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Glutamine synthetase antibody

GTX109121
GeneTex
ApplicationsImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Frozen, ImmunoHistoChemistry Paraffin
Product group Antibodies
TargetGLUL
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Overview

  • Supplier
    GeneTex
  • Product Name
    Glutamine synthetase antibody
  • Delivery Days Customer
    9
  • Application Supplier Note
    WB: 1:5000-1:20000. ICC/IF: 1:100-1:1000. IHC-P: 1:100-1:1000. IHC-Fr: 1:100-1:1000. IP: 1:100-1:500. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
  • Applications
    ImmunoFluorescence, ImmunoPrecipitation, Western Blot, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Frozen, ImmunoHistoChemistry Paraffin
  • Certification
    Research Use Only
  • Clonality
    Polyclonal
  • Concentration
    0.65 mg/ml
  • Conjugate
    Unconjugated
  • Gene ID2752
  • Target name
    GLUL
  • Target description
    glutamate-ammonia ligase
  • Target synonyms
    cell proliferation-inducing protein 59; GLNS; glutamate decarboxylase; glutamine synthase; glutamine synthetase; GS; palmitoyltransferase GLUL; PIG43; PIG59; proliferation-inducing protein 43
  • Host
    Rabbit
  • Isotype
    IgG
  • Protein IDP15104
  • Protein Name
    Glutamine synthetase
  • Scientific Description
    Glutamine is a main source of energy and is involved in cell proliferation, inhibition of apoptosis, and cell signaling (Haberle et al., 2005 [PubMed 16267323]). Fetal glutamine requirements are very high and depend largely on active glutamine synthesis and the release of glutamine into the fetal circulation by the placenta. Glutamine synthetase (EC 6.3.1.2), also called glutamate-ammonia ligase (GLUL), is expressed throughout the body and plays an important role in controlling body pH and in removing ammonia from the circulation. The enzyme clears L-glutamate, the major neurotransmitter in the central nervous system, from neuronal synapses (see references in Clancy et al., 1996 [PubMed 8975719]).[supplied by OMIM]
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203

References

  • Retinal Injury Activates Complement Expression in Mueller Cells Leading to Neuroinflammation and Photoreceptor Cell Death.
    Read more
  • Glutamine synthetase regulates the immune microenvironment and cancer development through the inflammatory pathway.
    Read more
  • Trafficking of the glutamate transporter is impaired in LRRK2-related Parkinsons disease. Iovino L et al., 2022 Jul, Acta Neuropathol
    Read more
  • Liver injury in non-alcoholic fatty liver disease is associated with urea cycle enzyme dysregulation. Gallego-Duran R et al., 2022 Mar 1, Sci Rep
    Read more
  • TRPV4-induced Mueller cell gliosis and TNF-alpha elevation-mediated retinal ganglion cell apoptosis in glaucomatous rats via JAK2/STAT3/NF-kappaB pathway. Li Q et al., 2021 Nov 17, J Neuroinflammation
    Read more
  • Microglia-Derived Small Extracellular Vesicles Reduce Glioma Growth by Modifying Tumor Cell Metabolism and Enhancing Glutamate Clearance through miR-124. Serpe C et al., 2021 Aug 12, Cells
    Read more
  • Hepatoblastoma: glutamine depletion hinders cell viability in the embryonal subtype but high GLUL expression is associated with better overall survival. Schmidt A et al., 2021 Nov, J Cancer Res Clin Oncol
    Read more
  • Patient-Derived Mutant Forms of NFE2L2/NRF2 Drive Aggressive Murine Hepatoblastomas. Wang H et al., 2021, Cell Mol Gastroenterol Hepatol
    Read more
  • Cancer Cachexia Induces Preferential Skeletal Muscle Myosin Loss When Combined With Denervation. Yamada T et al., 2020, Front Physiol
    Read more
  • A spatial similarity of stereochemical environments formed by amino acid residues defines a common epitope of two non-homologous proteins. Nakashima K et al., 2019 Oct 15, Sci Rep
    Read more

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Figure 1. Western blot analysis of GLUL using anti-GLUL antibody (A03191-3). Electrophoresis was performed on a 5-20% SDS-PAGE gel at 70V (Stacking gel) / 90V (Resolving gel) for 2-3 hours. The sample well of each lane was loaded with 30 ug of sample under reducing conditions. Lane 1: human K562 whole cell lysates, Lane 2: rat brain tissue lysates, Lane 3: mouse brain tissue lysates. After electrophoresis, proteins were transferred to a nitrocellulose membrane at 150 mA for 50-90 minutes. Blocked the membrane with 5% non-fat milk/TBS for 1.5 hour at RT. The membrane was incubated with rabbit anti-GLUL antigen affinity purified polyclonal antibody (Catalog # A03191-3) at 0.5 microg/mL overnight at 4°C, then washed with TBS-0.1%Tween 3 times with 5 minutes each and probed with a goat anti-rabbit IgG-HRP secondary antibody at a dilution of 1:5000 for 1.5 hour at RT. The signal is developed using an Enhanced Chemiluminescent detection (ECL) kit (Catalog # EK1002) with Tanon 5200 system. A specific band was detected for GLUL at approximately 42 kDa. The expected band size for GLUL is at 42 kDa.
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