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Mouse Anti-D2HGDH Recombinant Antibody (1E9B3) (CBMAB-D0134-YC)

Provided herein is a Mouse monoclonal antibody, which binds to D-2-Hydroxyglutarate Dehydrogenase (D2HGDH). The antibody can be used for immunoassay techniques, such as ELISA, IHC, WB.
See all D2HGDH antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
1E9B3
Antibody Isotype
IgG1
Application
ELISA, IHC, WB

Basic Information

Specificity
Human, Mouse
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!]

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
D-2-Hydroxyglutarate Dehydrogenase
Introduction
D2HGDH is D-2hydroxyglutarate dehydrogenase, a mitochondrial enzyme belonging to the FAD-binding oxidoreductase/transferase type 4 family. D2HGDH, which is most active in liver and kidney but also active in heart and brain, converts D-2-hydroxyglutarate to 2-ketoglutarate. Mutations in D2HGDH are present in D-2-hydroxyglutaric aciduria, a rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features.
Entrez Gene ID
Human728294
Mouse98314
UniProt ID
HumanQ8N465
MouseQ8CIM3
Alternative Names
D-2-Hydroxyglutarate Dehydrogenase; D2HGD; D-2-Hydroxyglutarate Dehydrogenase, Mitochondrial; EC 1.1.99.-; EC 1.1.99;
Function
Catalyzes the oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate.
Biological Process
2-oxoglutarate metabolic process Source: Reactome
Cellular protein metabolic process Source: HGNC-UCL
Response to cobalt ion Source: HGNC-UCL
Response to manganese ion Source: HGNC-UCL
Response to zinc ion Source: HGNC-UCL
Cellular Location
Mitochondrion
Involvement in disease
D-2-hydroxyglutaric aciduria 1 (D2HGA1):
A rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine.

Xiao, D., Zhang, W., Guo, X., Liu, Y., Hu, C., Guo, S., ... & Xu, P. (2021). A D-2-hydroxyglutarate biosensor based on specific transcriptional regulator DhdR. Nature communications, 12(1), 1-14.

Chou, F. J., Liu, Y., Lang, F., & Yang, C. (2021). D-2-Hydroxyglutarate in Glioma Biology. Cells, 10(9), 2345.

Berger, R. S., Ellmann, L., Reinders, J., Kreutz, M., Stempfl, T., Oefner, P. J., & Dettmer, K. (2019). Degradation of D-2-hydroxyglutarate in the presence of isocitrate dehydrogenase mutations. Scientific reports, 9(1), 1-11.

Pop, A., Struys, E. A., Jansen, E. E., Fernandez, M. R., Kanhai, W. A., van Dooren, S. J., ... & Salomons, G. S. (2019). D‐2‐hydroxyglutaric aciduria Type I: Functional analysis of D2HGDH missense variants. Human mutation, 40(7), 975-982.

Toplak, M., Brunner, J., Schmidt, J., & Macheroux, P. (2019). Biochemical characterization of human D-2-hydroxyglutarate dehydrogenase and two disease related variants reveals the molecular cause of D-2-hydroxyglutaric aciduria. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1867(11), 140255.

Guo, X., Zhang, M., Cao, M., Zhang, W., Kang, Z., Xu, P., ... & Gao, C. (2018). d-2-Hydroxyglutarate dehydrogenase plays a dual role in l-serine biosynthesis and d-malate utilization in the bacterium Pseudomonas stutzeri. Journal of Biological Chemistry, 293(40), 15513-15523.

Han, J., Jackson, D., Holm, J., Turner, K., Ashcraft, P., Wang, X., ... & Theiss, A. L. (2018). Elevated d-2-hydroxyglutarate during colitis drives progression to colorectal cancer. Proceedings of the National Academy of Sciences, 115(5), 1057-1062.

Zhang, W., Zhang, M., Gao, C., Zhang, Y., Ge, Y., Guo, S., ... & Xu, P. (2017). Coupling between d-3-phosphoglycerate dehydrogenase and d-2-hydroxyglutarate dehydrogenase drives bacterial l-serine synthesis. Proceedings of the National Academy of Sciences, 114(36), E7574-E7582.

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

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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