Analytical Data
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Gene name
GLS
- Application
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Alternative Names
GLS；GA；Glutaminase liver isoform. mitochondrial
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Species
Human
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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
O94925
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Expression Region
616-669aa
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AA Sequence
KDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL
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Molecular Weight
54.1 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
Related Products
Protein Description
The study of GLS (glutaminase) recombinant proteins has gained significant attention due to their crucial role in cellular metabolism and cancer biology. Glutaminase catalyzes the conversion of glutamine to glutamate, a key process in glutamine metabolism that supports cancer cell growth and proliferation. Abnormal activation of GLS has been implicated in various cancers, making it an attractive target for therapeutic intervention. Researchers have been exploring GLS recombinant proteins to better understand their structural properties, enzymatic mechanisms, and regulatory functions. The recombinant production of GLS allows for the examination of its activity in controlled laboratory settings, facilitating the identification of potential inhibitors that could disrupt its function in tumor cells. Furthermore, advancements in protein engineering and expression systems have enabled improved yields and functionalities of these recombinant proteins. This research is particularly valuable in the context of developing novel cancer treatments that target metabolic pathways, potentially leading to more effective therapies for patients with glutamine-dependent tumors. As the understanding of GLS's role in metabolic reprogramming deepens, studies focusing on GLS recombinant proteins are paving the way for innovative approaches to combat cancer and other diseases associated with dysregulated glutamine metabolism.
