Render Target: SSR
Render Timestamp: 2024-12-19T21:16:01.835Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:58:53.734
Product last modified at: 2024-12-17T19:02:50.622Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Glutaminase-2/GLS2 (E9C7V) Rabbit mAb #85934

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 60
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Glutaminase-2/GLS2 (E9C7V) Rabbit mAb recognizes endogenous levels of total glutaminase-2/GLS2 protein. This antibody does not cross-react with glutaminase-1/GLS1 protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human glutaminase-2/GLS2 protein.

    Background

    Glutaminase catalyzes the conversion of glutamine to glutamate, the first and rate-limiting step of glutaminolysis (1). Both kidney-type glutaminase (GLS1) and liver-type glutaminase (GLS2) are found in mammals (2). GLS1-mediated glutathione synthesis plays an essential role in redox homeostasis and contributes to increased survival of postimplantation bone cells preconditioned to the hypoxic and ischemic environment in the bone defect site (3). In addition, KEAP1NRF2-mutant LUAD (KRAS-mutant lung adenocarcinoma) tumors are dependent on increased glutaminolysis (1). Furthermore, recent studies showed higher glutaminolysis and glucose production from glutamine in human primary hepatocytes with GLS2 gain-of-function missense mutations (4). These findings suggest GLS1 and GLS2 as potential targets in the therapy of bone regeneration and in the treatments of diseases such as cancer and hyperglycemia, respectively (1,3,4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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