Mouse Anti-DLD Recombinant Antibody (D1013) (CBMAB-D1018-YC)

Name: Mouse Anti-DLD Recombinant Antibody (D1013)
SKU: CBMAB-D1018-YC
Rating: 5 (1 reviews)

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Datasheet

SDS

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Basic Information

Host Animal

Mouse

Clone

D1013

Application

WB, IP, IF, ELISA, IHC-P

Immunogen

Amino acids 373-407 within an internal region of DLD.

Host Species

Mouse

Specificity

Human, Mouse, Rat, Chicken, Cattle, Pig, Horse

Antibody Isotype

IgM, 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
IHC-P	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 freeze/thaw cycles.

More Infomation

Target

Full Name

dihydrolipoamide dehydrogenase

Introduction

DLD belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In homodimeric form, the encoded protein functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. However, as a monomer, this protein can function as a protease. 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

Dihydrolipoamide Dehydrogenase; E3 Component Of Pyruvate Dehydrogenase Complex, 2-Oxo-Glutarate Complex, Branched Chain Keto Acid Dehydrogenase Complex; Glycine Cleavage System L Protein; EC 1.8.1.4; GCSL; PHE3; LAD; Dihydrolipoamide Dehydrogenase (E3 Component Of Pyruvate Dehydrogenase Complex, 2-Oxo-Glutarate Complex, Branched Chain Keto Acid Dehydrogenase Complex); Dihydrolipoyl Dehydrogenase, Mitochondrial; Glycine Cleavage System Protein L;

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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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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Isotype control

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

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