Analytical Data
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Gene name
aqpZ
- Application
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Alternative Names
aqpZ；bniP；Aquaporin Z
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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
P60844
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Expression Region
1-231aa
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AA Sequence
MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGGHFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNGYGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPVTNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD
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Molecular Weight
23.7 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
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Protein Description
The study of aquaporin Z (AqpZ) has gained significant attention due to its critical role in cell membrane permeability and water transport in various organisms. AqpZ, a member of the aquaporin family, is primarily found in bacteria and is known for its efficient facilitation of water movement across lipid bilayers. Understanding the structure and function of AqpZ is essential for elucidating the mechanisms of osmoregulation, cellular hydration, and even the development of new biotechnological applications, such as the enhancement of water transport in plants or the design of bio-inspired membranes. The recombinant expression of AqpZ in heterologous systems, such as E. coli, enables researchers to obtain sufficient quantities of pure protein for functional and structural studies. These studies often utilize techniques like X-ray crystallography and nuclear magnetic resonance (NMR) to analyze the molecular dynamics and permeability characteristics of AqpZ. The insights gained from AqpZ research not only deepen our understanding of water channels in prokaryotic organisms but also have broader implications in fields ranging from agriculture to medicine, where the manipulation of water transport could lead to advancements in crop resilience and therapeutic interventions in water balance disorders. Overall, the ongoing research on AqpZ continues to reveal important aspects of cellular physiology and opens up possibilities for innovative applications.
