DLD Recombinant Monoclonal Antibody

Code: CSB-RA208703A0HU

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Size:

50μl100μl

US$210

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Species Reactivity: Human

Application: ELISA, IHC

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Target Background

Product Details

Uniprot NO.

P09622

Target Names

DLD

Alternative Names

Dehydrogenase complex; E3 component antibody; Diaphorase antibody; Dihydrolipoamide dehydrogenase antibody; Dihydrolipoyl dehydrogenase antibody; Dihydrolipoyl dehydrogenase mitochondrial antibody; dld antibody; DLDD antibody; DLDH antibody; DLDH_HUMAN antibody; E3 antibody; E3 branched chain aplha-keto acid antibody; E3 component of pyruvate dehydrogenase antibody; E3 component of pyruvate dehydrogenase complex 2 oxo glutarate complex branched chain keto acid dehydrogenase complex antibody; GCSL antibody; Glycine cleavage system L protein antibody; Glycine cleavage system protein L antibody; LAD antibody; lipoamide dehydrogenase antibody; Lipoamide reductase antibody; Lipoyl dehydrogenase antibody; mitochondrial antibody; OTTHUMP00000206744 antibody; OTTHUMP00000206746 antibody; OTTHUMP00000206748 antibody; OTTHUMP00000206749 antibody; PHE 3 antibody; PHE3 antibody; Pyruvate dehydrogenase component E3 antibody

Species Reactivity

Human

Immunogen

A synthesized peptide from human DLD protein

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

8G4

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Scope Application

ELISA Protocol Immunohistochemistry (IHC) Protocol

Recommended Dilution

Application	Recommended Dilution
IHC	1:50-1:200

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Datasheet & COA

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Images

IHC image of CSB-RA208703A0HU diluted at 1:100 and staining in paraffin-embedded human kidney tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.
IHC image of CSB-RA208703A0HU diluted at 1:100 and staining in paraffin-embedded human gastric cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB.

Description

Dihydrolipoamide dehydrogenase (DLD) serves as the E3 component shared among several critical mitochondrial multienzyme complexes, including pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and the branched-chain alpha-keto acid dehydrogenase complex. This flavoprotein also functions as the L protein in the glycine cleavage system, positioning it at the intersection of carbohydrate metabolism, amino acid catabolism, and cellular energy production. Mutations in DLD are associated with metabolic disorders, making it a significant target for researchers investigating mitochondrial function, metabolic disease mechanisms, and signal transduction pathways.

This recombinant monoclonal antibody (clone 8G4) offers the reproducibility and consistency that demanding research protocols require. Generated against a synthetic peptide derived from human DLD protein, the recombinant production method ensures sequence-defined specificity and eliminates the lot-to-lot variability that can compromise longitudinal studies or multi-site collaborations. The rabbit IgG format, purified by affinity chromatography, delivers reliable performance across experimental workflows.

Validation studies demonstrate effective immunohistochemical detection in human tissues, with testing performed on paraffin-embedded human kidney and gastric cancer specimens using a Leica Bond system with citrate buffer antigen retrieval. At a 1:100 dilution, the antibody produced clear staining patterns in both normal and pathological tissue contexts, with recommended working dilutions ranging from 1:50 to 1:200 depending on your specific application requirements. The antibody is also validated for ELISA applications, providing flexibility for researchers employing multiple detection strategies.

For investigators exploring mitochondrial metabolism, cancer biology, or metabolic disorders, this DLD antibody provides a dependable tool for characterizing protein expression and localization in human tissue samples.

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Target Background

Function(From Uniprot)

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). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. 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. In monomeric form may have additional moonlighting function as serine protease. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.

Gene References into Functions

Molecular characterization of dihydrolipoamide dehydrogenase binding sites to titanium dioxide has been reported. PMID:28247484
study found that individuals infected with HBV withwith basal core promoter (BCP) double mutations (A1762T, G1764A)have lower concentrations of serum DLD than those with the wild-type BCP PMID:27303803
Mitochondrial dihydrolipoamide dehydrogenase is upregulated in response to the brain intermittent hypoxic preconditioning. PMID:26078703
IgA autoantibody against DLD could be a novel diagnostic marker for endometrial cancer. PMID:25202086
Case Report: novel mutation in the DLD interface giving rise to DLD deficiency. PMID:20652410
Human, mouse, and pig Dld has moonlighting function as a protease in addition to its canonical function as a a dehydrogenase. PMID:17404228
This molecular dynamics study proposes the structural changes that may lead to the modulation in reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase. PMID:24012808
ATP consumption is demonstrated in respiration-impaired isolated and in situ neuronal somal mitochondria from transgenic mice that exhibit a 20-48% decrease in alpha-ketoglutarate dehydrogenase activity. PMID:23475850
the cryptic activities of DLD promote oxidative damage to neighboring molecules and thus contribute to the clinical severity of DLD mutations PMID:21930696
Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex. PMID:21543315
the E3 binding protein component of the pyruvate dehydrogenase complex appear to be a rare cause of pyruvate dehydrogenase deficiency PMID:11935326
Activity of human dihydrolipoamide dehydrogenase is reduced by mutation at threonine-44 of FAD-binding region to valine. PMID:12297006
A c.1444A>G substitution in E3 exon 13, predictive of a p.R482G (or R447G in the processed gene product) substitution in a highly conserved domain of the protein was found. PMID:15712224
Asparagine-473 residue is important for the catalytic function of dihydrolipoamide dehydrogenase. PMID:15826505
the disease-causing mutations of E3 occur at three locations in the human enzyme: the dimer interface, the active site, and the FAD and NAD(+)-binding sites PMID:15946682
specificity of pairing for human E3BP with E3 from its subcomplex structure to be most likely due to conformational rigidity of the binding fragment of the E3-binding domain of E3BP and its exquisite amino acid match with the E3 target interface PMID:16263718
dihydrolipoamide dehydrogenase PMID:16442803
The conservation of the Ile-51 residue with Ala using site-directed mutagenesis in human Dihydrolipoamide dehydrogenase(E3) was very important to the efficient catalytic function of the enzyme. PMID:16584639
These results suggest that N286 and D320 play a role in the catalytic function of the E3. PMID:17171578
Certain DLD mutations can simultaneously induce the loss of a primary metabolic activity and the gain of a moonlighting proteolytic activity thus contributing to the metabolic derangement associated with DLD deficiency. PMID:17404228
kinetic studies suggest that T148 is not important to E3 catalytic function and R281 plays a role in the catalytic function of E3 PMID:17960497
This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia. PMID:19405953