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Mouse Anti-DLD Monoclonal Antibody (Y6C) (CBMAB-1012-YC)

Provided herein is a mouse monoclonal antibody against Human DLD. The antibody, clone Y6C, can be used for immunoassay techniques, such as ELISA, ICC, IHC-Fr, IHC-P and WB.
See all DLD antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
Y6C
Antibody Isotype
IgG
Application
ELISA, ICC, IHC-Fr, IHC-P, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG
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
Purity
>95%, as determined by SDS-PAGE analysis
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
dihydrolipoamide dehydrogenase
Introduction
Dihydrolipoamide dehydrogenase (DLD) is a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. In homodimeric form, DLD functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.
Entrez Gene ID
1738
UniProt ID
P09622
Alternative Names
E3; LAD; DLDD; DLDH; GCSL; PHE3
Function
Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101).

The 2-oxoglutarate dehydrogenase complex is 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).

In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228).

Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).
Biological Process
2-oxoglutarate metabolic process Source: Ensembl
Aging Source: Ensembl
Cell redox homeostasis Source: InterPro
Dihydrolipoamide metabolic process Source: Ensembl
Gastrulation Source: Ensembl
Histone succinylation Source: UniProtKB
Lipoate metabolic process Source: Ensembl
Mitochondrial acetyl-CoA biosynthetic process from pyruvate Source: MGI
Mitochondrial electron transport, NADH to ubiquinone Source: Ensembl
Proteolysis Source: Ensembl
Regulation of membrane potential Source: Ensembl
Sperm capacitation Source: Ensembl
Cellular Location
Mitochondrion matrix; Nucleus; Flagellum; Acrosome. Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation.
Involvement in disease
Dihydrolipoamide dehydrogenase deficiency (DLDD):
An autosomal recessive metabolic disorder characterized biochemically by a combined deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate dehydrogenase complex (KGDC). Clinically, affected individuals have lactic acidosis and neurologic deterioration due to sensitivity of the central nervous system to defects in oxidative metabolism.
PTM
Tyrosine phosphorylated.

Yumnam, S., Kang, M. C., Oh, S. H., Kwon, H. C., Kim, J. C., Jung, E. S., ... & Kim, S. Y. (2021). Downregulation of dihydrolipoyl dehydrogenase by UVA suppresses melanoma progression via triggering oxidative stress and altering energy metabolism. Free Radical Biology and Medicine, 162, 77-87.

Ahmad, W., & Ebert, P. R. (2021). Suppression of a core metabolic enzyme dihydrolipoamide dehydrogenase (dld) protects against amyloid beta toxicity in C. elegans model of Alzheimer's disease. Genes & diseases, 8(6), 849-866.

Staretz-Chacham, O., Pode-Shakked, B., Kristal, E., Abraham, S. Y., Porper, K., Wormser, O., ... & Anikster, Y. (2021). The Effects of a Ketogenic Diet on Patients with Dihydrolipoamide Dehydrogenase Deficiency. Nutrients, 13(10), 3523.

Duarte, I. F., Caio, J., Moedas, M. F., Rodrigues, L. A., Leandro, A. P., Rivera, I. A., & Silva, M. F. B. (2021). Dihydrolipoamide dehydrogenase, pyruvate oxidation, and acetylation-dependent mechanisms intersecting drug iatrogenesis. Cellular and Molecular Life Sciences, 78(23), 7451-7468.

Quinonez, S. C., & Thoene, J. G. (2020). Dihydrolipoamide dehydrogenase deficiency.

Shin, D., Lee, J., You, J. H., Kim, D., & Roh, J. L. (2020). Dihydrolipoamide dehydrogenase regulates cystine deprivation-induced ferroptosis in head and neck cancer. Redox biology, 30, 101418.

Ambrus, A. (2019). An updated view on the molecular pathomechanisms of human dihydrolipoamide dehydrogenase deficiency in light of novel crystallographic evidence. Neurochemical Research, 44(10), 2307-2313.

Dai, F., Zhang, W., Zhuang, Q., Shao, Y., Zhao, X., Lv, Z., & Li, C. (2019). Dihydrolipoamide dehydrogenase of Vibrio splendidus is involved in adhesion to Apostichopus japonicus. Virulence, 10(1), 839-848.

Ambrus, A., & Adam-Vizi, V. (2018). Human dihydrolipoamide dehydrogenase (E3) deficiency: Novel insights into the structural basis and molecular pathomechanism. Neurochemistry International, 117, 5-14.

Ahmad, W. (2018). Dihydrolipoamide dehydrogenase suppression induces human tau phosphorylation by increasing whole body glucose levels in a C. elegans model of Alzheimer’s Disease. Experimental brain research, 236(11), 2857-2866.

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

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