DLD Antibody

Code CSB-PA006928LA01HU
Size US$166
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  • Western Blot
    Positive WB detected in: HepG2 whole cell lysate, Hela whole cell lysate, MCF-7 whole cell lysate, 293 whole cell lysate, Jurkat whole cell lysate, Rat liver tissue, Rat brain tissue, Rat heart tissue, Mouse heart tissue
    All lanes: DLD antibody at 2µg/ml
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 55, 44, 50 kDa
    Observed band size: 55 kDa

  • IHC image of CSB-PA006928LA01HU 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 biotinylated secondary antibody and visualized using an HRP conjugated SP system.

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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) DLD Polyclonal antibody
Uniprot No.
Target Names
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
Raised in
Species Reactivity
Human, Rat, Mouse
Recombinant Human Dihydrolipoyl dehydrogenase, mitochondrial protein (398-495AA)
Immunogen Species
Homo sapiens (Human)

The DLD Antibody (Product code: CSB-PA006928LA01HU) is Non-conjugated. For DLD Antibody with conjugates, please check the following table.

Available Conjugates
Conjugate Product Code Product Name Application
HRP CSB-PA006928LB01HU DLD Antibody, HRP conjugated ELISA
FITC CSB-PA006928LC01HU DLD Antibody, FITC conjugated
Biotin CSB-PA006928LD01HU DLD Antibody, Biotin conjugated ELISA
Purification Method
>95%, Protein G purified
It differs from different batches. Please contact us to confirm it.
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Tested Applications
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:5000
IHC 1:20-1:200
Troubleshooting and FAQs
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.

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Target Background

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
  1. Molecular characterization of dihydrolipoamide dehydrogenase binding sites to titanium dioxide has been reported. PMID: 28247484
  2. 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
  3. Mitochondrial dihydrolipoamide dehydrogenase is upregulated in response to the brain intermittent hypoxic preconditioning. PMID: 26078703
  4. IgA autoantibody against DLD could be a novel diagnostic marker for endometrial cancer. PMID: 25202086
  5. Case Report: novel mutation in the DLD interface giving rise to DLD deficiency. PMID: 20652410
  6. Human, mouse, and pig Dld has moonlighting function as a protease in addition to its canonical function as a a dehydrogenase. PMID: 17404228
  7. 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
  8. 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
  9. the cryptic activities of DLD promote oxidative damage to neighboring molecules and thus contribute to the clinical severity of DLD mutations PMID: 21930696
  10. Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex. PMID: 21543315
  11. the E3 binding protein component of the pyruvate dehydrogenase complex appear to be a rare cause of pyruvate dehydrogenase deficiency PMID: 11935326
  12. Activity of human dihydrolipoamide dehydrogenase is reduced by mutation at threonine-44 of FAD-binding region to valine. PMID: 12297006
  13. 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
  14. Asparagine-473 residue is important for the catalytic function of dihydrolipoamide dehydrogenase. PMID: 15826505
  15. 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
  16. 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
  17. dihydrolipoamide dehydrogenase PMID: 16442803
  18. 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
  19. These results suggest that N286 and D320 play a role in the catalytic function of the E3. PMID: 17171578
  20. 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
  21. 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
  22. This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia. PMID: 19405953

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Involvement in disease
Dihydrolipoamide dehydrogenase deficiency (DLDD)
Subcellular Location
Mitochondrion matrix. Nucleus. Cell projection, cilium, flagellum. Cytoplasmic vesicle, secretory vesicle, acrosome.
Protein Families
Class-I pyridine nucleotide-disulfide oxidoreductase family
Database Links

HGNC: 2898

OMIM: 238331

KEGG: hsa:1738

STRING: 9606.ENSP00000205402

UniGene: Hs.131711

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