Analytical Data
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Gene name
AQP8
- Application
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O94778
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Expression Region
Lys129~Trp228
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Molecular Weight
44kDa
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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
Aquaporin 8 (AQP8) is a member of the aquaporin family, which are integral membrane proteins that facilitate water and small solute transport across cellular membranes. Research on AQP8 has garnered significant interest due to its unique expression in various tissues such as the liver, kidney, and epithelia of the gastrointestinal tract, indicating its potential role in physiological processes like osmoregulation and cell volume control. Unlike other aquaporins, AQP8 is also permeable to urea, making it crucial for urinary concentration and metabolic activities. Understanding AQP8's structure, function, and regulatory mechanisms could provide insights into its involvement in diseases like nephrogenic diabetes insipidus and other water balance disorders. Furthermore, the development of recombinant AQP8 proteins allows for in-depth studies of its biophysical properties and interactions with other cellular components, thus advancing our understanding of aquaporin biology and its therapeutic implications.
