Analytical Data
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Gene name
AQP11
- Application
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Alternative Names
AQP11；AQPX1；Aquaporin-11
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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
Q8NBQ7
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Expression Region
1-271aa
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AA Sequence
MSPLLGLRSELQDTCTSLGLMLSVVLLMGLARVVARQQLHRPVAHAFVLEFLATFQLCCCTHELQLLSEQHPAHPTWTLTLVYFFSLVHGLTLVGTSSNPCGVMMQMMLGGMSPETGAVRLLAQLVSALCSRYCTSALWSLGLTQYHVSERSFACKNPIRVDLLKAVITEAVCSFLFHSALLHFQEVRTKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFMCFDEAFPQFFIVYWLAPSLGILLMILMFSFFLPWLHNNHTINKKE
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Molecular Weight
30.2 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
AQP11 (Aquaporin 11) is a member of the aquaporin family of water channel proteins, known for facilitating the transport of water and small solutes across cell membranes. Its unique expression in various tissues, particularly in the kidney, brain, and reproductive organs, highlights its potential role in physiological processes such as urine concentration, fluid balance, and cellular homeostasis. Recent studies have identified mutations in the AQP11 gene that are associated with specific genetic disorders, including nephropathic cystinosis and other kidney-related conditions. Such findings underline the importance of understanding AQP11's structure and function at the molecular level. Research involving recombinant AQP11 protein has played a crucial role in elucidating its biochemical properties, membrane integration mechanisms, and regulatory pathways. By expressing AQP11 in heterologous systems, scientists can investigate its role in water transport and permeability and develop therapeutic strategies aimed at rectifying the dysfunction linked to its abnormalities. Understanding the functional dynamics of AQP11 is essential not only for clarifying its physiological significance but also for exploring its potential as a pharmacological target in the treatment of related pathologies. Thus, the study of recombinant AQP11 protein continues to gain importance in both basic and applied biomedical research, fostering advancements in the field of aquaporin biology and its implications for human health.
