Analytical Data
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Gene name
gltI
- Application
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Alternative Names
gltI；ybeJ；yzzK；Glutamate/aspartate import solute-binding Protein
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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
P37902
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Expression Region
23-302aa
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AA Sequence
DDAAPAAGSTLDKIAKNGVIVVGHRESSVPFSYYDNQQKVVGYSQDYSNAIVEAVKKKLNKPDLQVKLIPITSQNRIPLLQNGTFDFECGSTTNNVERQKQAAFSDTIFVVGTRLLTKKGGDIKDFANLKDKAVVVTSGTTSEVLLNKLNEEQKMNMRIISAKDHGDSFRTLESGRAVAFMMDDALLAGERAKAKKPDNWEIVGKPQSQEAYGCMLRKDDPQFKKLMDDTIAQVQTSGEAEKWFDKWFKNPIPPKNLNMNFELSDEMKALFKEPNDKALN
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Molecular Weight
47.2 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 study of the gltI recombinant protein has gained significant attention due to its critical role in the metabolism of glutamate in various organisms. Glutamate is a key amino acid and neurotransmitter, playing vital roles in cellular signaling and metabolic pathways. The gltI gene encodes a specific glutamate transporter, which is responsible for the uptake of glutamate into cells, thereby regulating its concentration in the extracellular environment. Discordant regulation of glutamate is associated with numerous neurological disorders, making the understanding of gltI function vital for therapeutic development. Researchers employ recombinant DNA technology to produce gltI protein, allowing for detailed structural and functional analysis. This enables the study of its transport mechanisms, interaction with ligands, and potential inhibition by therapeutic agents. Furthermore, studying gltI contributes to the broader understanding of glutamate transport systems and their implications in health and disease. As such, the recombinant gltI protein serves as a valuable tool in both basic research and the potential development of pharmaceutical interventions targeting glutamate dysregulation in various clinical settings. This growing body of work highlights the protein's importance in neurobiology and the promise it holds for addressing glutamate-related pathologies.
