dehydrogenase (Succinyl-Transferring); 2-Oxoglutarate Dehydrogenase, Mitochondrial
Function
2-oxoglutarate dehydrogenase (E1o) component of the 2-oxoglutarate dehydrogenase complex (OGDHC) (PubMed:24495017, PubMed:25210035, PubMed:28435050).
Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2 catalyzed by the whole OGDHC (PubMed:24495017, PubMed:25210035, PubMed:28435050).
Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST) (PubMed:24495017, PubMed:25210035, PubMed:28435050).
Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids (PubMed:25210035).
Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate (PubMed:28435050).
Mainly active in the mitochondrion (PubMed:29211711).
A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711).
Biological Process
2-oxoglutarate metabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Cerebellar cortex developmentIEA:Ensembl
Generation of precursor metabolites and energyISS:UniProtKB
Glycolytic processIEA:UniProtKB-KW
Hippocampus developmentIEA:Ensembl
Histone succinylationManual Assertion Based On ExperimentIDA:UniProtKB
NADH metabolic processIEA:Ensembl
Olfactory bulb mitral cell layer developmentIEA:Ensembl
Pyramidal neuron developmentIEA:Ensembl
Striatum developmentIEA:Ensembl
Succinyl-CoA metabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Tangential migration from the subventricular zone to the olfactory bulbIEA:Ensembl
Thalamus developmentIEA:Ensembl
Tricarboxylic acid cycleManual Assertion Based On ExperimentIBA:GO_Central
Cellular Location
Mitochondrion
Nucleus
Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation.

Whittle, E. F., Chilian, M., Karimiani, E. G., Progri, H., Buhas, D., Kose, M., ... & Carroll, C. J. (2023). Biallelic variants in OGDH encoding oxoglutarate dehydrogenase lead to a neurodevelopmental disorder characterized by global developmental delay, movement disorder, and metabolic abnormalities. Genetics in Medicine, 25(2), 100332.

Jiang, X., Peng, J., Xie, Y., Xu, Y., Liu, Q., Cheng, C., ... & Yu, D. (2023). Oxoglutarate dehydrogenase-like inhibits the progression of hepatocellular carcinoma by inducing DNA damage through non-canonical function. Cell Death & Differentiation, 30(8), 1931-1942.

Chang, L. C., Chiang, S. K., Chen, S. E., & Hung, M. C. (2022). Targeting 2-oxoglutarate dehydrogenase for cancer treatment. American Journal of Cancer Research, 12(4), 1436.

Yap, Z. Y., Strucinska, K., Matsuzaki, S., Lee, S., Si, Y., Humphries, K., ... & Yoon, W. H. (2021). A biallelic pathogenic variant in the OGDH gene results in a neurological disorder with features of a mitochondrial disease. Journal of inherited metabolic disease, 44(2), 388-400.

Leandro, J., Dodatko, T., Aten, J., Nemeria, N. S., Zhang, X., Jordan, F., ... & Houten, S. M. (2020). DHTKD1 and OGDH display substrate overlap in cultured cells and form a hybrid 2-oxo acid dehydrogenase complex in vivo. Human molecular genetics, 29(7), 1168-1179.

Bailey, P. S., Ortmann, B. M., Martinelli, A. W., Houghton, J. W., Costa, A. S., Burr, S. P., ... & Nathan, J. A. (2020). ABHD11 maintains 2-oxoglutarate metabolism by preserving functional lipoylation of the 2-oxoglutarate dehydrogenase complex. Nature communications, 11(1), 4046.

Eprinstev, A. T., Fedorin, D. N., Anokhina, G. B., & Sedykh, A. V. (2020). Molecular and biochemical aspects of light regulation of 2-oxoglutarate dehydrogenase in plants. Russian journal of plant physiology, 67, 378-385.

Condori-Apfata, J. A., Batista-Silva, W., Medeiros, D. B., Vargas, J. R., Valente, L. M. L., Heyneke, E., ... & Nunes-Nesi, A. (2019). The Arabidopsis E 1 subunit of the 2-oxoglutarate dehydrogenase complex modulates plant growth and seed production. Plant molecular biology, 101, 183-202.

Choi, S., Pfleger, J., Jeon, Y. H., Yang, Z., He, M., Shin, H., ... & Abdellatif, M. (2019). Oxoglutarate dehydrogenase and acetyl-CoA acyltransferase 2 selectively associate with H2A. Z-occupied promoters and are required for histone modifications. Biochimica et Biophysica Acta (BBA)-Gene Regulatory Mechanisms, 1862(10), 194436.

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

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