Analytical Data
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Gene name
AQP1
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简介
The AQP1 protein forms water-specific channels that allow water to cross red blood cells and renal proximal tubule membranes. AQP1 Protein, Human (His-SUMO) is the recombinant human-derived AQP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
- Application
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Species
Human
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Source
E. coli
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Tag
N-6*His;N-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P29972
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Expression Region
G220-K269
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Protein Length
Partial
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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
Aquaporin 1 (AQP1) is a water channel protein that facilitates the transport of water across cell membranes, playing a crucial role in cellular osmoregulation and fluid homeostasis. The study of AQP1 has garnered significant interest due to its involvement in various physiological processes, including kidney function, eye health, and brain hydration. Additionally, dysregulation of AQP1 has been linked to several pathophysiological conditions, such as edema, diabetes insipidus, and cancer progression. The recombinant production of AQP1 provides a valuable tool for researchers to explore its structure-function relationship, investigate its role in cellular mechanisms, and develop potential therapeutic applications. Advances in protein expression techniques, particularly in systems like bacteria, yeast, or mammalian cells, have enabled the generation of high yields of functional AQP1. Characterization of the recombinant protein through techniques such as X-ray crystallography and cryo-electron microscopy has further elucidated its structural properties and permeability characteristics. By analyzing AQP1 interactions with various ligands and other proteins, researchers aim to deepen the understanding of its regulatory mechanisms and potential as a drug target. Overall, the study of recombinant AQP1 not only enhances insights into fundamental biological processes but also holds promise for innovative approaches to treat diseases associated with water transport dysregulation.
