Glutamine Synthetase Antibody (YA751)
(Synonyms: GLNS, GLUL, Glutamine synthetase, GS, Glutamate--ammonia ligase, Palmitoyltransferase GLUL)Based on 1 Customer Validation
Glutamine Synthetase Antibody (YA751) is a Mouse-derived and non-conjugated IgG2a monoclonal antibody, targeting to Glutamine Synthetase.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, IHC-P, FC
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Reactivity :
Human, Mouse
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Formulation:
Supplied in 1*TBS (pH7.4), 0.2% BSA and 50% Glycerol. Preservative: 0.05% Sodium Azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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FC
FC: Flow Cytometry
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|---|---|---|---|
| Dilution Ratio | 1:500-1:2000 | 1:50-1:200 | 1:50-1:100 |
Product Details
Glutamine Synthetase Antibody (YA751) is a Mouse-derived and non-conjugated IgG2a monoclonal antibody, targeting to Glutamine Synthetase.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse
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Observed Molecular WeightObserved band size: 42 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 42 kDa
Synthetic peptide corresponding to Human Glutamine synthetase.AA range:190-373.
Endogenous
Protein G affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 1*TBS (pH7.4), 0.2% BSA and 50% Glycerol. Preservative: 0.05% Sodium Azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Verification Images
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Western blot analysis was performed on protein extracts (25 μg) from MCF-7 (lane 2), HeLa (lane 3), and 293T (lane 4) using Glutamine Synthetase antibody. Proteins were transferred onto a 0.45 μm PVDF membrane using the Trans-Blot® Turbo™ system for 13 min. The membrane was then blocked with 5% nonfat milk in TBST (HY-K1025) for 1 h at room temperature. The primary antibody (1:1000) and loading control antibody GAPDH Antibody (HRP) (HY-P80954A) (1:5000) were diluted in 5% nonfat milk in TBST and incubated with the membrane overnight at 4°C. After washing, the membrane of primary antibody was incubated with HRP-conjugated goat anti-rabbit/mouse IgG secondary antibody (HY-P8001/HY-P8004) (1:5000) diluted in 5% nonfat milk in TBST for 1 h at room temperature. Protein bands were visualized using an Ultra High Sensitivity ECL detection kit (HY-K1005).
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Western blot analysis of extracts from MCF-7(lane 2(20μg), K562(lane 3(20μg), Jurkat(lane 4(20μg) and HEK293(lane 5(20μg) ) using Glutamine Synthetase (HY-P80408) Mouse mAb. Proteins were transferred to a PVDF membrane and blocked with 5% BSA in TBST for 2 hour at room temperature. The primary antibody (HY-P80408, 1/1000) and Loading control antibody (GAPDH, HY-P80954, 1/3000) was used in 5% BSA in TBST at 4°C overnight. Goat Anti-Mouse IgG-HRP Secondary Antibody (HY-P8004, 1/10,000) was used for 1 hour at room temperature.
Background
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Function
Glutamine Synthetase is a Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia. Plays a key role in ammonium detoxification during erythropoiesis: the glutamine synthetase activity is required to remove ammonium generated by porphobilinogen deaminase (HMBS) during heme biosynthesis to prevent ammonium accumulation and oxidative stress. Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ. Plays a role in ribosomal 40S subunit biogenesis. Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2[1][2][3][4][5].
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Subcellular Localization
Cytoplasm, cytosol; Microsome; Mitochondrion; Cell membrane; Lipid-anchor
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Expression
Tissue_specificity:Expression in endothelial cells
Induction:By glucocorticoids. Vitamin D and the Wnt signaling pathway inhibit its expression and activity (PubMed:18555765) . Glutamine synthase (GS) levels are regulated by a negative feedback mechanism where elevated glutamine levels stimulate GS ubiquitin-mediated proteasomal degradation (PubMed:26990986, PubMed:38579670) -
Subunit
Decamer; composed of two pentamers (PubMed:18005987). Interacts with PALMD (By similarity). Interacts with RHOJ (PubMed:30158707). Interacts with BEST2; this interaction tethers a fraction of GLUL to the membrane, causing a decrease of cytosolic glutamine synthase (GS) activity and inhibits the chloride channel activity of BEST2 by affecting the gating at the aperture in the absence of intracellular glutamate (PubMed:36289327)
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SwissProt ID
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Synonyms
GLNS, GLUL, Glutamine synthetase, GS, Glutamate--ammonia ligase, Palmitoyltransferase GLUL
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Research Field
Neuroscience
Documentation
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Data Sheet (262 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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User Guide for Antibodies (1077 KB)
[1]. Häberle J, et al. Congenital glutamine deficiency with glutamine synthetase mutations. N Engl J Med. 2005 Nov 3;353(18):1926-33. [Content Brief]
[2]. Eelen G, et al. Role of glutamine synthetase in angiogenesis beyond glutamine synthesis. Nature. 2018 Sep;561(7721):63-69. [Content Brief]
[3]. Owji AP, et al. Bestrophin-2 and glutamine synthetase form a complex for glutamate release. Nature. 2022 Nov;611(7934):180-187. [Content Brief]
[4]. Vermeulen T, et al. Glutamine synthetase is essential for proliferation of fetal skin fibroblasts. Arch Biochem Biophys. 2008 Oct 1;478(1):96-102. [Content Brief]
[5]. Badertscher L, et al. Genome-wide RNAi Screening Identifies Protein Modules Required for 40S Subunit Synthesis in Human Cells. Cell Rep. 2015 Dec 29;13(12):2879-91. [Content Brief]