R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Glutaminase-1/GLS1 (E4T9Q) Rabbit mAb #49363
Filter:
- WB
- IP
- IF
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 55-65 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Immunofluorescence (Immunocytochemistry) | 1:200 - 1:800 |
| Flow Cytometry (Fixed/Permeabilized) | 1:200 - 1:800 |
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.
For a carrier free (BSA and azide free) version of this product see product #84021.
For a carrier free (BSA and azide free) version of this product see product #84021.
Protocol
Specificity / Sensitivity
Glutaminase-1/GLS1 (E4T9Q) Rabbit mAb recognizes endogenous levels of total glutaminase-1/GLS1 protein. This antibody does not cross-react with glutaminase-2/GLS2 protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly116 of human glutaminase-1/GLS1 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, KEAP1–NRF2-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).
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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