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AB222354

Recombinant human Glutamine Synthetase protein (Tag Free)

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Recombinant human Glutamine Synthetase protein (Tag Free) is a Human Full Length protein, in the 1 to 373 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, FuncS.

View Alternative Names

GLNS, GLUL, Glutamine synthetase, GS, Glutamate--ammonia ligase, Palmitoyltransferase GLUL

1 Images
SDS-PAGE - Recombinant human Glutamine Synthetase protein (Tag Free) (AB222354)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human Glutamine Synthetase protein (Tag Free) (AB222354)

Recombinant human Glutamine synthetase (3μg) analysed by 15% SDS-PAGE.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific activity is > 2.000 pmol/min/ug, and is defined as the amount of enzyme that convert L-glutamate to L-glutamine per miunte at pH 7.5 at 37C in coupled system with PK/LDH.

Accession

P15104

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN","proteinLength":"Full Length","predictedMolecularWeight":"42 kDa","actualMolecularWeight":null,"aminoAcidEnd":373,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P15104","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

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.
Biological function summary

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.

Pathways

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.

Specifications

Form

Liquid

Additional notes

Purified by conventional chromatography techniques.

General info

Function

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).

Sequence similarities

Belongs to the glutamine synthetase family.

Post-translational modifications

Acetylated by EP300/p300; acetylation is stimulated by increased glutamine levels and promotes ubiquitin-mediated proteasomal degradation.. Palmitoylated; undergoes autopalmitoylation.. Ubiquitinated by ZNRF1 (By similarity). Ubiquitinated by the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex called CRL4(CRBN), leading to proteasomal degradation (PubMed:26990986).

Subcellular localisation

Mitochondrion

Product protocols

Target data

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).
See full target information GLUL

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