Analytical Data
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Gene name
GS
- Application
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Alternative Names
GS；GS27；Golgi SNAP receptor complex member 2
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
W8JWW7
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Expression Region
1-364aa
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AA Sequence
MAGETTKLDLSVKAVGWGAADASGVLQPIKFYRRVPGERDVKIRVLYSGVCNFDMEMVRNKWGFTRYPYVFGHETAGEVVEVGSKVEKFKVGDKVAVGCMVGSCGQCYNCQSGMENYCPEPNMADGSVYREQGERSYGGCSNVMVVDEKFVLRWPENLPQDKGVALLCAGVVVYSPMKHLGLDKPGKHIGVFGLGGLGSVAVKFIKAFGGKATVISTSRRKEKEAIEEHGADAFVVNTDSEQLKALAGTMDGVVDTTPGGRTPMSLMLNLLKFDGAVMLVGAPESLFELPAAPLIMGRKKIIGSSTGGLKEYQEMLDFAAKHNIVCDTEVIGIDYLSTAMERIKNLDVKYRFAIDIGNTLKFEE
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Molecular Weight
39.5 kDa
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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
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Protein Description
The research on GS (glutamine synthetase) recombinant proteins has gained significant attention in the fields of biochemistry and molecular biology due to their critical role in nitrogen metabolism and cellular homeostasis. GS catalyzes the conversion of glutamate and ammonia into glutamine, a vital amino acid that serves as a nitrogen donor in various biosynthetic pathways. Dysregulation of GS activity has been implicated in several pathological conditions, including neurodegenerative diseases, metabolic disorders, and certain types of cancer. The ability to produce recombinant GS proteins allows for detailed studies into their structure, function, and regulatory mechanisms. Advances in recombinant DNA technology and protein expression systems have enabled researchers to generate large quantities of these proteins for biochemical assays, structural analysis, and potential therapeutic applications. Additionally, the characterization of GS isoforms from different species enhances our understanding of evolutionary adaptations in nitrogen metabolism. By elucidating the intricacies of GS function and regulation, researchers aim to develop targeted interventions that can modulate its activity in disease contexts, paving the way for novel treatment strategies. Overall, the study of GS recombinant proteins not only deepens our comprehension of fundamental biological processes but also holds promise for innovative medical advancements.
