Analytical Data
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Gene name
Glutamine synthetase/GLUL
- Application
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Alternative Names
GLNS; GLUL; Glutamate-Ammonia Ligase; Glutamate decarboxylase
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P15105
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Expression Region
Met1~Asn373
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Molecular Weight
44kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Glutamine synthetase (GS), encoded by the GLUL gene, plays a crucial role in nitrogen metabolism and neurotransmitter regulation in both prokaryotic and eukaryotic organisms. This enzyme catalyzes the ATP-dependent conversion of glutamate and ammonia into glutamine, which is essential for synthesizing proteins, nucleotides, and other biomolecules. Dysregulation of glutamine levels has been implicated in various pathological conditions, including neurodegenerative diseases, metabolic disorders, and certain cancers. The study of recombinant glutamine synthetase has gained prominence due to its potential applications in biochemistry and medicine. Researchers have focused on producing recombinant GS to investigate its structural properties, enzymatic mechanisms, and regulatory pathways. Additionally, recombinant GS can be utilized as a tool in metabolic engineering, aiding in the development of microbial strains with enhanced nitrogen assimilation capabilities. Understanding the function and regulation of glutamine synthetase through recombinant protein studies provides valuable insights into nutrient metabolism and opens avenues for therapeutic interventions in diseases linked to metabolic dysregulation.
