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GLUD1 + GLUD2 antibody

GTX105765
GeneTex
ApplicationsImmunoFluorescence, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityDrosophila, Human, Mouse, Rat
TargetGLUD1
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Overview

  • Supplier
    GeneTex
  • Product Name
    GLUD1 + GLUD2 antibody
  • Delivery Days Customer
    9
  • Application Supplier Note
    WB: 1:500-1:3000. ICC/IF: 1:100-1:1000. IHC-P: 1:100-1:1000. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
  • Applications
    ImmunoFluorescence, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
  • Certification
    Research Use Only
  • Clonality
    Polyclonal
  • Concentration
    0.07 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID2746
  • Target name
    GLUD1
  • Target description
    glutamate dehydrogenase 1
  • Target synonyms
    GDH, GDH1, GLUD, hGDH1, glutamate dehydrogenase 1, mitochondrial, epididymis secretory sperm binding protein, epididymis tissue sperm binding protein Li 18mP, glutamate dehydrogenase (NAD(P)+)
  • Host
    Rabbit
  • Isotype
    IgG
  • Protein IDP00367
  • Protein Name
    Glutamate dehydrogenase 1, mitochondrial
  • Scientific Description
    L-glutamate dehydrogenase (EC 1.4.1.3) has a central role in nitrogen metabolism in plants and animals. Glutamate dehydrogenase is found in all organisms and catalyzes the oxidative deamination of 1-glutamate to 2-oxoglutarate (Smith et al., 2001 [PubMed 11254391]). Glutamate, the main substrate of GLUD, is present in brain in concentrations higher than in other organs. In nervous tissue, GLUD appears to function in both the synthesis and the catabolism of glutamate and perhaps in ammonia detoxification (Mavrothalassitis et al., 1988 [PubMed 3368458]).[supplied by OMIM]
  • Reactivity
    Drosophila, Human, Mouse, Rat
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203

References

  • Geiszler PC, Ugun-Klusek A, Lawler K, et al. Dynamic metabolic patterns tracking neurodegeneration and gliosis following 26S proteasome dysfunction in mouse forebrain neurons. Sci Rep. 2018,8(1):4833. doi: 10.1038/s41598-018-23155-2
    Read this paper
  • Gonzalez SN, Valsecchi WM, Maugeri D, et al. Structure, kinetic characterization and subcellular localization of the two ribulose 5-phosphate epimerase isoenzymes from Trypanosoma cruzi. PLoS One. 2017,12(2):e0172405. doi: 10.1371/journal.pone.0172405
    Read this paper
  • Cho CK, Smith CR, Diamandis EP. Amniotic fluid proteome analysis from Down syndrome pregnancies for biomarker discovery. J Proteome Res. 2010,9(7):3574-82. doi: 10.1021/pr100088k
    Read this paper