Recombinant human Glutamine Synthetase protein is a Human Full Length protein, in the 1 to 373 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:16267323, PubMed:30158707, PubMed:36289327). 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 (By similarity). Essential for proliferation of fetal skin fibroblasts (PubMed:18662667). 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 (PubMed:30158707). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (PubMed:30158707). Plays a role in ribosomal 40S subunit biogenesis (PubMed:26711351). 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 (PubMed:36289327).
GLNS, GLUL, Glutamine synthetase, GS, Glutamate--ammonia ligase, Palmitoyltransferase GLUL
Recombinant human Glutamine Synthetase protein is a Human Full Length protein, in the 1 to 373 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF
Purified by conventional chromatography techniques.
Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:16267323, PubMed:30158707, PubMed:36289327). 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 (By similarity). Essential for proliferation of fetal skin fibroblasts (PubMed:18662667). 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 (PubMed:30158707). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (PubMed:30158707). Plays a role in ribosomal 40S subunit biogenesis (PubMed:26711351). 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 (PubMed:36289327).
Belongs to the glutamine synthetase family.
Acetylated by EP300/p300; acetylation is stimulated by increased glutamine levels and promotes ubiquitin-mediated proteasomal degradation.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Glutamine synthetase also known as glutamine s synthetase or glnA is an enzyme that catalyzes the ATP-dependent conversion of glutamate and ammonia into glutamine. This reaction plays an important role in nitrogen metabolism. Glutamine synthetase has a molecular weight of approximately 620 kDa and forms a multimeric structure commonly seen in bacteria plants and animal tissues with significant expression in the brain liver and kidneys.
This enzyme supports the detoxification of ammonia by incorporating it into glutamine an essential amino acid and nitrogen donor. Glutamine synthetase operates independently rather than as part of a larger protein complex. It assists in maintaining cellular nitrogen balance and facilitates the synthesis of proteins and other nitrogen-containing molecules. Glutamine peptides serve vital roles in cellular processes underlining the significance of their synthesis.
Glutamine synthetase integrates into the glutamate and glutamine cycle between neurons and glial cells highlighting its part in neurotransmitter metabolism. It also features prominently in the urea cycle influencing nitrogen disposal in organisms. Glutamine synthetase interacts with glutaminase which assists in transforming glutamine back to glutamate maintaining a balance of nitrogenous compounds within these pathways.
Glutamine synthetase abnormalities link to hepatic encephalopathy and neurodegenerative disorders such as Alzheimer's disease. Altered enzyme expression contributes to increased ammonia levels adversely affecting brain function. In Alzheimer's disease connections with tau and amyloid-beta proteins suggest a link between glutamine synthetase activity and neurotoxic events. Understanding these interactions may offer insights into therapeutic approaches for these conditions.
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Recombinant human Glutamine synthetase (3μg) analysed by 15% SDS-PAGE.
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