DLD Antibody

Code CSB-PA783949
Size US$166
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  • The image on the left is immunohistochemistry of paraffin-embedded Human gastic cancer tissue using CSB-PA783949(DLD Antibody) at dilution 1/20, on the right is treated with fusion protein. (Original magnification: ×200)
  • The image on the left is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using CSB-PA783949(DLD Antibody) at dilution 1/20, on the right is treated with fusion protein. (Original magnification: ×200)
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Product Details

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
Fusion protein of Human DLD
Immunogen Species
Homo sapiens (Human)
Purification Method
Antigen affinity purification
It differs from different batches. Please contact us to confirm it.
-20°C, pH7.4 PBS, 0.05% NaN3, 40% Glycerol
Tested Applications
Recommended Dilution
Application Recommended Dilution
ELISA 1:2000-1:5000
IHC 1:50-1:200
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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