Analytical Data
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Gene name
aqpZ
- Application
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Alternative Names
Bacterial nodulin-like intrinsic protein
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P60844
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Expression Region
1-231aa
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Molecular Weight
27.7 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
AqpZ, a member of the aquaporin family, is a channel protein primarily found in bacterial cells that facilitates the transport of water and, in certain cases, small solutes across cellular membranes. The study of AqpZ has gained significant attention due to its crucial role in maintaining osmotic balance and its potential biotechnological applications. Research indicates that AqpZ exhibits remarkable efficiency in water transport, surpassing that of other aquaporins, making it an ideal candidate for studies in membrane biology and bioengineering. Furthermore, understanding its structure and function can provide insights into the evolution of aquaporins and their diverse roles in different organisms. Recombinant expression of AqpZ in various host systems allows for detailed investigations into its properties and potential applications in industries such as food processing, pharmaceuticals, and water purification. By elucidating the mechanistic details of AqpZ, researchers aim to harness its capabilities for innovative solutions in water management and enhance our understanding of cellular osmoregulation.
