Analytical Data
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Gene name
EAAT3
- Application
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Alternative Names
SLC1A1; EAAC1; Solute Carrier 1 Member 1; Sodium-dependent glutamate/aspartate transporter 3; Excitatory amino-acid carrier 1; Neuronal and epithelial glutamate transporter
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Species
Human
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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
P43005
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Expression Region
Ser115~Gly209
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Molecular Weight
14kDa
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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
EAAT3 (Excitatory Amino Acid Transporter 3) is a crucial member of the glutamate transporter family, responsible for the uptake of glutamate in the central nervous system, thus playing a vital role in regulating synaptic transmission and maintaining excitatory neurotransmission homeostasis. Dysregulation of EAAT3 has been implicated in various neurological disorders, including epilepsy, schizophrenia, and neurodegenerative diseases like Alzheimer's and Parkinson's. As a result, understanding the structure and function of EAAT3 through recombinant protein studies has become increasingly important. Recombinant EAAT3 can provide valuable insights into its transport mechanism and interaction with glutamate, offering potential therapeutic targets for restoring glutamate balance in pathological conditions. Furthermore, studying EAAT3's structure-function relationships through crystallography and electrophysiological assays can elucidate how mutations or alterations in its activity contribute to neuronal dysfunction. Thus, research on EAAT3 recombinant proteins not only enhances our fundamental understanding of excitatory amino acid transporters but also opens avenues for developing novel strategies to treat glutamate-related neuropsychiatric conditions.
