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DLD Antibody

  • 货号：
    CSB-PA783949
  • 规格：
    ￥1100
  • 图片：
    • 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)
  • 其他：

产品详情

  • Uniprot No.：
    P09622
  • 基因名：
    DLD
  • 别名：
    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
  • 宿主：
    Rabbit
  • 反应种属：
    Human,Mouse,Rat
  • 免疫原：
    Fusion protein of Human DLD
  • 免疫原种属：
    Homo sapiens (Human)
  • 标记方式：
    Non-conjugated
  • 抗体亚型：
    IgG
  • 纯化方式：
    Antigen affinity purification
  • 浓度：
    It differs from different batches. Please contact us to confirm it.
  • 保存缓冲液：
    -20°C, pH7.4 PBS, 0.05% NaN3, 40% Glycerol
  • 产品提供形式：
    Liquid
  • 应用范围：
    ELISA,IHC
  • 推荐稀释比：
    Application Recommended Dilution
    ELISA 1:2000-1:5000
    IHC 1:50-1:200
  • Protocols：
  • 储存条件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 货期：
    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.

产品评价

靶点详情

  • 功能：
    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.
  • 基因功能参考文献：
    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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  • 相关疾病：
    Dihydrolipoamide dehydrogenase deficiency (DLDD)
  • 亚细胞定位：
    Mitochondrion matrix. Nucleus. Cell projection, cilium, flagellum. Cytoplasmic vesicle, secretory vesicle, acrosome.
  • 蛋白家族：
    Class-I pyridine nucleotide-disulfide oxidoreductase family
  • 数据库链接：

    HGNC: 2898

    OMIM: 238331

    KEGG: hsa:1738

    STRING: 9606.ENSP00000205402

    UniGene: Hs.131711