Analytical Data
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Gene name
GLUT1
- Application
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Alternative Names
GLUT1
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Species
Human
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Source
Baculovirus
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11166
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Expression Region
M1-V492, N45T, E329Q
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Protein Length
Full Length
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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
GLUT1, or glucose transporter type 1, is a pivotal membrane protein responsible for facilitating the transport of glucose across the plasma membranes of various cells, particularly in the brain and erythrocytes. Its crucial role in maintaining glucose homeostasis underscores its importance in metabolic processes. Mutations and dysregulation of GLUT1 have been implicated in several pathological conditions, such as GLUT1 deficiency syndrome, which leads to neurological disorders due to inadequate glucose supply to the brain. The study of recombinant GLUT1 proteins is essential for understanding its structure-function relationships, interactions with other cellular components, and regulatory mechanisms. Recent advancements in protein engineering and expression systems have enabled researchers to produce large quantities of functional GLUT1 for detailed investigations. Characterizing the protein through techniques such as crystallography, spectroscopy, and site-directed mutagenesis provides insights into its transport mechanism and potential therapeutic targets. As research continues, recombinant GLUT1 proteins not only enhance our comprehension of glucose transport physiology but may also foster the development of novel strategies for treating metabolic disorders.
